Information on EC 3.1.1.74 - cutinase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.1.1.74
-
RECOMMENDED NAME
GeneOntology No.
cutinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cutin + H2O = cutin monomers
show the reaction diagram
Cutin, a polymeric structural component of plant cuticles, is a hydroxy fatty acid polymer, usually C16 or C18 and that contains one to three hydroxyl groups. The enzyme from several fungal sources also hydrolyses the p-nitrophenyl esters of hexadecanoic acid. It is however inactive towards several esters that are substrates for non-specific esterases.
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylic ester hydrolysis
-
-
-
-
carboxylic ester hydrolysis
A8QPD8
-
hydrolysis
-
-
SYSTEMATIC NAME
IUBMB Comments
cutin hydrolase
Cutin, a polymeric structural component of plant cuticles, is a polymer of hydroxy fatty acids that are usually C16 or C18 and contain up to three hydroxy groups. The enzyme from several fungal sources also hydrolyses the p-nitrophenyl esters of hexadecanoic acid. It is however inactive towards several esters that are substrates for non-specific esterases.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acidic cutinase
-
-
acidic cutinase
-
-
-
acidic cutinase
S4VCH4
-
acidic cutinase
Sirococcus conigenus VTT D-04989
S4VCH4
-
-
CcCUT1
B9U443
-
CDEF1
-
-
CDEF1
Q9SZW7
-
CLE
Q874E9
-
Cut1
Q00298
-
Cut1
P00590
-
Cut1
P30272
-
Cut1
Thermobifida cellulosilytica DSM44535
-
-
-
Cut1
G8GER6
-
Cut1
G8GER6
gene name
Cut1
Thermobifida fusca DSM 44342, Thermobifida fusca DSM44342
-
-
-
Cut1
Thermobifida fusca NRRL B-8184
G8GER6
gene name
-
Cut2
Thermobifida cellulosilytica DSM44535
-
-
-
Cut2
Q6A0I4
gene name
Cut2
Thermobifida fusca NRRL B-8184
Q6A0I4
gene name
-
cuticle destructing factor 1
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-
cuticle destructing factor 1
Q9SZW7
-
cutin esterase
-
-
-
-
cutinase
P41744
-
cutinase
-
-
cutinase
Q9SZW7
-
cutinase
-
-
cutinase
B9U443
-
cutinase
-
-
cutinase
P00590
-
cutinase
P11373
-
cutinase
-
-
cutinase
Magnaporthe grisea, Neurospora crassa, no activity in Saccharomycotina
-
-
cutinase
-
-
cutinase
-
-
cutinase
A8QPD8
-
cutinase 1
P52956
-
cutinase 1
Fusarium roseum
-
-
cutinase 1
Fusarium solani pisi
P00590
-
cutinase 1
E9LVH7
-
cutinase 1
E9LVH8
-
cutinase 2
Q5AVY9
-
cutinase 2
E9LVH9
-
cutinase-1
P00590
-
cutinase-like enzyme
Q874E9
-
cutinolytic polyesterase
B9U443
-
fungal cutinase
-
-
Tfu_0883
-
-
Thcut1
A8QPD8
-
THCUT1 protein
A8QPD8
-
Thc_Cut1
Thermobifida cellulosilytica DSM 44535
E9LVH8
-
-
Thc_Cut2
Thermobifida cellulosilytica DSM 44535
E9LVH9
-
-
LC-cutinase
-
-
additional information
-
the cutinase is an esterase that belongs to the alpha/beta hydrolases family
CAS REGISTRY NUMBER
COMMENTARY
51377-41-4
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene cut1, the organism harbors four cutinases
-
-
Manually annotated by BRENDA team
Cut2; isozyme Cut2, the organism harbors four cutinases
UniProt
Manually annotated by BRENDA team
strain 15; strain 20; strain 211; strain 35; strain CECT
-
-
Manually annotated by BRENDA team
Aspergillus nidulans 15
strain 15
-
-
Manually annotated by BRENDA team
Aspergillus nidulans 20
strain 20
-
-
Manually annotated by BRENDA team
Aspergillus nidulans 211
strain 211
-
-
Manually annotated by BRENDA team
Aspergillus nidulans 35
strain 35
-
-
Manually annotated by BRENDA team
Aspergillus nidulans CECT
strain CECT
-
-
Manually annotated by BRENDA team
gene An09g00790, the organism harbors five cutinases
-
-
Manually annotated by BRENDA team
gene anig5
-
-
Manually annotated by BRENDA team
Cut1; gene cut1, the organism harbors two cutinases
UniProt
Manually annotated by BRENDA team
Cut1; gene cutA, the organism harbors one cutinase
UniProt
Manually annotated by BRENDA team
Pser.: Fr.
-
-
Manually annotated by BRENDA team
Botrytis cinerea Pser.: Fr.
Pser.: Fr.
-
-
Manually annotated by BRENDA team
Burkholderia cepacia NRRL B 2320
-
-
-
Manually annotated by BRENDA team
the organism harbors one cutinase
-
-
Manually annotated by BRENDA team
Coprinopsis cinerea C29-2
-
-
-
Manually annotated by BRENDA team
cutinase-like enzyme
UniProt
Manually annotated by BRENDA team
gladioli; lini; lycopersici; lycopersici 2
-
-
Manually annotated by BRENDA team
sp. pisi
-
-
Manually annotated by BRENDA team
the organism harbors one cutinase
-
-
Manually annotated by BRENDA team
Fusarium roseum
culmorum
-
-
Manually annotated by BRENDA team
Fusarium roseum
var. culmorum; var. sambucinum
-
-
Manually annotated by BRENDA team
cutinase I and cutinase II; pisi
-
-
Manually annotated by BRENDA team
pisi
SwissProt
Manually annotated by BRENDA team
pisi 4
SwissProt
Manually annotated by BRENDA team
recombinantly expressed in Escherichia coli
SwissProt
Manually annotated by BRENDA team
recombinantly expressed in in Escherichia coli WK-6
-
-
Manually annotated by BRENDA team
Fusarium solani pisi
Cut1; gene cut1, the organism harbors two cutinases
UniProt
Manually annotated by BRENDA team
Helminthosporium sativum
-
-
-
Manually annotated by BRENDA team
gene hic
-
-
Manually annotated by BRENDA team
native enzyme and mutant myHiC with increased activity and decreased surfactanct sensitivity
-
-
Manually annotated by BRENDA team
recombinantly expressed in Aspergillus oryzae
-
-
Manually annotated by BRENDA team
Humilica insolens
-
-
-
Manually annotated by BRENDA team
Cut1; gene cut1, the organism harbors five cutinases
UniProt
Manually annotated by BRENDA team
(Wint.) Honey
-
-
Manually annotated by BRENDA team
enzyme precursor
SwissProt
Manually annotated by BRENDA team
gene cut1, the organism harbors four cutinases
UniProt
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
expression in Saccharomyces cerevisiae
-
-
Manually annotated by BRENDA team
no activity in Saccharomycotina
-
-
-
Manually annotated by BRENDA team
the organism harbors one cutinase
-
-
Manually annotated by BRENDA team
gene PANT_9c00247; gene PANT_9c00247
UniProt
Manually annotated by BRENDA team
Cut1; gene cut1, the organism harbors one cutinase
UniProt
Manually annotated by BRENDA team
gene ScCut1
UniProt
Manually annotated by BRENDA team
Sirococcus conigenus VTT D-04989
gene ScCut1
UniProt
Manually annotated by BRENDA team
Cut1; gene cut1, the organism harbors two cutinases
UniProt
Manually annotated by BRENDA team
Cut1; gene cut1, the organsim harbors two cutinases
UniProt
Manually annotated by BRENDA team
Cut2; gene cut2, the organism harbors two cutinases
UniProt
Manually annotated by BRENDA team
Thc_Cut1 and Thc_Cut2
-
-
Manually annotated by BRENDA team
Thermobifida cellulosilytica DSM 44535
Cut1
UniProt
Manually annotated by BRENDA team
Thermobifida cellulosilytica DSM 44535
Cut2
UniProt
Manually annotated by BRENDA team
Thermobifida cellulosilytica DSM44535
Thc_Cut1 and Thc_Cut2
-
-
Manually annotated by BRENDA team
ATCC 27730
-
-
Manually annotated by BRENDA team
Thf42_Cut1
-
-
Manually annotated by BRENDA team
two isozymes Tfu 0882 and Tfu 0883
-
-
Manually annotated by BRENDA team
Thermobifida fusca DSM 44342
Cut1
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-
Manually annotated by BRENDA team
Thermobifida fusca DSM44342
Thf42_Cut1
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-
Manually annotated by BRENDA team
Thermobifida fusca NRRL B-8184
gene Cut1
UniProt
Manually annotated by BRENDA team
Thermobifida fusca NRRL B-8184
gene cut2
UniProt
Manually annotated by BRENDA team
metagenome-derived LC-cutinase
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters
evolution
Fusarium solani pisi
P00590
cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters
evolution
-
cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters
evolution
Q5AVY9
cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters
evolution
Q2VF46
cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters
evolution
Q9Y7G8
cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters
evolution
Q00298
cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters
evolution
P30272
cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters
evolution
P52956
cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters
evolution
M9M134
cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters
evolution
-
cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters
evolution
-
cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters
evolution
Q874E9
cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters
evolution
E9LVH7
cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters. The cutinase from Thermobifida alba also adopts an alpha/beta fold, but it is larger than the ones from other family members. It contains nine sheets at the heart of the protein, two of which are antiparallel, rather than the five parallel sheets present in the fungal enzymes
evolution
E9LVH8, E9LVH9
modeling and comparison of the structures of the two closely related cutinases Thc_Cut1 and Thc_Cut2 from Thermobifida cellulosilytica DSM44535 reveal that dissimilarities in their electrostatic and hydrophobic surface properties in the vicinity to the active site might be responsible for pronounced differences in hydrolysis efficiencies of polyester (i.e., PET, polyethyleneterephthalate), isozyme Thc_Cut2 hydrolyzes PET much less efficiently than Thc_Cut1
evolution
E9LVH8, E9LVH9
modeling and comparison of the structures of the two closely related cutinases Thc_Cut1 and Thc_Cut2 from Thermobifida cellulosilytica DSM44535 reveal that dissimilarities in their electrostatic and hydrophobic surface properties in the vicinity to the active site might be responsible for pronounced differences in hydrolysis efficiencies of polyester (i.e., PET, polyethyleneterephthalate), Thc_Cut2 hydrolyzes PET much less efficiently than Thc_Cut1
evolution
-
residues N168, Q170 an N171 of Glomerella cingulata are highly conserved with all cutinases of fungal phytopathogens
evolution
S4VCH4
the enzyme contains the conserved motif G-Y-S-Q-G surrounding the active site serine as well as the aspartic acid and histidine residues of the cutinase active site
evolution
Thermobifida fusca DSM 44342
-
cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters
-
evolution
Sirococcus conigenus VTT D-04989
-
the enzyme contains the conserved motif G-Y-S-Q-G surrounding the active site serine as well as the aspartic acid and histidine residues of the cutinase active site
-
evolution
Thermobifida cellulosilytica DSM 44535
-
modeling and comparison of the structures of the two closely related cutinases Thc_Cut1 and Thc_Cut2 from Thermobifida cellulosilytica DSM44535 reveal that dissimilarities in their electrostatic and hydrophobic surface properties in the vicinity to the active site might be responsible for pronounced differences in hydrolysis efficiencies of polyester (i.e., PET, polyethyleneterephthalate), isozyme Thc_Cut2 hydrolyzes PET much less efficiently than Thc_Cut1, modeling and comparison of the structures of the two closely related cutinases Thc_Cut1 and Thc_Cut2 from Thermobifida cellulosilytica DSM44535 reveal that dissimilarities in their electrostatic and hydrophobic surface properties in the vicinity to the active site might be responsible for pronounced differences in hydrolysis efficiencies of polyester (i.e., PET, polyethyleneterephthalate), Thc_Cut2 hydrolyzes PET much less efficiently than Thc_Cut1
-
malfunction
-
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
Fusarium solani pisi
P00590
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
-
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
Q5AVY9
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
Q2VF46
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
Q9Y7G8
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
Q00298
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
P30272
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
P52956
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
M9M134
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
physiological function
Q9SZW7
CDEF1 is a plant cutinase, recombinant CDEF1 protein has esterase activity. Ectopic expression of CDEF1 driven by the 35S promoter causes fusion of organs, including leaves, stems and flowers, and increased surface permeability. CDEF1 is involved in the penetration of the stigma by pollen tubes. CDEF1 degrades cell wall components to facilitate the emergence of the lateral roots
physiological function
-
contains four cutinase genes, which may result from its low repetitive content and mild form of repeat induced point mutation
physiological function
-
contains three cutinases, which show less than 80% sequence identity, indicating that they are duplicated and diverged before the emergence of the active repeat induced point mutation defence mechanism, and have been retained in the genome by virtue of their varying regulatory or functional diversity
physiological function
-
cutinases are hydrolytic enzymes that share properties of lipases and esterases, and also display the unique characteristic of being active regardless of the presence of an interface
physiological function
-
cutinases are hydrolytic enzymes that share properties of lipases and esterases, they are active regardless of the presence of an interface
physiological function
-
ectopic expression of CDEF1 driven by the 35S promoter causes fusion of organs, including leaves, stems and flowers, and increased surface permeability
physiological function
-
the organism contains 11 cutinases, despite the 3-4% repetitive DNA content and the repeat induced point mutation-based elimination of transposable elements
physiological function
-
the organism contains 12 cutinases. High number of cutinases likely reflects its needs during post-invasion necrotrophic growth and overwintering as saprotrophic mycelia, and its ability to infect many different monocotyledonous genera asymptomatically
physiological function
-
the organism contains 17 cutinases. Preservation of a large number of diverse cutinases within the genome may provide the fungus with a great selective advantage to breach multiple, diverse grass cuticles, or may reflect its requirements to degrade different plant debris while overwintering as a soil saprotroph
physiological function
-
role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase
physiological function
Fusarium solani pisi
P00590
role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase
physiological function
-
role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase
physiological function
Q5AVY9
role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase
physiological function
Q2VF46
role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase
physiological function
Q9Y7G8
role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase
physiological function
Q00298
role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase
physiological function
P30272
role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase
physiological function
P52956
role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase
physiological function
M9M134
role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase
physiological function
Humilica insolens
-
role of cutinase in the infection of plants by fungi. Fungal spores landing on the plant cuticle respond to cutin monomers by expressing cutinase
physiological function
A7EQQ8
the enzyme is an elicitor that triggers defense responses in plants, recombinant His-tagged enzyme causes cell death in Arabidopsis thaliana, Glycine max, Brassica napus, Oryza sativa, Zea mays, and Triticum aestivum, indicating that both dicot and monocot species are responsive to the elicitor. The elicitation of Nicotiana tabacum is effective in the induction of the activities of hydrogen peroxide, phenylalanine ammonia-lyase, peroxides, and polyphenol oxidase. Phenotypes, detailed overview
malfunction
Humilica insolens
-
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
additional information
-
biophysical parameters of cutinase as a function of pH, overview
additional information
-
enzyme homology modeling
additional information
A7EQQ8
residues Ser117, Asp169, and His182 form the active site
additional information
-
residues Ser165, Asp210, and His242 form the catalytic triad. The disulfide bond formed by Cys275 and Cys292 contributes not only to the thermodynamic stability but also to the kinetic stability of LC-cutinase
additional information
-
structure analysis, structure comparisons of isozymes Cut1 and Cut2 during denaturation and unfolding, homology modeling, overview
additional information
Fusarium solani pisi
P00590
structure-activity relationship analysis, active site structure, the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent, the catalytic triad, formed by S120, H188, D175, and key residues in the oxyanion hole, S42 and Q121, are important for stabilizing the transitions states in the acylation/deacylation steps of the enzyme mechanism
additional information
-
the enzyme has a Ser130-His208-Asp176 catalytic triad in which Ser130 is critical to the hydrolytic activity
additional information
Q5AVY9
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
Q9Y7G8
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
Q00298
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
P30272
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
M9M134
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
-
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
-
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
P52956
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent, the catalytic triad, formed by S126, H194, and D181, and key residues in the oxyanion hole, S48 and Q127
additional information
E9LVH7
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent, the catalytic triad, formed by S169, H247, and D215, and key residues in the oxyanion hole, M179 and Y99, active site structure, overview
additional information
Q874E9
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent, the catalytic triad, formed by S85, H180, and D165, and key residues in the oxyanion hole, T17 and Q86
additional information
Q2VF46
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Residues S103 and H173 from Monilinia fructicola cutinase play important roles in catalysis
additional information
-
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. The conformation of the Glomerella cingulata catalytic triad appears to cycle between an inactive form and an active form during catalysis. In the uninhibited structure, the histidine residue that forms the center of the catalytic triad is positioned outside of the active site, and does not interact with the remainder of the triad, catalytic serine and catalytic aspartate. In addition, there is a small helix in the vicinity of the active site that places the catalytic serine in a deep hole in a deep pocketwithin the active site
additional information
Thermobifida fusca DSM 44342
-
the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
-
additional information
-
enzyme homology modeling
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,4-butanediol + adipic acid
?
show the reaction diagram
-
polycondensation reaction, degree of polymerization is 13
-
-
?
1,4-cyclohexanedimethanol + adipic acid
?
show the reaction diagram
-
polycondensation reaction, degree of polymerization is 16
-
-
?
1,4-cyclohexanedimethanol + sebacic acid
?
show the reaction diagram
-
polycondensation reaction, degree of polymerization is 61
-
-
?
1,4-cyclohexanedimethanol + suberic acid
?
show the reaction diagram
-
polycondensation reaction, degree of polymerization is 18
-
-
?
1,4-cyclohexanedimethanol + succinic acid
?
show the reaction diagram
-
polycondensation reaction, degree of polymerization is 4
-
-
?
1,8-octanediol + adipic acid
?
show the reaction diagram
-
polycondensation reaction, degree of polymerization is 47
-
-
?
2-hydroxyethyl benzoate + H2O
ethane-1,2-diol + benzoate
show the reaction diagram
-
is hydrolyzed after 24 h of incubation of bisbenzoyloxyethyl terephthalate
-
-
?
4-nitrophenyl (16-methyl sulfone ester) hexadecanoate + H2O
?
show the reaction diagram
G8GER6, Q6A0I4
-
-
-
?
4-nitrophenyl (16-methyl sulfonyl ester) hexadecanoate + H2O
4-nitrophenol + (16-methyl sulfonyl ester) hexadecanoate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl (16-methyl sulfonyl ester) hexadecanoate + H2O
4-nitrophenol + 16-(methylsulfonyl)hexadecanoate
show the reaction diagram
G8GER6, Q6A0I4
-
-
-
?
4-nitrophenyl acetate
4-nitrophenol + acetate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
A8QPD8
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
Fusarium solani pisi
P00590
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
P52956
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
E9LVH7
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
E9LVH8, E9LVH9
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
E9LVH8, E9LVH9
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
-
low activity
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
G8GER6, Q6A0I4
high activity
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
S4VCH4
high activity
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
Thermobifida fusca DSM44342
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
Thermobifida fusca DSM 44342
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
Sirococcus conigenus VTT D-04989
S4VCH4
high activity
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
Thermobifida cellulosilytica DSM44535
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
Thermobifida fusca NRRL B-8184
G8GER6, Q6A0I4
high activity
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
Thermobifida cellulosilytica DSM 44535
E9LVH8, E9LVH9
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl butyrate
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
-
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
-
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
-
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
-
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
A8QPD8
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
Q9SZW7
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
P41744
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
A6N6J6
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
S4VCH4
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
Fusarium solani pisi
P00590
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
Q5AVY9
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
Q2VF46
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
P52956
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
E9LVH8, E9LVH9
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
low activity
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
best 4-nitrophenyl ester substrate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
G8GER6, Q6A0I4
best 4-nitrophenyl ester substrate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
A6N6J6
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
Burkholderia cepacia NRRL B 2320
-
best 4-nitrophenyl ester substrate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
Thermobifida fusca DSM44342
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
Thermobifida fusca DSM 44342
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
Sirococcus conigenus VTT D-04989
S4VCH4
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
Thermobifida cellulosilytica DSM44535
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
Thermobifida fusca NRRL B-8184
G8GER6, Q6A0I4
best 4-nitrophenyl ester substrate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
Thermobifida cellulosilytica DSM 44535
E9LVH8, E9LVH9
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
show the reaction diagram
-
high activity
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
show the reaction diagram
Burkholderia cepacia NRRL B 2320
-
-
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
show the reaction diagram
G8GER6, Q6A0I4
-
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
show the reaction diagram
Thermobifida fusca NRRL B-8184
G8GER6, Q6A0I4
-
-
-
?
4-nitrophenyl dodecanoate + H2O
4-nitrophenol + dodecanoate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl dodecanoate + H2O
4-nitrophenol + dodecanoate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl hexanoate
4-nitrophenol + hexanoate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
show the reaction diagram
S4VCH4
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
show the reaction diagram
Fusarium solani pisi
P00590
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
show the reaction diagram
P52956
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
show the reaction diagram
Sirococcus conigenus VTT D-04989
S4VCH4
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
show the reaction diagram
G8GER6, Q6A0I4
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
show the reaction diagram
-
low activity
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
show the reaction diagram
G8GER6, Q6A0I4
low activity
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
show the reaction diagram
-
high activity
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
show the reaction diagram
G8GER6, Q6A0I4
low activity
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
show the reaction diagram
-
high activity
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
show the reaction diagram
G8GER6, Q6A0I4
-
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
show the reaction diagram
Thermobifida fusca NRRL B-8184
G8GER6, Q6A0I4
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
show the reaction diagram
A8QPD8
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
show the reaction diagram
P41744
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
show the reaction diagram
Q874E9
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
show the reaction diagram
-
low activity
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
show the reaction diagram
-
low activity
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
show the reaction diagram
G8GER6, Q6A0I4
low activity
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
show the reaction diagram
Burkholderia cepacia NRRL B 2320
-
low activity
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
show the reaction diagram
Coprinopsis cinerea C29-2
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
show the reaction diagram
Sirococcus conigenus, Sirococcus conigenus VTT D-04989
S4VCH4
high activity
-
-
?
4-nitrophenyl valerate
4-nitrophenol + pentanoate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
show the reaction diagram
G8GER6, Q6A0I4
-
-
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
show the reaction diagram
S4VCH4
-
-
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
show the reaction diagram
Fusarium solani pisi
P00590
-
-
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
show the reaction diagram
P52956
-
-
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
show the reaction diagram
Burkholderia cepacia NRRL B 2320
-
-
-
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
show the reaction diagram
Thermobifida fusca NRRL B-8184
G8GER6, Q6A0I4
-
-
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + pentanoate
show the reaction diagram
A8QPD8
-
-
-
?
4-nitrophenylbutyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
?
6-mercapto-1-butanol + methyl acrylate
6-mercaptobutyl acrylic ester
show the reaction diagram
-
besides two minor Michael-addition by-products, 6-mercaptobutyl acrylic ester is identified as the main product with the thiol as the functional end group
-
-
?
6-mercapto-1-butanol + methyl methacrylate
6-mercaptobutyl methacrylic ester
show the reaction diagram
-
-
-
-
?
6-mercapto-1-hexanol + methyl acrylate
6-mercaptohexyl acrylic ester
show the reaction diagram
-
besides two minor Michael-addition by-products, 6-mercaptohexyl acrylic ester is identified as the main product with the thiol as the functional end group
-
-
?
6-mercapto-1-hexanol + methyl methacrylate
6-mercaptohexyl methacrylic ester
show the reaction diagram
-
-
-
-
?
6-mercapto-1-hexanol + methyl propionate
6-mercaptohexyl propionic ester
show the reaction diagram
-
-
-
-
?
beta-butyrolactone
?
show the reaction diagram
-
ring-opening polymerizations
-
-
?
birch bark suberin + H2O
?
show the reaction diagram
S4VCH4
-
-
-
?
bis(2-hydroxyethyl)terephthalate + H2O
?
show the reaction diagram
-
fast hydrolysis after treatment for 30 min
-
-
?
bis(2-hydroxyethyl)terephthalate + H2O
?
show the reaction diagram
-
hydrolysis after treatment for 5 h
-
-
?
bis(benzoyloxyethyl)terephthalate + H2O
terephthalate + benzoic acid + 2-hydroxyethylbenzoate + mono-(2-hydroxyethyl)terephthalate + bis-(2-hydroxyethyl)terephthalate
show the reaction diagram
E9LVH8, E9LVH9
-
-
-
?
bis(benzoyloxyethyl)terephthalate + H2O
terephthalate + benzoic acid + 2-hydroxyethylbenzoate + mono-(2-hydroxyethyl)terephthalate + bis-(2-hydroxyethyl)terephthalate
show the reaction diagram
E9LVH8, E9LVH9
-
product ratios of wild-type and mutant enzymes, overview
-
?
bis(benzoyloxyethyl)terephthalate + H2O
terephthalate + benzoic acid + 2-hydroxyethylbenzoate + mono-(2-hydroxyethyl)terephthalate + bis-(2-hydroxyethyl)terephthalate
show the reaction diagram
Thermobifida cellulosilytica DSM 44535
E9LVH8, E9LVH9
-
-
-
?
bis(benzoyloxyethyl)terephthalate + H2O
terephthalate + benzoic acid + 2-hydroxyethylbenzoate + mono-(2-hydroxyethyl)terephthalate + bis-(2-hydroxyethyl)terephthalate
show the reaction diagram
Thermobifida cellulosilytica DSM 44535
E9LVH8, E9LVH9
-
product ratios of wild-type and mutant enzymes, overview
-
?
cutin + H2O
cutin monomers
show the reaction diagram
-
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
B9U443
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
-
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
A8QPD8
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
G8GER6, Q6A0I4
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
S4VCH4
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
Fusarium solani pisi
P00590
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
-
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
Q5AVY9
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
Q2VF46
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
Q9Y7G8
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
Q00298
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
P30272
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
P52956
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
M9M134
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
-
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
E9LVH7
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
E9LVH8, E9LVH9
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
Q874E9
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
-
-
main products: hexadecaoic acid, octadecaoic acid, and 10,16-dihydroxyhexadecaoic acid
-
?
cutin + H2O
cutin monomers
show the reaction diagram
-
-
reaction products include hexadecanoic acid, octadecanoic acid, 9-octadecenoic acid, 9,12-octadecadienoic acid, 16-hydroxy hexadecanoic acid, and 18-hydroxyoctadeca-9,12-dienoic acid, ratios of wild-type and recombinant alpha-hemolysin-enzyme differ, overview
-
?
cutin + H2O
cutin monomers
show the reaction diagram
-
cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
Fusarium solani pisi
P00590
cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
P52956
cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed
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-
?
cutin + H2O
cutin monomers
show the reaction diagram
E9LVH7
cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed
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-
?
cutin + H2O
cutin monomers
show the reaction diagram
E9LVH8, E9LVH9
cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed
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-
?
cutin + H2O
cutin monomers
show the reaction diagram
Q874E9
cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed
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-
?
cutin + H2O
cutin monomers
show the reaction diagram
Thermobifida fusca DSM 44342
-
cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed
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-
?
cutin + H2O
16-hydroxyhexadecanoic acid + 10,16-dihydroxyhexadecanoic acid + 9,10,18-trihydroxyoctadecanoic acid + 9,10,18-trihydroxyoctadecanoic acid-9.enoic acid
show the reaction diagram
-
hydrolysis of tritiated apple cutin, and GC-MS analysis of the hydrolysis products, overview
major apple cutin monomers released by the action of cutinases, but no formation of 18-hydroxyoctadeca-9-enoic acid and 18-hydroxyoctadeca-9,12-dienoic acid
-
?
cyclohexyl hexadecanoate + H2O
hexadecanoic acid + cyclohexanol
show the reaction diagram
-
-
-
-
?
delta-valerolactone
?
show the reaction diagram
-
ring-opening polymerizations
-
-
?
dihexyl phthalate + H2O
1,3-isobenzofurandione + ?
show the reaction diagram
-
-
-
-
?
dihexylphthalate + H2O
?
show the reaction diagram
-
degradation by cutinase is nearly 70% after 4 h, while 85% of the initial amount remains intact after 72 h of incubation with Candida cylindracea esterase. Products of cutinase-catalyzed hydrolysis are less toxic than those employing Candida cylindracea esterase
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-
?
dipentyl phthalate + H2O
?
show the reaction diagram
-
degradation rate of fungal cutinase is high, i.e., almost 60% of the initial dipentyl phthalate is decomposed within 2.5 hours, and nearly 40% of the degraded dipentyl phthalate disappears within the initial 15 min
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-
?
dipropyl phthalate + H2O
1,3-isobenzofurandione + propanol
show the reaction diagram
-
-
-
-
?
epsilon-caprolactone
?
show the reaction diagram
-
ring-opening polymerizations
-
-
?
ethyl butyrate + H2O
butyric acid + ethanol
show the reaction diagram
P41744
-
-
-
?
ethyl caprylate + H2O
caprylic acid + ethanol
show the reaction diagram
P41744
-
-
-
?
hexadecyl hexadecanoate + H2O
hexadecanoic acid + hexadecanol
show the reaction diagram
-
weak activity
-
-
?
malathion + H2O
?
show the reaction diagram
-
-
-
-
?
malathion + H2O
malathion monoacid + malathion diacid + ethanol
show the reaction diagram
-
60% of initial 500 mg/l malathion are degraded within 0.5 h
diacid is the major degradation product
-
?
methyl acetate + H2O
acetic acid + methanol
show the reaction diagram
P41744
-
-
-
?
methyl butyrate + H2O
butyric acid + methanol
show the reaction diagram
P41744
-
-
-
?
methyl caproate + H2O
caproic acid + methanol
show the reaction diagram
P41744
-
-
-
?
methyl caprylate + H2O
caprylic acid + methanol
show the reaction diagram
P41744
-
-
-
?
methyl decanoate + H2O
decanoic acid + methanol
show the reaction diagram
P41744
-
-
-
?
methyl hexadecanoate + H2O
hexadecanoic acid + methanol
show the reaction diagram
-
-
-
-
?
methyl laurate + H2O
lauric acid + methanol
show the reaction diagram
P41744
-
-
-
?
methyl myristate + H2O
myristic acid + methanol
show the reaction diagram
P41744
-
-
-
?
n-butyl benzyl phthalate + H2O
1,3-isobenzofurandione + n-butanol + benzyl alcohol
show the reaction diagram
-
-
major product, less than 5% of byproducts such as dimethyl phthalate, butyl methyl phthalate
-
?
omega-pentadecalactone
?
show the reaction diagram
-
ring-opening polymerizations
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
show the reaction diagram
B9U443
concentration of substrate dispersion is 5 mM
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
show the reaction diagram
P00590
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
show the reaction diagram
-
molecular modelling allows the synthesis of a solid-phase combinatorial library of triazine-based synthetic affinity compounds that is assessed for binding cutinase with high affinity while preserving enzyme functionality. Detection of binding ligands, in which immobilized cutinase retains 3060% of its enzymatic activity as compared to free enzyme
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-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
show the reaction diagram
B9U443
concentration of substrate dispersion is 5 mM
-
-
?
p-nitrophenyl butyrate + H2O
phenol + butyrate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl caprate + H2O
p-nitrophenol + ?
show the reaction diagram
B9U443
concentration of substrate dispersion is 5 mM
-
-
?
p-nitrophenyl caproate + H2O
p-nitrophenol + ?
show the reaction diagram
B9U443
concentration of substrate dispersion is 5 mM
-
-
?
p-nitrophenyl hexanoate + H2O
p-nitrophenol + hexanoate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl hexanoate + H2O
p-nitrophenol + hexanoate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl laurate + H2O
p-nitrophenol + ?
show the reaction diagram
B9U443
concentration of substrate dispersion is 5 mM
-
-
?
p-nitrophenyl myristate + H2O
p-nitrophenol + ?
show the reaction diagram
B9U443
concentration of substrate dispersion is 5 mM
-
-
?
p-nitrophenyl palmitate + H2O
p-nitrophenol + ?
show the reaction diagram
B9U443
concentration of substrate dispersion is 5 mM
-
-
?
p-nitrophenyl propionate + H2O
p-nitrophenol + ?
show the reaction diagram
B9U443
concentration of substrate dispersion is 5 mM
-
-
?
p-nitrophenyl stearate + H2O
p-nitrophenol + ?
show the reaction diagram
B9U443
a lower concentration of p-nitrophenyl stearate (2.5 mM) is used due to its lower solubility
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-
?
p-nitrophenyl valerate + H2O
p-nitrophenol + pentanoate
show the reaction diagram
A8QPD8
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-
-
-
p-nitrophenyl valerate + H2O
p-nitrophenol + pentanoate
show the reaction diagram
B9U443
concentration of substrate dispersion is 5 mM
-
-
?
p-nitrophenylbutanoate + H2O
p-nitrophenol + butanoate
show the reaction diagram
-
-
-
-
?
p-nitrophenylbutanoate + H2O
p-nitrophenol + butanoate
show the reaction diagram
-
-
-
-
?
p-nitrophenylbutanoate + H2O
p-nitrophenol + butanoate
show the reaction diagram
Fusarium roseum
-
-
-
-
?
p-nitrophenylbutanoate + H2O
p-nitrophenol + butanoate
show the reaction diagram
-
-
-
-
?
p-nitrophenylbutanoate + H2O
p-nitrophenol + butanoate
show the reaction diagram
-
-
-
-
?
p-nitrophenylbutanoate + H2O
p-nitrophenol + butanoate
show the reaction diagram
-
-
-
-
?
p-nitrophenylbutanoate + H2O
p-nitrophenol + butanoate
show the reaction diagram
Q8TGB8
-
-
-
?
p-nitrophenyldecanoate + H2O
p-nitrophenol + decanoate
show the reaction diagram
-
-
-
-
?
p-nitrophenyldecanoate + H2O
p-nitrophenol + decanoate
show the reaction diagram
-
-
-
-
?
p-nitrophenylhexadecanoate + H2O
p-nitrophenol + hexadecanoate
show the reaction diagram
-
-
-
-
?
p-nitrophenyltetradecanoate + H2O
p-nitrophenol + tetradecanoate
show the reaction diagram
-
-
-
-
?
poly(caprolactone) + H2O
?
show the reaction diagram
-
-
-
-
?
poly(ethylene terephthalate) + H2O
mono-(2-hydroxyethyl) terephthalate + terephthalic acid
show the reaction diagram
-
-
no formation of bis(2-hydroxyethyl) terephthalate, terephthalic acid is the major hydrolysis product for Thc_Cut1, whereas for Thc_Cut2, mono-(2-hydroxyethyl) terephthalate is the most abundant product
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?
poly(ethylene terephthalate) + H2O
mono-(2-hydroxyethyl) terephthalate + terephthalic acid
show the reaction diagram
Thermobifida fusca, Thermobifida fusca DSM44342
-
-
no formation of bis(2-hydroxyethyl) terephthalate. Terephthalic acid is the major hydrolysis product for Thf42_Cut1
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?
poly(ethylene terephthalate) + H2O
mono-(2-hydroxyethyl) terephthalate + terephthalic acid
show the reaction diagram
Thermobifida cellulosilytica DSM44535
-
-
no formation of bis(2-hydroxyethyl) terephthalate, terephthalic acid is the major hydrolysis product for Thc_Cut1, whereas for Thc_Cut2, mono-(2-hydroxyethyl) terephthalate is the most abundant product
-
?
polyamide + H2O
?
show the reaction diagram
-
-
-
-
?
polyethylene terephthalate + H2O
terephthalate + ?
show the reaction diagram
-
-
-
-
?
polyethyleneterephthalate + H2O
terephthalate + benzoic acid + 2-hydroxyethylbenzoate + mono-(2-hydroxyethyl)terephthalate + bis-(2-hydroxyethyl)terephthalate
show the reaction diagram
E9LVH8, E9LVH9
-
-
-
?
polyethyleneterephthalate + H2O
terephthalate + benzoic acid + 2-hydroxyethylbenzoate + mono-(2-hydroxyethyl)terephthalate + bis-(2-hydroxyethyl)terephthalate
show the reaction diagram
E9LVH8, E9LVH9
-
product ratios of wild-type and mutant enzymes, overview
-
?
polyethyleneterephthalate + H2O
terephthalate + benzoic acid + 2-hydroxyethylbenzoate + mono-(2-hydroxyethyl)terephthalate + bis-(2-hydroxyethyl)terephthalate
show the reaction diagram
Thermobifida cellulosilytica DSM 44535
E9LVH8, E9LVH9
-
-
-
?
polyethyleneterephthalate + H2O
terephthalate + benzoic acid + 2-hydroxyethylbenzoate + mono-(2-hydroxyethyl)terephthalate + bis-(2-hydroxyethyl)terephthalate
show the reaction diagram
Thermobifida cellulosilytica DSM 44535
E9LVH8, E9LVH9
-
product ratios of wild-type and mutant enzymes, overview
-
?
suberin + H2O
?
show the reaction diagram
B9U443
9,10-epoxy-18-hydroxy 5 octadecanoic acid
-
-
?
tributyrin + H2O
?
show the reaction diagram
-
-
-
-
?
tributyrin + H2O
?
show the reaction diagram
-
-
-
-
?
tributyrin + H2O
?
show the reaction diagram
-
-
-
-
?
tributyrin + H2O
?
show the reaction diagram
P41744
-
-
-
?
tributyrin + H2O
butyric acid + 1,2-dibutyrylglycerol
show the reaction diagram
Fusarium solani pisi
P00590
-
-
-
?
tricaprylin + H2O
?
show the reaction diagram
-
-
-
-
?
tricaprylin + H2O
?
show the reaction diagram
-
-
-
-
?
tricaprylin + H2O
?
show the reaction diagram
P41744
-
-
-
?
triglyceride + H2O
?
show the reaction diagram
-
triglycerides in which one of the primary acyl ester functions has been replaced by an alkyl grpup and the secondary acyl ester bond has been replaced by an acyl amino bond. The activity is very sensitive to the length and distribution of the acyl chains, the highest activity is found when the chains at position 1 and 3 contain three or four carbon atoms
-
-
?
trioctanoin + H2O
?
show the reaction diagram
Fusarium solani pisi
P00590
-
-
-
?
triolein + H2O
?
show the reaction diagram
-
-
-
-
?
triolein + H2O
?
show the reaction diagram
-
-
-
-
?
triolein + H2O
?
show the reaction diagram
P41744
-
-
-
?
triolein + H2O
?
show the reaction diagram
Fusarium solani pisi
P00590
-
-
-
?
tripalmitin + H2O
?
show the reaction diagram
P41744
-
-
-
?
tristearin + H2O
?
show the reaction diagram
P41744
-
-
-
?
tritiated apple cutin + H2O
?
show the reaction diagram
S4VCH4
-
-
-
?
bisbenzoyloxyethyl terephthalate + H2O
terephthalic acid + mono(2-hydroxyethyl) terephthalate + bis(2-hydroxyethyl)terephthalate + benzoic acid + 2-hydroxyethyl benzoate
show the reaction diagram
-
-
-
-
?
cutin + H2O
additional information
-
-
-
-
-
?
cutin + H2O
additional information
-
-
-
-
-
?
cutin + H2O
additional information
-
P00590
-
-
-
?
cutin + H2O
additional information
-
-
-
-
-
?
cutin + H2O
additional information
-
Fusarium roseum
-
-
-
-
?
cutin + H2O
additional information
-
-
-
-
-
?
cutin + H2O
additional information
-
-
-
-
-
?
cutin + H2O
additional information
-
-
-
-
-
?
cutin + H2O
additional information
-
-
-
-
-
?
cutin + H2O
additional information
-
-
-
-
-
?
cutin + H2O
additional information
-
-
-
-
-
?
cutin + H2O
additional information
-
-
-
dihydroxyhexadecanoic acid, cutin monomer + cutin oligomers
?
cutin + H2O
additional information
-
-
apple cutin
-
-
?
cutin + H2O
additional information
-
Botrytis cinerea Pser.: Fr.
-
-
-
-
?
cutin + H2O
additional information
-
Aspergillus nidulans CECT, Aspergillus nidulans 20, Aspergillus nidulans 211, Aspergillus nidulans 15, Aspergillus nidulans 35
-
-
-
-
?
methyl propionate + H2O
propionic acid + methanol
show the reaction diagram
P41744
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
does not act on tripalmitoyl glycerol or trioleoyl glycerol
-
-
-
additional information
?
-
Fusarium roseum
-
no hydrolysis of p-nitrophenyl palmitate
-
-
-
additional information
?
-
-
catalytic triad: S120, H188, D175. Presence of a preformed oxyanion hole
-
-
-
additional information
?
-
-
constitutive enzyme
-
-
-
additional information
?
-
-
induced by cutin
-
-
-
additional information
?
-
-
Cutinase is known for its hydrolytic activity for a variety of esters ranging from soluble p-nitrophenyl esters to insoluble long-chain triglycerides. The hydrolytic activity of cutinase, especially on p-nitrophenyl esters of fatty acids, is extremely sensitive to fatty acid chain length.
-
-
-
additional information
?
-
B9U443
CcCUT1 has higher activity on shorter (C2-C10) 12 fatty acid esters of p-nitrophenol than on longer ones and it also exhibited lipase activity. Microscopical analyses and determination of released hydrolysis products showed that the enzyme is able to depolymerize apple cutin and birch outer bark suberin
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-
-
additional information
?
-
-
during its catalytic cycle, cutinase undergoes a significant conformational rearrangement converting the loop bearing the histidine from an inactive conformation, in which the histidine of the triad is solvent exposed, to an active conformation, in which the triad assumes a classic configuration. Major difference between the structures is in the position of the loop connecting beta5 and alpha5 (Gly196Phe205 in Glomerella cingulata cutinase and Gly180Leu189 in Fusarium solani cutinase). Consequence of the repositioning of the loop is that the active-site regions of the enzymes differ substantially in the location of the putative catalytic histidine (His188 of Fusarium solani cutinase and His204 of Glomerella cingulata cutinase)
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-
-
additional information
?
-
-
four cysteine residues pivotal to the formation of the two disulphide bridges and a highly conserved cut-1 motif (GYSQG) surrounding a cutinase active serine, but a less precise cut-2 motif, DxVCxG(ST)-(LIVMF)(3)-x(3)H, which carries the aspartate and histidine residues of the active site
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-
-
additional information
?
-
-
four cysteine residues pivotal to the formation of the two disulphide bridges and a highly conserved cut-1 motif (GYSQG) surrounding a cutinase active serine, but a less precise cut-2 motif, DxVCxG(ST)-(LIVMF)(3)-x(3)H, which carries the aspartate and histidine residues of the active site. Two exceptions: one cutinase gene is truncated at the 3' end immediately after the cut-1 motif owing to a gap in the genomic sequence, and one cutinase gene, which is truncated at the 3' end shortly before the cut-2 motif because of a repetitive sequence, making further prediction impossible
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-
-
additional information
?
-
-
major difference between the structures is in the position of the loop connecting beta5 and alpha5 (Gly196Phe205 in Glomerella cingulata cutinase and Gly180Leu189 in Fusarium solani cutinase). Consequence of the repositioning of the loop is that the active-site regions of the enzymes differ substantially in the location of the putative catalytic histidine (His188 of Fusarium solani cutinase and His204 of Glomerella cingulata cutinase)
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-
-
additional information
?
-
-
shows promising activity in polymerization reactions
-
-
-
additional information
?
-
-
cutinase is an esterase, whose active site, located at the middle of a sharp turn between beta-strand and alpha-helix, is composed by the triad Ser120, Asp175 and His188
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-
-
additional information
?
-
-
the enzyme exhibits a broad substrate specificity against plant cutin, synthetic polyesters, insoluble triglycerides, and soluble esters
-
-
-
additional information
?
-
-
cutinase catalyzes esterification of caproic acid in an organic solvent system, alcohol, acid and n-decane are mixed thoroughly in iso-octane before the addition of the lyophilized enzyme, overview. The main kinetic characteristics observed in esterification reaction follow an ordered Ping-Pong Bi-Bi mechanism
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-
-
additional information
?
-
-
substrate binding, modelling and docking study, overview
-
-
-
additional information
?
-
-
substrate binding, modelling and docking study,overview
-
-
-
additional information
?
-
-
the cutinase demonstrates enhanced poly(epsilon-caprolactone) hydrolysis at high temperatures and under all pH value. The cutinase shows activity on 4-nitrophenyl butyrate
-
-
-
additional information
?
-
-
the enzyme catalyzes the transesterification of triolein and methanol, overview
-
-
-
additional information
?
-
-
cutinase is a multi-functional esterase, which shows hydrolytic activity (cutin and a variety of soluble synthetic esters, insoluble triglycerides and polyesters), synthetic activity and transester activity
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-
-
additional information
?
-
Q5AVY9
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
Q2VF46
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
Q9Y7G8
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
Q00298
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
P30272
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
P52956
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
M9M134
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
Humilica insolens, Streptomyces badius
-
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
E9LVH7
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
E9LVH8, E9LVH9
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
Q874E9
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification. The cuticle layer of a cotton fiber has a complicated composition that includes cutin, wax, pectin and protein, and both the wax and cutin can be hydrolysed by the cutinase
-
-
-
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification. The cuticle layer of a cotton fiber has a complicated composition that includes cutin, wax, pectin and protein, and both the wax and cutin can be hydrolysed by the cutinase. The cutinase can modify the surface of synthetic fibers, like polyesters, polyamides, acrylics, and cellulose acetate, and improve their wettability and dyeability
-
-
-
additional information
?
-
Fusarium solani pisi
P00590
cutinases are capable of catalyzing esterification and transesterification. The enzyme prefers triacylglyceride substrates with short acyl groups
-
-
-
additional information
?
-
-
the enzyme has hydrolytic activity toward phospholipids of the cell membrane, cf. EC 3.1.1.3
-
-
-
additional information
?
-
-
the enzyme shows polyethylene terephthalate-degrading activity
-
-
-
additional information
?
-
-
applying methyl methacrylate, transesterification with 6-mercapto-1-hexanol is significantly lower compared to transesterification of methyl acrylate with 6-mercapto-1-hexanol
-
-
-
additional information
?
-
Fusarium solani pisi
P00590
the cuticle layer of a cotton fiber has a complicated composition that includes cutin, wax, pectin and protein, and both the wax and cutin can be hydrolysed by the cutinase. The cutinase can modify the surface of synthetic fibers, like polyesters, polyamides, acrylics, and cellulose acetate, and improve their wettability and dyeability
-
-
-
additional information
?
-
-
the enzyme catalyzes the synthesis of methyl esters of tributyrin, triolein, and soybean oil by transesterification, maximum conversion of 65% at optimal conditions of methanol to oil ratio of 1.5:1 and 2.5mg/ml enzyme
-
-
-
additional information
?
-
E9LVH7
the enzyme hydrolyzes synthetic polyesters, including Ecoflex, poly(caprolactone), poly(butylene succinate-coadipate), poly(butylene succinate), poly(L-lactic acid) and poly(D-lactic acid), but not poly(3-hydroxybutyric acid)
-
-
-
additional information
?
-
-
the enzyme prefers 4-nitrophenyl ester substrates with chain lengths of C4-C6, production and assay method optimization, overview
-
-
-
additional information
?
-
S4VCH4
the enzyme prefers shorter (C2 to C3) fatty acid esters of 4-nitrophenol to longer ones, no or poor activity with 4-nitrophenyl esters substrates of C10-C18, overview. The enzyme also shows lipase activity with olive oil as substrate
-
-
-
additional information
?
-
-
the optimum ratio of butyrate, acetate, and lactate is 4:1:3
-
-
-
additional information
?
-
Botrytis cinerea Pser.: Fr.
-
constitutive enzyme
-
-
-
additional information
?
-
Burkholderia cepacia NRRL B 2320
-
the enzyme catalyzes the synthesis of methyl esters of tributyrin, triolein, and soybean oil by transesterification, maximum conversion of 65% at optimal conditions of methanol to oil ratio of 1.5:1 and 2.5mg/ml enzyme
-
-
-
additional information
?
-
Burkholderia cepacia NRRL B 2320
-
the enzyme prefers 4-nitrophenyl ester substrates with chain lengths of C4-C6, production and assay method optimization, overview
-
-
-
additional information
?
-
Thermobifida fusca DSM44342
-
substrate binding, modelling and docking study,overview
-
-
-
additional information
?
-
Thermobifida fusca DSM 44342
-
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
Sirococcus conigenus VTT D-04989
S4VCH4
the enzyme prefers shorter (C2 to C3) fatty acid esters of 4-nitrophenol to longer ones, no or poor activity with 4-nitrophenyl esters substrates of C10-C18, overview. The enzyme also shows lipase activity with olive oil as substrate
-
-
-
additional information
?
-
Thermobifida cellulosilytica DSM44535
-
substrate binding, modelling and docking study, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cutin + H2O
cutin monomers
show the reaction diagram
-
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
G8GER6, Q6A0I4
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
S4VCH4
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
-
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
Q5AVY9
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
Q2VF46
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
Q9Y7G8
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
Q00298
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
P30272
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
M9M134
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
-
-
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
-
cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
Fusarium solani pisi
P00590
cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
P52956
cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
E9LVH7
cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
E9LVH8, E9LVH9
cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed
-
-
?
cutin + H2O
cutin monomers
show the reaction diagram
Q874E9
cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed
-
-
?
cutin + H2O
16-hydroxyhexadecanoic acid + 10,16-dihydroxyhexadecanoic acid + 9,10,18-trihydroxyoctadecanoic acid + 9,10,18-trihydroxyoctadecanoic acid-9.enoic acid
show the reaction diagram
-
hydrolysis of tritiated apple cutin, and GC-MS analysis of the hydrolysis products, overview
major apple cutin monomers released by the action of cutinases, but no formation of 18-hydroxyoctadeca-9-enoic acid and 18-hydroxyoctadeca-9,12-dienoic acid
-
?
cutin + H2O
cutin monomers
show the reaction diagram
Thermobifida fusca DSM 44342
-
cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed
-
-
?
poly(caprolactone) + H2O
?
show the reaction diagram
-
-
-
-
?
cutin + H2O
16-hydroxyhexadecanoic acid + 10,16-dihydroxyhexadecanoic acid + 9,10,18-trihydroxyoctadecanoic acid + 9,10,18-trihydroxyoctadecanoic acid-9.enoic acid
show the reaction diagram
-
hydrolysis of tritiated apple cutin, and GC-MS analysis of the hydrolysis products, overview
major apple cutin monomers released by the action of cutinases, but no formation of 18-hydroxyoctadeca-9-enoic acid and 18-hydroxyoctadeca-9,12-dienoic acid
-
?
additional information
?
-
-
constitutive enzyme
-
-
-
additional information
?
-
-
induced by cutin
-
-
-
additional information
?
-
-
Cutinase is known for its hydrolytic activity for a variety of esters ranging from soluble p-nitrophenyl esters to insoluble long-chain triglycerides. The hydrolytic activity of cutinase, especially on p-nitrophenyl esters of fatty acids, is extremely sensitive to fatty acid chain length.
-
-
-
additional information
?
-
-
cutinase is an esterase, whose active site, located at the middle of a sharp turn between beta-strand and alpha-helix, is composed by the triad Ser120, Asp175 and His188
-
-
-
additional information
?
-
-
the enzyme exhibits a broad substrate specificity against plant cutin, synthetic polyesters, insoluble triglycerides, and soluble esters
-
-
-
additional information
?
-
-
cutinase is a multi-functional esterase, which shows hydrolytic activity (cutin and a variety of soluble synthetic esters, insoluble triglycerides and polyesters), synthetic activity and transester activity
-
-
-
additional information
?
-
Q5AVY9
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
Q2VF46
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
Q9Y7G8
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
Q00298
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
P30272
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
P52956
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
M9M134
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
Humilica insolens, Streptomyces badius
-
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
E9LVH7
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
E9LVH8, E9LVH9
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
Q874E9
cutinases are capable of catalyzing esterification and transesterification
-
-
-
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification. The cuticle layer of a cotton fiber has a complicated composition that includes cutin, wax, pectin and protein, and both the wax and cutin can be hydrolysed by the cutinase
-
-
-
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification. The cuticle layer of a cotton fiber has a complicated composition that includes cutin, wax, pectin and protein, and both the wax and cutin can be hydrolysed by the cutinase. The cutinase can modify the surface of synthetic fibers, like polyesters, polyamides, acrylics, and cellulose acetate, and improve their wettability and dyeability
-
-
-
additional information
?
-
Fusarium solani pisi
P00590
cutinases are capable of catalyzing esterification and transesterification. The enzyme prefers triacylglyceride substrates with short acyl groups
-
-
-
additional information
?
-
-
the enzyme has hydrolytic activity toward phospholipids of the cell membrane, cf. EC 3.1.1.3
-
-
-
additional information
?
-
-
the enzyme shows polyethylene terephthalate-degrading activity
-
-
-
additional information
?
-
Botrytis cinerea Pser.: Fr.
-
constitutive enzyme
-
-
-
additional information
?
-
Thermobifida fusca DSM 44342
-
cutinases are capable of catalyzing esterification and transesterification
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
-
activates isozyme Tfu 0883 7% at 1 mM
Ca2+
-
slight activation at 1 mM
Ca2+
-
activates at 1 mM
Co2+
-
activates 7% at 1 mM
Co2+
-
activates isozyme Tfu 0882 4% and isozyme Tfu 0883 24% at 1 mM
Co2+
-
activates at 1 mM
K+
-
activates at 1 mM
KCl
-
activates 12% at 1 mM
Mg2+
-
activates isozyme Tfu 0883 11% at 1 mM
Mg2+
-
activates at 1 mM
Mn2+
-
activates 36% at 1 mM
Na+
-
slight activation at 1 mM
Na+
-
activates at 1 mM
NaCl
-
activates 15% at 1 mM; activates 20% at 1 mM
Ni2+
-
activates isozyme Tfu 0882 5% and isozyme Tfu 0883 7% at 1 mM
NiCl2
-
activates 11% at 1 mM
Mn2+
-
activates isozyme Tfu 0882 9% and isozyme Tfu 0883 24% at 1 mM
additional information
-
EDTA has no effect on enzyme activity at 10 mM
additional information
-
Ba2+ and EDTA have no effect on enzyme activity at 1 mM and 10 mM, respectively
additional information
-
no effect on enzyme activity by 1 mM CoCl2, KCl, NiCl2, MgSO4, and MnCl2; no effect on enzyme activity by 1 mM CoCl2, MnCl2, and MgSO4
additional information
S4VCH4
incubating the enzyme with 5 mM CaCl2, CoCl2, CuSO4, EDTA, FeCl2, MgCl2, MnCl2, Ni(NO3)2, ZnCl2, or 10 mM dithiothreitol has no significant effect on the 4-nitrophenyl butyrate hydrolysis activity
additional information
-
the enzyme activity is poorly or not affected by 1 mM Li+, K+, Co2+, and Zn2+
additional information
-
Ni2+ and Mn2+ do not affect enzyme activity at 1 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(O,O)-diethyl-(3,5,6-trichloro)-2-pyridylphosphorothioate
-
1 mM, 90% inhibition
1-Heptanol
-
27% inhibition at 40% v/v; 28% inhibition at 40% v/v
1-Hexanol
-
68% inhibition at 40% v/v; 86% inhibition at 40% v/v
2,3,5-trichloropyridine-6-(O-methyl-O-n-butyl)-phosphate ester
-
i.e. MAT 9564
2-mercaptoethanol
-
slight inhibition at 10 mM
2-[(ethylsulfanyl)methyl]phenyl hydrogen methylcarbonimidate
-
-
3-(4-mercaptobutylthio)-1,1,1-trifluoro-2-propanone
-
-
3-n-octylthio-1,1,1-trifluoro-2-propanone
-
-
3-phenethylthio-1,1,1-trifluoropropan-2-one
-
-
3-phenylthio-1,1,1-trifluoropropan-2-one
-
-
4-nitrophenyl P-methyl-N-octylphosphonamidoate
-
-
6-mercaptohexyl acrylic ester
-
product inhibition
-
acetone
-
92% inhibition at 75% v/v
AgNO3
-
90% inhibition at 1 mM; 93% inhibition at 1 mM
alkylboronic acids
-
-
ANS
P00590
binds strongly to native cutinase as a noncompetitive inhibitor with up to 5 ANS per cutinase molecule. The first ANS molecule stabilizes cutinase. The last 4 ANS molecules decrease Tm by up to 7C
Ba2+
-
inhibits isozyme Tfu 0882 7%
BaCl2
-
14% inhibition at 1 mM; 8% inhibition at 1 mM
Benzene
-
77% inhibition at 40% v/v; 79% inhibition at 40% v/v
butanol
-
10% inhibition at 40% v/v; 17% inhibition at 40% v/v
Ca2+
-
inhibits 6% at 1 mM
Ca2+
-
inhibits isozyme Tfu 0882 28% and isozyme Tfu 0883 18% at 1 mM
Carbaryl
-
-
carbofuran
-
-
chlorpyrifos-methyl
-
upon chloroperoxidase oxidation, chlorpyrifos-methyl shows a very strong cutinase inhibition as compared to the corresponding oxon standard
chlorpyrifos-methyl oxon
-
-
Cr3+
-
inhibits 72% at 1 mM
Cr3+
-
inhibits isozyme Tfu 0882 89% and isozyme Tfu 0883 90% at 1 mM
CrCl2
-
99% inhibition at 1 mM; 99% inhibition at 1 mM
Cu2+
-
inhibits 17% at 1 mM
Cu2+
-
85% inhibition at 1 mM
CuSO4
-
26% inhibition at 1 mM; 32% inhibition at 1 mM
D-glucose
A8QPD8
Thcut1 mRNA is repressed by glucose
deoxycholate
-
24% inhibition at 10 mM; 25% inhibition at 10 mM
Dichloromethane
-
61% inhibition at 40% v/v; 74% inhibition at 40% v/v
Dichloromethane
-
78% inhibition at 75% v/v
Diethyl p-nitrophenyl phosphate
-
covalent
Diethyl p-nitrophenyl phosphate
-
; E600
diethyl-p-nitrophenyl phosphate
-
-
diethyldicarbonate
-
54% inhibition at 1 mM; 56% inhibition at 1 mM
diisopropyl fluorophosphate
-
102 nM, 90% inhibition
diisopropyl fluorophosphate
-
1 mM, 90% inhibition
diisopropyl fluorophosphate
Fusarium roseum
-
0.025 mM, complete inhibition
diisopropyl fluorophosphate
-
-
Dioxan
-
23% inhibition at 75% v/v
DMSO
-
49% inhibition at 75% v/v
ethanol
-
97% inhibition at 75% v/v
Fe2+
-
inhibits 54% at 1 mM
Fe2+
-
inhibits isozyme Tfu 0882 45% and isozyme Tfu 0883 36% at 1 mM
Fe2+
-
slight inhibition at 1 mM
Fe2+
-
20% inhibition at 1 mM
FeSO4
-
55% inhibition at 1 mM; 55% inhibition at 1 mM
glycerol
-
inhibits the transesterification activity of the cutinase after 10 min of incubation
guanidine hydrochloride
-
;
guanidine hydrochloride
-
GdnHCl-induced unfolding of LC-cutinase is analyzed at pH 8.0 by circular dichroism spectroscopy, overview
hexyl acetate
-
63% inhibition at 40% v/v; 83% inhibition at 40% v/v
Hg2+
-
inhibits completely at 1 mM
Hg2+
-
inhibits isozyme Tfu 0882 and isozyme Tfu 0883 completely at 1 mM
Hg2+
-
inhibits completely at 1 mM
HgCl2
-
99% inhibition at 1 mM; 99% inhibition at 1 mM
Isopropanol
-
complete inhibition at 75% v/v
methanol
-
8% inhibition at 40% v/v
methanol
-
inhibits the transesterification reaction of the enzyme
methanol
-
90% inhibition at 75% v/v
methomyl
-
-
Mg2+
-
inhibits 11% at 1 mM
Mg2+
-
inhibits isozyme Tfu 0882 34%
Mg2+
-
slight inhibition at 1 mM
MgCl2
-
15% inhibition at 1 mM; 8% inhibition at 1 mM
n-hexane
-
10% inhibition at 40% v/v
n-hexane
-
18.5% inhibition at 75% v/v
Ni2+
-
inhibits 7% at 1 mM
O-(4-nitrophenyl) S-octyl methylphosphonothioate
-
-
O-methyl-O-(p-nitrophenyl)octylphosphonate
-
-
O-octyl-O-(p-nitrophenyl)ethylphosphonate
-
-
O-octyl-O-(p-nitrophenyl)methylphosphonate
-
-
oxidized malathion
-
oxidized malathion, contrarily to malaoxon, reveals cutinase inhibition
Paraoxon
Fusarium roseum
-
0.1 mM, complete inhibition
paraoxon-methyl
-
-
Pb2+
-
inhibits 39% at 1 mM
Pb2+
-
inhibits isozyme Tfu 0882 48% and isozyme Tfu 0883 52% at 1 mM
PbCl2
-
53% inhibition at 1 mM; 54% inhibition at 1 mM
phenylboronic acid
-
5 mM, 63% inhibition, competitive
PMSF
-
48% inhibition at 1 mM; 59% inhibition at 1 mM
PMSF
-
95% inhibition at 1 mM
primicarb
-
-
propoxur
-
-
RbCl
-
93% inhibition at 1 mM; 95% inhibition at 1 mM
SDS
-
30% inhibition at 1 mM; 9% inhibition at 1 mM
sodium bis(2-ethylhexyl)ester sulfosuccinic acid
-
pseudo-competitive inhibitor
Sodium deoxycholate
-
-
sodium dioctyl sulfosuccinate
-
-
Sodium dodecyl sulfate
-
competitive, detailed study of interaction with enzyme. At molar ratio of SDS:enzyme of about 10, formation of aggregates which include more than one protein molecule. At higher concentration of SDS, denaturation of protein, denatured state of enzyme is unusually compact
triethylamine
-
24% inhibition at 40% v/v
Triton X-100
-
35% inhibition at 1 mM; 55% inhibition at 1 mM
Tween-20
-
28% inhibition at 1 mM; 35% inhibition at 1 mM
Tween-80
-
24% inhibition at 1 mM; 60% inhibition at 1 mM
Urea
-
17% inhibition at 1 mM; 30% inhibition at 1 mM
Zn2+
-
inhibits 18% at 1 mM
Zn2+
-
inhibits isozyme Tfu 0882 50% and isozyme Tfu 0883 56% at 1 mM
Zn2+
-
18% inhibition at 1 mM
ZnSO4
-
59% inhibition at 1 mM; 65% inhibition at 1 mM
Mn2+
-
slight inhibition at 1 mM
additional information
-
except for methomyl no significant effects of chloroperoxidase oxidation on the inhibition strength of insecticidal carbamates can be detected. No inhibition by malathion and malaoxon
-
additional information
-
crystallization and preliminary X-ray analysis of cutinase-inhibitor complexes
-
additional information
-
inhibition by organophosphate pesticides. Carbamate pesticides reveal an efficient cutinase inhibitor effect, though less potent than the organophosphates
-
additional information
-
no or poor inhibition by tetrahydrofuran, n-hexane, methanol, ethanol, acetone, and acetonitrile at 40% v/v, or by 10 mM sodium deoxycholate and 1 mM EDTA; no or poor inhibition by tetrahydrofuran, triethylamine, ethanol, acetone, and acetonitrile at 40% v/v, or by 10 mM sodium deoxycholate and 1 mM EDTA
-
additional information
-
structure comparisons of isozymes Cut1 and Cut2 during denaturation and unfolding, overview; structure comparisons of isozymes Cut1 and Cut2 during denaturation and unfolding, overview
-
additional information
-
no inhibition by EDTA, Triton X-100 and Tween 80, or by 75% v/v chloroform, isooctane, isoamyl alcohol, or butanol
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
16-hydroxyhexadecanoic acid
A8QPD8
is strongly induced in vitro by cutin monomer 16-hydroxyhexadecanoic acid
DMF
-
activates 10% at 40% v/v; activates 6% at 40% v/v
N,N-diethyl-2-phenylacetamide
-
increases hydrolysis rates of semi-crystalline poly(ethylene terephthalate) films and fabrics for cutinase. The outer layers of the polymer will be better exposed to the enzyme in the presence of N,N-diethyl-2-phenylacetamide. Overall enhancement in colour depth of 300%
olive oil
A8QPD8
Thcut1 mRNA is strongly induced in vitro by olive oil
-
sodium dioctyl sulfosuccinate
-
in the absence of surfactant the S54D variant catalytic activity is similar to that of the wild type cutinase, whereas L153Q and T179C variants show a lower activity
sodium taurodeoxychlate
-
activates 10% at 10 mM; activates 24% at 10 mM
-
DMSO
-
activates 14% at 40% v/v; activates 9% at 40% v/v
additional information
-
pseudo-activation in presence of sodium bis(2-ethylhexyl)ester sulfosuccinic acid and hexadecyltrimethyl-ammoniumbromide
-
additional information
-
absence of interfacial activation
-
additional information
-
water:surfactant molar rate has a marked influence on the enzyme activity, with the best results in the range between 5 and 8. The use of detergents improves the reaction yield during wetting of cotton fibers. Increase in the stereoselectivity of the primary hydroxyl group acylation is obtained through the preincubation of the enzyme in the presence of the substrate diol 1, there is no correlation with the incubation time
-
additional information
-
no activation in the presence of Triton X-100 due to the absence of a lid covering the active site pocket
-
additional information
-
Pichia pastoris expressing the native non-tagged cutinase exhibits about 2- and 3fold higher values of protein amount and cutinase activity in the culture supernatant, respectively, than those containing the C-terminal tagged cutinase
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00067
4-nitrophenyl acetate
-
in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol
0.00496
4-nitrophenyl acetate
-
in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol
0.127
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH and temperature not specified in the publication
0.167
4-nitrophenyl acetate
-
pH and temperature not specified in the publication
0.2
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH and temperature not specified in the publication
0.213
4-nitrophenyl acetate
E9LVH7
pH and temperature not specified in the publication
0.8
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R187K
1.2
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R19S; pH 7.0, 25C, recombinant mutant R19S/R29N/A30V
1.3
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R29N; pH 7.0, 25C, recombinant mutant R29N/A30V
1.5
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant isozyme; pH 7.0, 25C, recombinant mutant Q65E
1.7
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant A30V
1.9
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant L183A; pH 7.0, 25C, recombinant wild-type isozyme
63
4-nitrophenyl acetate
-
pH 8.0, 25C, recombinant enzyme
0.00021
4-nitrophenyl butyrate
-
in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol
0.00126
4-nitrophenyl butyrate
-
in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol
0.00136
4-nitrophenyl butyrate
-
pH 7.5, 25C
0.00196
4-nitrophenyl butyrate
-
pH 7.5, 25C
0.0025
4-nitrophenyl butyrate
-
pH 7.5, 25C
0.00896
4-nitrophenyl butyrate
-
pH 7.5, 25C
0.029
4-nitrophenyl butyrate
-
pH 7.5, 25C
0.18
4-nitrophenyl butyrate
-
pH 8.0, 50C, recombinant mutant C275A/C292A, absence of 1% PEG
0.19
4-nitrophenyl butyrate
-
pH 8.0, 70C, recombinant mutant C275A/C292A, absence of 1% PEG
0.21
4-nitrophenyl butyrate
-
pH 8.0, 50C, recombinant wild-type enzyme, absence of 1% PEG
0.22
4-nitrophenyl butyrate
-
pH 8.0, 30C, recombinant wild-type enzyme, absence of 1% PEG
0.24
4-nitrophenyl butyrate
-
pH 8.0, 70C, recombinant wild-type enzyme, absence of 1% PEG
0.25
4-nitrophenyl butyrate
-
pH 8.0, 30C, recombinant mutant C275A/C292A, absence of 1% PEG; pH 8.0, 70C, recombinant wild-type enzyme, absence of 1% PEG
0.27
4-nitrophenyl butyrate
-
pH 8.0, 30C, recombinant wild-type enzyme, presence of 1% PEG; pH 8.0, 50C, recombinant wild-type enzyme, presence of 1% PEG
0.272
4-nitrophenyl butyrate
-
pH 8.0, 60C, recombinant cutinase FspC
0.454
4-nitrophenyl butyrate
-
pH 7.5, 30C, recombinant enzyme
0.505
4-nitrophenyl butyrate
-
pH 8.0, 60C, isozyme Tfu 0883
0.673
4-nitrophenyl butyrate
-
pH 8.0, 60C, isozyme Tfu 0882
0.8
4-nitrophenyl butyrate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant isozyme
1
4-nitrophenyl butyrate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R29N/A30V
1.1
4-nitrophenyl butyrate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant A30V
1.4
4-nitrophenyl butyrate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R19S/R29N/A30V
1.67
4-nitrophenyl butyrate
S4VCH4
pH 4.5, 25C, recombinant enzyme
2
4-nitrophenyl butyrate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R29N
2.1
4-nitrophenyl butyrate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant L183A
2.2
4-nitrophenyl butyrate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R19S
2.6
4-nitrophenyl butyrate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant Q65E
3.4
4-nitrophenyl butyrate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant wild-type isozyme
4
4-nitrophenyl butyrate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R187K
20
4-nitrophenyl butyrate
-
pH 8.0, 25C, recombinant enzyme
59.2
4-nitrophenyl butyrate
P52956
pH and temperature not specified in the publication
7.24
4-nitrophenyl caprylate
-
pH 8.0, 25C, recombinant enzyme
0.00029
4-nitrophenyl hexanoate
-
in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol
0.0015
4-nitrophenyl hexanoate
-
in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol
0.21
4-nitrophenyl hexanoate
-
-
0.86
4-nitrophenyl hexanoate
-
cutinase II
0.89
4-nitrophenyl hexanoate
-
cutinase I
7.14
4-nitrophenyl laurate
-
pH 8.0, 25C, recombinant enzyme
7.25
4-nitrophenyl myristate
-
pH 8.0, 25C, recombinant enzyme
0.207
4-nitrophenyl octanoate
-
pH 7.5, 30C, recombinant enzyme
0.59
4-nitrophenyl octanoate
-
cutinase II
0.88
4-nitrophenyl octanoate
-
cutinase I
1.7
4-nitrophenyl octanoate
-
-
2.246
4-nitrophenyl palmitate
-
pH 7.5, 30C, recombinant enzyme
0.00004
4-nitrophenyl valerate
-
in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol
0.00148
4-nitrophenyl valerate
-
in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol
0.33
p-nitrophenyl acetate
A8QPD8
-
0.000121
p-nitrophenyl butyrate
P00590
20C, pH 8, no additive
0.2
p-nitrophenyl butyrate
-
T179C mutant, sodium dioctyl sulfosuccinate concentration = 0 mM
0.31
p-nitrophenyl butyrate
-
L153Q mutant, sodium dioctyl sulfosuccinate concentration = 0 mM
0.33
p-nitrophenyl butyrate
-
S54D mutant, sodium dioctyl sulfosuccinate concentration = 0 mM
0.35
p-nitrophenyl butyrate
-
wild type, sodium dioctyl sulfosuccinate concentration = 0 mM
0.48
p-nitrophenyl butyrate
-
wild type, sodium dioctyl sulfosuccinate concentration = 0.5 mM
0.49
p-nitrophenyl butyrate
-
T179Cmutant, sodium dioctyl sulfosuccinate concentration = 0.5 mM
0.57
p-nitrophenyl butyrate
A8QPD8
-
0.66
p-nitrophenyl butyrate
-
T179C mutant, sodium dioctyl sulfosuccinate concentration = 1 mM
0.69
p-nitrophenyl butyrate
-
L153Q mutant, sodium dioctyl sulfosuccinate concentration = 0.5 mM
0.72
p-nitrophenyl butyrate
-
S54D mutant, sodium dioctyl sulfosuccinate concentration = 1 mM
0.74
p-nitrophenyl butyrate
-
S54D mutant, sodium dioctyl sulfosuccinate concentration = 0.5 mM
0.85
p-nitrophenyl butyrate
-
wild type, sodium dioctyl sulfosuccinate concentration = 1 mM
1.08
p-nitrophenyl butyrate
-
wild type, sodium dioctyl sulfosuccinate concentration = 2 mM
1.09
p-nitrophenyl butyrate
-
T179C mutant, sodium dioctyl sulfosuccinate concentration = 1.5 mM
1.12
p-nitrophenyl butyrate
-
wild type, sodium dioctyl sulfosuccinate concentration = 1.5 mM
1.14
p-nitrophenyl butyrate
-
S54D mutant, sodium dioctyl sulfosuccinate concentration = 1.5 mM
1.31
p-nitrophenyl butyrate
-
L153Q mutant, sodium dioctyl sulfosuccinate concentration = 1 mM
1.56
p-nitrophenyl butyrate
-
T179C mutant, sodium dioctyl sulfosuccinate concentration = 2 mM
1.74
p-nitrophenyl butyrate
-
S54D mutant, sodium dioctyl sulfosuccinate concentration = 2 mM
3.57
p-nitrophenyl butyrate
-
L153Q mutant, sodium dioctyl sulfosuccinate concentration = 1.5 mM
4.33
p-nitrophenyl butyrate
-
L153Q mutant, sodium dioctyl sulfosuccinate concentration = 2 mM
0.085
p-nitrophenyl palmitate
A8QPD8
-
0.82
p-nitrophenyl valerate
A8QPD8
-
0.9
p-Nitrophenylacetate
-
-
3
p-Nitrophenylacetate
-
without surfactant
6.8
p-Nitrophenylacetate
-
cutinase I
9.7
p-Nitrophenylacetate
-
cutinase II
0.27
p-nitrophenylbutanoate
-
-
0.35
p-nitrophenylbutanoate
-
cutinase I
0.35
p-nitrophenylbutanoate
-
-
0.47
p-nitrophenylbutanoate
-
without surfactant
0.75
p-nitrophenylbutanoate
-
cutinase II
1.23
p-nitrophenylbutanoate
Q8TGB8
36C, wild-type
1.45
p-nitrophenylbutanoate
Q8TGB8
36C, mutant H173L
1.5
p-nitrophenylbutanoate
Q8TGB8
36C, mutant S103T
1.68
p-nitrophenylbutanoate
Q8TGB8
36C, mutant S103A
0.36
p-nitrophenyldecanoate
-
cutinase II
0.48
p-nitrophenyldecanoate
-
cutinase I
3.98
p-nitrophenyldecanoate
-
-
0.45
p-nitrophenyldodecanoate
-
cutinase II
0.56
p-nitrophenyldodecanoate
-
cutinase I
3.55
p-nitrophenyldodecanoate
-
-
4.54
p-nitrophenylhexadecanoate
-
-
2.27
p-nitrophenyltetradecanoate
-
-
55.3
4-nitrophenyl valerate
P52956
pH and temperature not specified in the publication
additional information
additional information
-
Km-values in presence of surfactants
-
additional information
additional information
-
comparison of kinetics of cutinases from different organisms, overview
-
additional information
additional information
-
kinetic model of transesterification of triolein and methanol, overview
-
additional information
additional information
-
Michaelis-Menten kinetics; Michaelis-Menten kinetics
-
additional information
additional information
-
kinetic analysis of the synthesis of methyl esters of tributyrin, triolein, and soybean oil by transesterification through the enzyme, Ping-Pong Bi-Bi model for the reaction mechanism, overview
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
steady-state kinetic analysis
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.4
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH and temperature not specified in the publication
2.72
4-nitrophenyl acetate
E9LVH7
pH and temperature not specified in the publication
3 - 6
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R19S
7
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant Q65E
17
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant wild-type isozyme
25
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant L183A
35
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R187K
39.5
4-nitrophenyl acetate
-
pH and temperature not specified in the publication
76
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R19S/R29N/A30V
100
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R29N/A30V
207
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R29N
211.9
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH and temperature not specified in the publication
260
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant A30V
436
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant isozyme
0.0072
4-nitrophenyl butyrate
-
pH 7.5, 25C
0.0163
4-nitrophenyl butyrate
-
pH 7.5, 25C
0.022
4-nitrophenyl butyrate
-
pH 7.5, 25C
0.072
4-nitrophenyl butyrate
-
pH 7.5, 25C
0.0845
4-nitrophenyl butyrate
-
pH 7.5, 25C
15
4-nitrophenyl butyrate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant Q65E
16
4-nitrophenyl butyrate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant wild-type isozyme
32
4-nitrophenyl butyrate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant L183A
49
4-nitrophenyl butyrate
-
pH 8.0, 70C, recombinant mutant C275A/C292A, absence of 1% PEG
79
4-nitrophenyl butyrate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R187K
80
4-nitrophenyl butyrate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R19S
136
4-nitrophenyl butyrate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R19S/R29N/A30V
173
4-nitrophenyl butyrate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R29N/A30V
183
4-nitrophenyl butyrate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant A30V
191
4-nitrophenyl butyrate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R29N
191
4-nitrophenyl butyrate
-
pH 7.5, 30C, recombinant enzyme
196
4-nitrophenyl butyrate
-
pH 8.0, 50C, recombinant mutant C275A/C292A, absence of 1% PEG
213
4-nitrophenyl butyrate
-
pH 8.0, 70C, recombinant wild-type enzyme, absence of 1% PEG
232
4-nitrophenyl butyrate
-
pH 8.0, 30C, recombinant wild-type enzyme, absence of 1% PEG
278
4-nitrophenyl butyrate
-
pH 8.0, 30C, recombinant wild-type enzyme, presence of 1% PEG
318
4-nitrophenyl butyrate
-
pH 8.0, 70C, recombinant wild-type enzyme, absence of 1% PEG
327
4-nitrophenyl butyrate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant isozyme
342
4-nitrophenyl butyrate
-
pH 8.0, 30C, recombinant mutant C275A/C292A, absence of 1% PEG
343
4-nitrophenyl butyrate
-
pH 8.0, 50C, recombinant wild-type enzyme, absence of 1% PEG
359
4-nitrophenyl butyrate
-
pH 8.0, 50C, recombinant wild-type enzyme, presence of 1% PEG
483
4-nitrophenyl butyrate
-
pH 8.0, 60C, isozyme Tfu 0882
742
4-nitrophenyl butyrate
-
pH 8.0, 60C, isozyme Tfu 0883
837
4-nitrophenyl butyrate
-
pH 8.0, 60C, recombinant cutinase FspC
187
4-nitrophenyl octanoate
-
pH 7.5, 30C, recombinant enzyme
7900
p-nitrophenyl butyrate
-
T179C mutant, sodium dioctyl sulfosuccinate concentration = 0 mM
9600
p-nitrophenyl butyrate
-
T179Cmutant, sodium dioctyl sulfosuccinate concentration = 0.5 mM
11000
p-nitrophenyl butyrate
-
L153Q mutant, sodium dioctyl sulfosuccinate concentration = 0 mM; T179C mutant, sodium dioctyl sulfosuccinate concentration = 1.5 mM
11100
p-nitrophenyl butyrate
-
T179C mutant, sodium dioctyl sulfosuccinate concentration = 1 mM
11500
p-nitrophenyl butyrate
-
T179C mutant, sodium dioctyl sulfosuccinate concentration = 2 mM
13800
p-nitrophenyl butyrate
-
wild type, sodium dioctyl sulfosuccinate concentration = 2 mM
14700
p-nitrophenyl butyrate
-
S54D mutant, sodium dioctyl sulfosuccinate concentration = 0 mM
15200
p-nitrophenyl butyrate
-
wild type, sodium dioctyl sulfosuccinate concentration = 1.5 mM
15500
p-nitrophenyl butyrate
-
wild type, sodium dioctyl sulfosuccinate concentration = 0.5 mM
15600
p-nitrophenyl butyrate
-
wild type, sodium dioctyl sulfosuccinate concentration = 0 mM
16000
p-nitrophenyl butyrate
-
L153Q mutant, sodium dioctyl sulfosuccinate concentration = 0.5 mM
17400
p-nitrophenyl butyrate
-
wild type, sodium dioctyl sulfosuccinate concentration = 1 mM
17900
p-nitrophenyl butyrate
-
L153Q mutant, sodium dioctyl sulfosuccinate concentration = 1 mM
24200
p-nitrophenyl butyrate
-
S54D mutant, sodium dioctyl sulfosuccinate concentration = 1 mM
24700
p-nitrophenyl butyrate
-
S54D mutant, sodium dioctyl sulfosuccinate concentration = 0.5 mM
25200
p-nitrophenyl butyrate
-
S54D mutant, sodium dioctyl sulfosuccinate concentration = 1.5 mM
25800
p-nitrophenyl butyrate
-
L153Q mutant, sodium dioctyl sulfosuccinate concentration = 1.5 mM
28500
p-nitrophenyl butyrate
-
L153Q mutant, sodium dioctyl sulfosuccinate concentration = 2 mM
32100
p-nitrophenyl butyrate
-
S54D mutant, sodium dioctyl sulfosuccinate concentration = 2 mM
230
p-Nitrophenylacetate
-
without surfactant
0.25
p-nitrophenylbutanoate
Q8TGB8
36C, mutant H173L; 36C, mutant S103T
0.66
p-nitrophenylbutanoate
Q8TGB8
36C, wild-type
1.5
p-nitrophenylbutanoate
Q8TGB8
36C, mutant S103A
539
p-nitrophenylbutanoate
-
without surfactant
238
tributyrin
-
pH 7.5, 30C, recombinant enzyme
509
tricaprylin
-
pH 7.5, 30C, recombinant enzyme
172
triolein
-
pH 7.5, 30C, recombinant enzyme
18
4-nitrophenyl palmitate
-
pH 7.5, 30C, recombinant enzyme
additional information
additional information
-
turnover numbers in presence of surfactants
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00000167
4-nitrophenyl acetate
-
in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol
418
0.00004217
4-nitrophenyl acetate
-
in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol
418
0.48
4-nitrophenyl acetate
-
pH 8.0, 25C, recombinant enzyme
418
5
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant Q65E
418
9
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant wild-type isozyme
418
13
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant L183A
418
30
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R19S
418
42.4
4-nitrophenyl acetate
Fusarium solani pisi
P00590
pH and temperature not specified in the publication
418
44
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R187K
418
65
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R19S/R29N/A30V
418
76
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R29N/A30V
418
153
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant A30V
418
159
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant mutant R29N
418
291
4-nitrophenyl acetate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant isozyme
418
0.00000043
4-nitrophenyl butyrate
-
in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol
522
0.0000582
4-nitrophenyl butyrate
-
in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol
522
0.0053
4-nitrophenyl butyrate
-
pH 7.5, 25C
522
0.0093
4-nitrophenyl butyrate
-
pH 7.5, 25C
522
0.0162
4-nitrophenyl butyrate
-
pH 7.5, 25C
522
0.029
4-nitrophenyl butyrate
-
pH 7.5, 25C
522
0.0567
4-nitrophenyl butyrate
-
pH 7.5, 25C
522
2.2
4-nitrophenyl butyrate
-
pH 8.0, 25C, recombinant enzyme
522
5
4-nitrophenyl butyrate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant wild-type isozyme
522
150
4-nitrophenyl butyrate
-
pH 8.0, 60C, isozyme Tfu 0883
522
258
4-nitrophenyl butyrate
-
pH 8.0, 70C, recombinant mutant C275A/C292A, absence of 1% PEG
522
402
4-nitrophenyl butyrate
-
pH 7.5, 30C, recombinant enzyme
522
425
4-nitrophenyl butyrate
E9LVH8, E9LVH9
pH 7.0, 25C, recombinant isozyme
522
700
4-nitrophenyl butyrate
-
pH 8.0, 60C, isozyme Tfu 0882
522
888
4-nitrophenyl butyrate
-
pH 8.0, 70C, recombinant wild-type enzyme, absence of 1% PEG
522
1046
4-nitrophenyl butyrate
-
pH 8.0, 30C, recombinant wild-type enzyme, presence of 1% PEG
522
1050
4-nitrophenyl butyrate
-
pH 8.0, 30C, recombinant wild-type enzyme, absence of 1% PEG
522
1090
4-nitrophenyl butyrate
-
pH 8.0, 50C, recombinant mutant C275A/C292A, absence of 1% PEG
522
1295
4-nitrophenyl butyrate
-
pH 8.0, 70C, recombinant wild-type enzyme, absence of 1% PEG
522
1311
4-nitrophenyl butyrate
-
pH 8.0, 50C, recombinant wild-type enzyme, presence of 1% PEG
522
1350
4-nitrophenyl butyrate
-
pH 8.0, 50C
522
1370
4-nitrophenyl butyrate
-
pH 8.0, 30C, recombinant mutant C275A/C292A, absence of 1% PEG
522
1630
4-nitrophenyl butyrate
-
pH 8.0, 50C, recombinant wild-type enzyme, absence of 1% PEG
522
2840
4-nitrophenyl butyrate
-
pH 8.0, 50C
522
3200
4-nitrophenyl butyrate
-
pH 8.0, 60C, recombinant cutinase FspC
522
7.7
4-nitrophenyl caprylate
-
pH 8.0, 25C, recombinant enzyme
4683
0.0000023
4-nitrophenyl hexanoate
-
in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol
1191
0.000023
4-nitrophenyl hexanoate
-
in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol
1191
6.14
4-nitrophenyl laurate
-
pH 8.0, 25C, recombinant enzyme
2511
6.4
4-nitrophenyl myristate
-
pH 8.0, 25C, recombinant enzyme
11051
900
4-nitrophenyl octanoate
-
pH 7.5, 30C, recombinant enzyme
1486
6.2
4-nitrophenyl palmitate
-
pH 7.5, 30C, recombinant enzyme
1523
0.00001017
4-nitrophenyl valerate
-
in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol
4137
0.000053
4-nitrophenyl valerate
-
in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol
4137
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.44
sodium dioctyl sulfosuccinate
-
L153Q mutant
0.46
sodium dioctyl sulfosuccinate
-
T179C mutant
0.72
sodium dioctyl sulfosuccinate
-
wild type
1.38
sodium dioctyl sulfosuccinate
-
S54D mutant
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.004
A8QPD8
4-nitrophenyl palmitate, esterase activity of the recombinant THCUT1 protein against different chromogenic substrates
0.12
A8QPD8
in 1% olive oil, esterase activity values decreased after 4 h of incubation and are 1.8, 1.1, and 0.12 micromol/min/mg against 4-nitrophenyl palmitate, at 4, 8 and 24 h
0.218
-
pH 8.0, 50C, purified recombinant His-tagged enzyme, 4-nitrophenyl (16-methyl sulfoyl ester) hexadecanoate
0.25
A8QPD8
4 h cultures against 4-nitrophenyl palmitate
0.395
-
pH 8.0, 50C, purified recombinant His-tagged enzyme, 4-nitrophenyl (16-methyl sulfone ester) hexadecanoate
0.4
A8QPD8
4-nitrophenyl valerate, esterase activity of the recombinant THCUT1 protein against different chromogenic substrates
0.74
A8QPD8
4-nitrophenyl butyrate, esterase activity of the recombinant THCUT1 protein against different chromogenic substrates
0.85
A8QPD8
in 1% olive oil, esterase activity values decreased after 4 h of incubation and are 11.4, 5.4, and 0.85 micromol/min/mg against 4-nitrophenyl butyrate, at 4, 8 and 24 h
1.1
A8QPD8
in 1% olive oil, esterase activity values decreased after 4 h of incubation and are 1.8, 1.1, and 0.12 micromol/min/mg against 4-nitrophenyl palmitate, at 4, 8 and 24 h
1.2
A8QPD8
supernatant from 8 h culture on 0.2% cutin monomer 16-hydroxy-hexadecanoic acid shows slightly higher values against 4-nitrophenyl palmitate
1.3
A8QPD8
supernatant from 8 h culture on 0.05% cutin monomer 16-hydroxy-hexadecanoic acid shows slightly higher values against 4-nitrophenyl palmitate
1.8
A8QPD8
in 1% olive oil, esterase activity values decreased after 4 h of incubation and are 1.8, 1.1, and 0.12 micromol/min/mg against 4-nitrophenyl palmitate, at 4, 8 and 24 h
2.77
P41744
carrier bound CUTAB1 with tributyrin as substrate, in 40 ml of 50 mM potassium phosphate buffer, pH 5.5 containing 25% ethanol, at 8C, for 40 H
2.84
A8QPD8
4-nitrophenyl acetate, esterase activity of the recombinant THCUT1 protein against different chromogenic substrates
4.2
A8QPD8
4 h cultures against 4-nitrophenyl butyrate (6.6 and 4.2 micromol/min/mg)
5.4
A8QPD8
in 1% olive oil, esterase activity values decreased after 4 h of incubation and are 11.4, 5.4, and 0.85 micromol/min/mg against 4-nitrophenyl butyrate, at 4, 8 and 24 h
6.6
A8QPD8
4 h cultures against 4-nitrophenyl butyrate (6.6 and 4.2 micromol/min/mg)
7.5
A8QPD8
supernatant from 8 h culture on 0.2% cutin monomer 16-hydroxy-hexadecanoic acid shows higher activity values against 4-nitrophenyl butyrate
9.8
A8QPD8
supernatant from 8 h culture on 0.05% cutin monomer 16-hydroxy-hexadecanoic acid shows higher activity values against 4-nitrophenyl butyrate
10
P41744
crude extract, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
11.4
A8QPD8
in 1% olive oil, esterase activity values decreased after 4 h of incubation and are 11.4, 5.4, and 0.85 micromol/min/mg against 4-nitrophenyl butyrate, at 4, 8 and 24 h
17
P41744
1.6fold purified enzyme, with 4-nitrophenyl palmitate as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic; wild-type, with 4-nitrophenyl palmitate as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
30
P41744
wild-type, with tripalmitin as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
40
-
cutinase-tryptophan,proline4, after 72 h of Saccharomyces cerevisae cultivation
41
P41744
wild-type, with methyl acetate as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
45
Q9SZW7
at 30C
47
P41744
wild-type, with tristearin as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
66
P41744
mutant A84F, with tripalmitin as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
77
P41744
mutant A84F, with tristearin as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
114
-
purified recombinant enzyme, pH 8.0, 25C
125
P41744
wild-type, with ethyl caprylate as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic; wild-type, with methyl caproate as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
129
P41744
wild-type, with methyl caprylate as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
145
P41744
wild-type, with methyl myristate as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
157
P41744
wild-type, with methyl propionate as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
161
P41744
wild-type, with methyl decanoate as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
170
-
lyophilized cutinase, pH 8.0, 30C
188
P41744
mutant A84F, with 4-nitrophenyl palmitate as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
197
P41744
wild-type, with methyl laurate as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
200
-
cutinase-tryptophan,proline2, after 72 h of Saccharomyces cerevisae cultivation
257
P41744
wild-type, with methyl butyrate as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
281
P41744
wild-type, with ethyl butyrate as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
350
-
wild type, after 72 h of Saccharomyces cerevisae cultivation
446.2
-
purified recombinant alpha-hemolysin-enzyme, substrate 4-nitrophenyl butyrate, pH 8.0, 50C
454
P41744
wild-type, with triolein as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
542.5
-
pH 8.0, 50C, purified recombinant His-tagged enzyme, substrate 4-nitrophenyl butyrate
586
P41744
mutant A84F, with triolein as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
643.4
-
pH 8.0, 50C, purified recombinant His-tagged enzyme, substrate 4-nitrophenyl butyrate
948
P41744
mutant A84F, with 4-nitrophenyl butyrate as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
1057
P41744
wild-type, with 4-nitrophenyl butyrate as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
1286
P41744
wild-type, with tricaprylin as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
2019
P41744
mutant A84F, with tricaprylin as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
3302
P41744
wild-type, with tributyrin as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
4394
P41744
mutant A84F, with tributyrin as substrate, in 0.1 M Tris-HCl buffer, pH 8.0 with 0.5% (v/v) Triton X-100 and 0.1% (w/v) gum arabic
5359
-
substrate 4-nitrophenyl butyrate, recombinant enzyme, pH 8.0, 37C
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
Assay of enzymatic activity of the fusion mutant of cutinase (RpoS-CUT) shows the same selective bioactivity as native cutinase to degrade p-nitrophenyl butyrate (PNB) but not to degrade p-nitrophenyl butyrate.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.1 - 4.6
S4VCH4
substrate tritiated cutin, recombinant enzyme
4.7 - 5.2
S4VCH4
substrate 4-nitrophenyl butyrate, recombinant enzyme
5 - 6.5
-
broad optimum
5
-
assay at
7
-
and a second optimum at 8.0, but retains activity over a wide pH range
7
E9LVH8, E9LVH9
assay at; assay at
7
A7EQQ8
assay at
7.5
-
assay at
8
-
hydrolysis of cutin or p-nitrophenylbutyrate
8
-
and a second optimum at 7.0, but retains activity over a wide pH range
8
-
assay at
8
-
assay at; assay at
8
-
recombinant alpha-hemolysin-enzyme
8.5 - 10.5
-
-
8.5
-
study of thermal unfolding of enzyme as a function of pH-value in different buffers. At pH-optimum of 8.5, enzyme also has high thermal stability
10
Fusarium roseum, Fusarium solani
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 7.5
S4VCH4
the enzyme is active over a broad pH range, 25% of maximal activity at pH 3.0
3.5 - 7.5
-
activity range, no activity at pH 8.0 and pH 2.0
5 - 9
-
has activity superior to lipases
6 - 11
-
activity range, inactive below
6 - 9
-
pH dependence of enzyme activity is determined between pH 6.0 and 9.0
6.8 - 9
-
activity range; activity range
7 - 9
P41744
at both, room temperature and 40C
7 - 9
Q9SZW7
-
8 - 10
-
non-tagged and the C-terminal tagged cutinases
8 - 11
-
pH 8.0: about 60% of maximal activity, pH 11.0: about 50% of maximal activity
8 - 11
Fusarium roseum
-
pH 8.0: about 40% of maximal activity, pH 11.0: about 75% of maximal activity
additional information
-
evaluation of temperature and pH effect on protein conformation and dynamics by study of fluorescence of the single tryptophan
additional information
-
retains activity over a wide pH range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
assay at; assay at
25
S4VCH4
assay at, 4-nitrophenyl ester substrates
25
E9LVH8, E9LVH9
assay at; assay at
25
-
recombinant wild-type enzyme
30
-
displays an optimal temperature at 30C for triolein and 40C for 4-nitrophenyl butyrate
30
-
hydrolysis of triacylglyceride substrates
30
-
assay at
30
-
recombinant mutant N177D
37
-
assay at
37
-
assay at
37
A7EQQ8
assay at
40
-
activity assay at
40
-
displays an optimal temperature at 30C for triolein and 40C for 4-nitrophenyl butyrate
40
S4VCH4
assay at, tritiated cutin substrate
40
-
transesterification with substrate 6-mercapto-1-hexanol
40
-
assay at
60
-
wild-type enzyme
70
-
epsilon-caprolactone ring-opening polymerizations
70
-
immobilized enzyme
70
-
recombinant alpha-hemolysin-enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 65
-
activity range, inactive above
20 - 70
-
temperature dependence of enzyme activity is determined between 20 and 70C
30 - 70
-
activity range
35 - 45
-
non-tagged and the C-terminal tagged cutinases
40 - 50
-
-
40 - 80
-
activity range; activity range
60 - 80
-
60C: about 25% of maximal activity, 80C: less than 10% of maximal activity
additional information
-
evaluation of temperature and pH effect on protein conformation and dynamics by study of fluorescence of the single tryptophan
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.47
A7EQQ8
sequence calculation
8
P00590
-
8.1
A6N6J6
calculated from sequence
8.2
Q8TGB8
mature form, calculated
8.4
Q8TGB8
precursor protein, calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Q00298
ungerminated
Manually annotated by BRENDA team
Botrytis cinerea Pser.: Fr.
-
-
-
Manually annotated by BRENDA team
Fusarium roseum
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Q9SZW7
in mature pollen grains within non-dehiscent anthers
Manually annotated by BRENDA team
Q9SZW7
pollen tubes that are germinating on the stigma
Manually annotated by BRENDA team
Q9SZW7
at the zone of lateral root emergence
Manually annotated by BRENDA team
Q9SZW7
CDEF1 is secreted to the extracellular space in leaves
Manually annotated by BRENDA team
additional information
-
fermentation conditions for cutinase production with a mutant of Thermobifida fusca ATCC 27730 are studied
Manually annotated by BRENDA team
additional information
A6N6J6
microconidium
Manually annotated by BRENDA team
additional information
-
cultures are grown on agar plates at pH 4.0 with the cutinase model substrate polycaprolactone as a carbon source
Manually annotated by BRENDA team
additional information
Fusarium solani pisi
P00590
optimization of culture conditions for heterologous expression of the enzyme, overview
Manually annotated by BRENDA team
additional information
-
production of Fusarium oxysporum cutinase by solid-state fermentation using Brazilian agricultural by-products, with maximum yield 21.7 U/mL after 120 h of fermentation at 28.3C
Manually annotated by BRENDA team
additional information
-
microconidium
-
Manually annotated by BRENDA team
additional information
-
cultures are grown on agar plates at pH 4.0 with the cutinase model substrate polycaprolactone as a carbon source
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
110000 Da enzyme
Manually annotated by BRENDA team
Botrytis cinerea Pser.: Fr.
-
110000 Da enzyme
-
Manually annotated by BRENDA team
Botrytis cinerea Pser.: Fr.
-
40800 Da enzyme
-
Manually annotated by BRENDA team
Fusarium roseum
-
-
-
Manually annotated by BRENDA team
Fusarium solani pisi
P00590
-
-
Manually annotated by BRENDA team
Burkholderia cepacia NRRL B 2320, Thermobifida fusca DSM 44342, Sirococcus conigenus VTT D-04989, Aspergillus niger CBS 513.88
-
-
-
-
Manually annotated by BRENDA team
-
110000 Da enzyme, bound to membrane or cell wall
Manually annotated by BRENDA team
Botrytis cinerea Pser.: Fr.
-
110000 Da enzyme, bound to membrane or cell wall
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Fusarium solani subsp. pisi
Hypocrea jecorina (strain QM6a)
Hypocrea jecorina (strain QM6a)
Hypocrea jecorina (strain QM6a)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6982
-
N-terminal fragment, electrospray ionization Q-TOF mass spectrometric analysis
690559
12140
-
C-terminal fragment, Ala(95) - His(204), electrospray ionization Q-TOF mass spectrometric analysis
690559
12270
-
C-terminal fragment, Ala(95) - His(205), electrospray ionization Q-TOF mass spectrometric analysis
690559
18800
-
around, electrospray ionization Q-TOF mass spectrometric analysis gives two masses 18726.0 Da and 18863.0 Da
690559
20000
-
SDS-PAGE
690559
20400
-
cutinase II, equilibrium sedimentation
208318
21010
-
after preincubation with 20 mM diethyl p-nitrophenyl phosphate, the peak at 21010 Da represents the nonmodified H204N mutant, mass spectrometry; H204N mutant, mass spectrometry; H204N site-directed mutant, mass spectrometry
693678
21030
-
wild type, mass spectrometry; wild-type, mass spectrometry
693678
21170
-
after preincubation with 20 mM diethyl p-nitrophenyl phosphate, the peak at 21168 Da represents the covalently modified wild-type cutinase, mass spectrometry
693678
21700
-
gel filtration
208327
21700
A6N6J6
calculated from sequence
710013
21800
-
cutinase I and II, gel filtration
208318
22000
-
molar mass found for the wild type cutinase and its mutants is identical
691090
23400
-
cutinase I, equilibrium sedimentation
208318
29000
A8QPD8
SDS-PAGE
691941
30000
-
gel filtration
208331
30100
-
sequence analysis
710130
32000
-
recombinant isozymes Tfu 0882 and Tfu 0883, gel filtration
715944
36400
-
sequence analysis
710130
38700
-
sequence analysis
710130
39200
-
sequence analysis
710130
39200
-
sequence analysis
710267
41200
-
sequence analysis
710130
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 25000, SDS-PAGE
?
-
x * 22000, SDS-PAGE
?
-
x * 18600, protein bands of 18600 Da and 20800 Da show cutinase activity
?
Fusarium roseum
-
x * 24300, SDS-PAGE
?
-
x * 21800, cutinase I, SDS-PAGE
?
-
x * 40800, soluble enzyme, SDS-PAGE
?
-
x * 20800, protein bands of 18600 Da and 20800 Da show cutinase activity
?
-
x * 21800, and a smaller band of 10600 Da, cutinase II, SDS-PAGE
?
-
x * 110000, enzyme from cell wall or membrane, SDS-PAGE
?
Q8TGB8
x * 20227, precursor protein, x * 18134, mature form, calculated
?
-
x * 22800, x * 24900, two differently glycosylated forms, SDS-PAGE
?
-
x * 38700, calculated from sequence
?
-
x * 30100, calculated from sequence
?
-
x * 36400, calculated from sequence
?
-
x * 39200, calculated from sequence
?
-
x * 39200, calculated from sequence
?
-
x * 41200, calculated from sequence
?
-
x * 39000, recombinant His-tagged enzyme, SDS-PAGE
?
A7EQQ8
x * 20400, sequence calculation, x * 45000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 22800, about, sequence calculation, x * 25000-35000, glycosylated recombinant enzyme, SDS-PAGE
?
-
x * 26250, mass spectrometry, x * 26500, recombinant enzyme, SDS-PAGE
?
Botrytis cinerea Pser.: Fr.
-
x * 40800, soluble enzyme, SDS-PAGE, x * 110000, enzyme from cell wall or membrane, SDS-PAGE
-
?
Burkholderia cepacia NRRL B 2320
-
x * 26250, mass spectrometry, x * 26500, recombinant enzyme, SDS-PAGE
-
?
-
x * 22800, about, sequence calculation, x * 25000-35000, glycosylated recombinant enzyme, SDS-PAGE
-
monomer
-
1 * 23000, SDS-PAGE
monomer
-
1 * 30000, SDS-PAGE
monomer
-
1 * 21400, cutinase I and II, SDS-PAGE
monomer
-
crystallography
monomer
P41744
1 * 24000, SDS-PAGE, glycosylated CUTAB1. 1 * 20000, SDS-PAGE, non-glycosylated CUTAB1
monomer
-
1 * 29000, isozymes Tfu 0882 and Tfu 0883, SDS-PAGE, 1 * 29220, isozyme Tfu 0882, sequence calculation, 1 * 28997, isozyme Tfu 0883, sequence calculation
additional information
-
cutinase isozyme structure comparisons of cutinases, overview
additional information
-
structure analysis, structure comparisons of recombinant isozymes Cut1 and Cut2 during denaturation and unfolding, overview
additional information
Thermobifida cellulosilytica DSM44535
-
cutinase isozyme structure comparisons of cutinases, overview
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
P41744
the glycosylated form of CUTAB1 has a MW of 24000 Da. The non-glycosylated form of CUTAB1 has a MW of 20000 Da
glycoprotein
-
the enzyme has six putative glycosylation sites
glycoprotein
-
two differently glycosylated forms of 22800 and 24900 Da
no glycoprotein
S4VCH4
the enzyme contains no N- or O-glycosylation sites
no glycoprotein
Sirococcus conigenus VTT D-04989
-
the enzyme contains no N- or O-glycosylation sites
-
glycoprotein
-
contains 5.4% carbohydrate
glycoprotein
-
the enzyme has six putative glycosylation sites
-
additional information
Q8TGB8
sequence contains a 20 amino-acid secretory signal, one potential N-linked glycosilation site, a protein kinase C phosphorylation site, a lipase active serine and a cutinase active serine
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
PDB IDs 3GBS, 3PQD, X-ray diffraction structure determination at 1.75 A resolution
P52956
to 1.75 A resolution. Alpha/beta fold hallmarked by a central beta-sheet of 5 parallel strands surrounded by 10 alpha-helices. An additional disulfide bond and a topologically favored catalytic triad (Ser126, Asp181, and His194), with a continuous and deep groove
-
PDB ID 2CZQ, X-ray diffraction structure determination at 1.05 A resolution
Q874E9
crystallization of native enzyme, 27 mutant enzymes and 4 covalently inhibited complexes, crystallizes in 8 different crystal forms
-
PDB IDs 1CUS and 2CUT, X-ray diffraction structure determination
Fusarium solani pisi
P00590
; in the absence and in the presence of the inhibitors diethyl p-nitrophenyl phosphate (belongs to space group P21) and 3-phenethylthio-1,1,1-trifluoropropan-2-one (belongs to space group P212121), to resolutions of 2.6 and 2.3 A, respectively. Apo-cutinase, 1.9 A resolution, belongs to space group P41212 with one subunit in the asymmetric unit with unit cell parameters a = 60, b = 60, c = 86 A, respectively. The catalytic triad (Ser136, Asp191, and His204) adopts an unusual configuration with the putative essential histidine His204 swung out of the active site into a position where it is unable to participate in catalysis, with the imidazole ring 11 A away from its expected position
-
crystallization and preliminary X-ray analysis of cutinase-inhibitor complexes, resolution beyond 1.6 A
-
PDB IDs: two inhibited structures 3DEA and 3DD5 and one uninhibited structure 3DCN
-
PDB ID: 3VIS, X-ray diffraction structure determination at 1.76 A resolution
E9LVH7
purified recombinant C275A/C292A mutant enzyme, sitting drop vapor diffusion method, from 20% w/v PEG 3350 and 0.2 M sodium thiocyanate, 20C, 2 weeks, X-ray diffraction structure determination and analysis at 1.5 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 6
-
purified recombinant enzyme, 40C, 24 h, completely stable at
729656
4 - 11
-
purified recombinant alpha-hemolysin-cutinase retains more than 90% of its maximal activity after incubation at 37C for 24 h in this pH range, which is superior to that of wild-type cutinase
730328
6 - 11
-
recombinant enzyme, 25C, stable at
730094
7
-
purified recombinant enzyme, 40C, 24 h, loss of 70% activity
729656
additional information
-
retains activity over a wide pH range
690559
additional information
-
the enzyme is unstable and functions poorly at high temperatures as well as at acidic pH conditions, biophysical parameters of cutinase as a function of pH, overview
713927
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 25
S4VCH4
purified recombinant enzyme, pH 4.5, completely stable at
729077
22 - 60
-
purified recombinant enzyme, stable up to 50C with over 90% residual activity after 48 h of incubation, while the stability strongly decreases when incubated at 60C
729653
35
-
pH 8, in a water bath with agitation, half-life without additives: 45 days, half-life with 7.5% N,N-dimethylacetamide: 48 days, half-life with 15% N,N-dimethylacetamide: 159 days, half-life with 25% N,N-dimethylacetamide: 4 days, half-life with 50% N,N-dimethylacetamide: 0.4 day, half-life in presence of 25% glycerol: 134 days, half-life with 25% sorbitol: 113 days, half-life with 25% xylitol: 31 days, half-life in presence of 50% ethylene glycol: 29 days, half-life in presence of 50% polyethylene glycol: 23 days
678861
37
-
purified recombinant enzyme, residual activity is over 75% after 125 h; purified recombinant enzyme, residual activity is over 75% after 125 h
729000
37
-
purified recombinant alpha-hemolysin-cutinase retains more than 90% of its maximal activity after incubation at pH 4.0-11.0 for 24 h, which is superior to that of wild-type cutinase
730328
38.5
-
50% unfolding at pH 10.9; 50% unfolding at pH 10.9, presence of 0.5 M trehalose
666084
40 - 60
-
thermostability of Fusarium solani pisi cutinase is evaluated at both 40 and 60C. It exhibits a similar initial increase at 40C, but a simple exponential decay at 60C. 50% of activity retained after 85 h at 40C or after 5 min at 60C
693130
40
P00590
0.08 mM cutinase, pH 8.0, no additive, Tm-value is 40.3C
678741
40
P41744
retains 84% of its initial activity at 40C and pH 8.0 for 5 days
707267
40
-
purified recombinant enzyme, pH 3.0-6.0, 24 h, completely stable at
729656
42
-
50% unfolding at pH 10.5; 50% unfolding at pH 10.5, presence of 0.5 M trehalose
666084
42
S4VCH4
purified recombinant enzyme, pH 4.5, half-life is 46-76 h
729077
48
P00590
0.08 mM cutinase or 0.005 mM cutinase, pH 8.0, 2 M urea, Tm-value 47.5C
678741
49
-
at pH 4.5, cutinase unfolds with a Tm of 49.3C. point. The Tm value increases 7.2 C in the presence of 1 M of trehalose
678748
49.8
-
50% unfolding at pH 4.5; 50% unfolding at pH 4.5, presence of 0.5 M trehalose
666084
50
-
enzyme retains 80% of its activity after 20 h incubation at 50C, but residual activity decreases sharply at 60C
690559
50
-
recombinant enzyme, pH 8.0, 30 min, stable at
730094
50
-
purified wild-type enzyme and mutant L172K retain 10% activity after 2 h, mutant N177D retains 30% activity after 2 h with half-life of 30 min
730865
52
P00590
0.06 mM cutinase, pH 8.0, Tm-value is 52.0C
678741
52.6
-
50% unfolding at pH 9.2; 50% unfolding at pH 9.2, presence of 0.5 M trehalose
666084
55
P00590
0.08 mM cutinase, pH 8.0, 20 mM 0.5 M L-Arg, Tm-value
678741
55
-
purified recombinant enzyme, residual activity is over 38% after 125 h; purified recombinant enzyme, residual activity is over 38% after 125 h
729000
55
S4VCH4
purified recombinant enzyme, pH 4.5, half-life is 40 min
729077
56
P00590
0.005 mM cutinase, pH 8.0, 20 mM 0.5 M L-Arg, Tm-value is 56.4C
678741
56
-
melting temperature. Dramatic loss in activity at 40 C, 40% drop at 30 C, continuous decline in activity as a function of increasing temperature
708872
57
P00590
0.04 mM cutinase, pH 8.0, Tm-value is 57.3C
678741
57
-
Tm-value in prresence of 1 mM trehalose
678748
59
P00590
0.0001 mM cutinase, pH 8.0, Tm-value is 59.3C; 0.005 mM cutinase, pH 8.0, Tm-value is 59.3C
678741
59
-
melting temperature. Maintains a high level of activity at 40 C
708872
65
S4VCH4
purified recombinant enzyme, pH 4.5, half-life is 30 min
729077
80
S4VCH4
denaturation of recombinant enzyme by heating the protein sample to 80 C is to a great extent reversible
729077
85
S4VCH4
purified recombinant enzyme, pH 4.5, half-life is 24 min
729077
additional information
-
study of thermal unfolding of enzyme as a function of pH-value in different buffers. At pH-optimum of 8.5, enzyme also has high thermal stability
665756
additional information
P00590
ANS binds strongly to native cutinase as a noncompetitive inhibitor with up to 5 ANS per cutinase molecule. The first ANS molecule stabilizes cutinase. The last 4 ANS molecules decrease Tm-value by up to 7C
678741
additional information
-
trehalose delays thermal unfolding, thus increasing the temperature at the mid-point of unfolding by 7.2C
678748
additional information
-
thermal stability of Humicola insolens cutinase in aqueous SDS. SDS stabilizes noticeably against irreversible aggregation
681595
additional information
-
presence of hexanol and the low water content lead to the enzyme stabilization in the interior of the micelles, increasing its thermostability
707009
additional information
Q9SZW7
activity is reduced to less than 10% of the maximum activity by heating for 10 min at 99C
710267
additional information
-
the enzyme is unstable and functions poorly at high temperatures as well as at acidic pH conditions, differential scanning calorimetry thermograms of cutinase, overview
713927
additional information
-
thermal denaturation-induced unfolding of LC-cutinase is analyzed at pH 8.0 by circular dichroism spectroscopy, kinetics of transition of the thermal denaturation, overview. The disulfide bond formed by Cys275 and Cys292 contributes not only to the thermodynamic stability but also to the kinetic stability of LC-cutinase
729249
additional information
-
first order rate constants in thermal inactivation, overview
730129
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ANS binds strongly to native cutinase as a noncompetitive inhibitor with up to 5 ANS per cutinase molecule. The first ANS molecule stabilizes cutinase. The last 4 ANS molecules decrease Tm by up to 7C
P00590
encapsulation of enzyme in bis(2-ethylhexyl) sodium sulfosuccinate reverse micelles induces unfolding at room temperature, presence of 1-hexanol delays or even prevents unfolding
-
half-life time of cutinase at 35C, pH 8, in a water bath with agitation, increases by 3.5fold with the addition of 15% N,N-dimethylacetamide and by 3fold with 1 M glycerol
-
in bis(2-ethylhexyl) sodium sulfosuccinate reverse micelles, enzyme unfolds with mono-exponential rates, indicating a two-state process. After unfolding in reverse micelles, enzyme is less destabilised than in guanidinium hydrochloride-denatured state, which is supported by fluorescence data. NMR studies indicate a molten globule structure
-
micelle-forming short-chain phospholipids significantly reduce cutinase stability (both below and above the critical micelle concentration) and rates of folding (only above critical micelle concentration), trapping cutinase in an inactive state which only regains activity over hours to days, rather than the few seconds required for refolding in the absence of detergent. Destabilization decreases with increasing chain length, and increases with critical micelle concentration, indicating that monomers and micelles cooperate in destabilizing cutinase
-
stable in presence of hexadecyltrimethyl-ammoniumbromide
-
trehalose delays thermal unfolding, thus increasing the temperature at the mid-point of unfolding by 7.2C
-
unfolding of enzyme induced by guanidinium hydrochloride shows a stable intermediate, molten globule
-
unstable in presence of sodium bis(2-ethylhexyl)ester sulfosuccinic acid, unfolding of protein structure
-
in bis(2-ethylhexyl) sodium sulfosuccinate reverse micelles, enzyme unfolds with mono-exponential rates, indicating a two-state process. After unfolding in reverse micelles, enzyme is less destabilised than in guanidinium hydrochloride-denatured state, which is supported by fluorescence data. NMR studies indicate a molten globule structure
-
Using RNA polymerase sigma factor (RpoS) or glutathione transferase as fusion expression partners, the solubility of cutinase significantly increases.
-
the disulfide bond formed by Cys275 and Cys292 contributes not only to the thermodynamic stability but also to the kinetic stability of LC-cutinase
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
vinyl acetate
-
has a stabilizing effect on the enzyme activity
additional information
-
hexanol has a stabilizing effect on the enzyme activity in reverse micelles
additional information
-
stability of the cutinase in different organic solvents. The cutinase is incubated with 75% v/v of organic solvent in assay buffer at 20C for 18 h, overview
additional information
-
stability of the cutinase in different organic solvents. The cutinase isozymes are incubated with 75% v/v of organic solvent in assay buffer at 20C for 18 h, overview
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
22C, high stability
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild-type and mutants purified by ultrafiltration, wild-type further purified by hydrophobic interaction chromatography and ammonium sulfate precipitation, 1.6fold with a yield of 70%
P41744
on Ni2+ affinity column
Q9SZW7
native extracellular enzyme 1.42fold to homogeneity by ammoium sulfate fractionation, cation exchange chromatography, and two steps of gel filtration
-
by immobilized metal affinity chromatography exploiting a C-terminal His-tag
-
optimization and evaluation of foam fractionation as purification method to purify an extracellular cutinase from untreated supernatant of mycelium of submerged cultures of the basidiomycete Coprinopsis cinerea as a model enzyme, detailed overview
-
; by nickel-affinity chromatography
-
by centrifugation, ultrafiltration and on Ni2+ column
-
non-tagged and the C-terminal tagged cutinases, by diafiltration
-
osmotic shock, acid precipitation, dialysis and two sequential anion exchange chromatographic steps, followed by a final dialysis and subsequently freeze-dried. Cutinase purity is confirmed by 12.5% SDS-PAGE
-
; by ion-exchange chromatography
-
recombinant enzyme partially 293fold from Pichia pastoris strain X-33 by ultrafiltration
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain Origami B (DE3) by nickel affinity chromatography, tag cleavage by recombinant enterokinase, and anion exchange chromatography
-
recombinant enzyme from Pichia pastoris strain X-33culture supernatant by tangential flow filtration and filter cell-based ultrafiltration
-
affinity purification
-
His-tagged protein, expressed in Pichia pastoris
Q8TGB8
recombinant cutinase FspC from Bacillus subtilis
-
study of enzyme partition in a 20% polyethylene glykol/15% phosphate two-phase system. Specific interaction of butyrate to the active site of enzyme, enzyme-butyrate complex is over two times the size of the free enzyme
-
purification of his-tagged protein using Ni2+-affinity chromatography
-
purification includes cationic Expanded Bed Adsorption (EBA) followed by hydrophobic interaction chromatography (HIC)
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 by nickel affinity and anion exchange chromatography and gel filtration
A7EQQ8
recombinant C-terminally His-tagged enzyme from Pichia pastoris by nickel affinity chromatography
S4VCH4
recombinant enzyme from Escherichia coli strain BL21-Gold(DE3); recombinant enzyme from Escherichia coli strain BL21-Gold(DE3)
E9LVH8, E9LVH9
recombinant C-terminally His-tagged wild-type and mutant cutinases lacking the signal peptide sequence 1.9fold from Escherichia coli strain BL21(DE3) culture supernatant by ammonium sulfate fractionation and nickel affinity chromatography
-
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) culture supernatant by nickel affinity chromatography to homogeneity; recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) culture supernatant by nickel affinity chromatography to homogeneity
-
recombinant cutinase isozymes Tfu 0882 and Tfu 0883 from Escherichia coli strain BL21(DE3)
-
recombinant extracellular enzyme 2.0fold from culture supernatant by ammonium sulfate precipitation and two different steps of anion exchange chromatography
-
recombinant extracellular wild-type and mutant enzymes without a putative N-terminal signal peptide (Met1-Ala34) and Gln35 from Escherichia coli
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
PCR product digested with EcoRI and NotI, and ligated in corresponding sites of the linearized pPICZalphaA vector. Transformation of Escherichia coli DH5alpha cells. Wild-type and mutants heterologously expressed in Pichia pastoris X-33 cells under the control of the methanol-inducible AOX1 promoter
P41744
transgenic Arabidopsis plants expressing GFP-CDEF1 fusion protein driven by the 35S promoter. CDEF1 expressed with a 6 x His tag at its C-terminus in suspension cultures of BY-2 tobacco cells
Q9SZW7
codon optimized cutinase gene anig5, subcloning of C-terminally His-tagged enzyme in Escherichia coli strain XL1-Blue and recombinant expression in Pichia pastoris after selection from 38 strains for production, screening and pH-Profiling of the cutinase activities of the culture supernatants, overview
-
two genes, DNA and amino acid sequence determination and analysis, phylogenetic tree, recombinant expression in Escherichia coli strain BL21(DE3), production and assay method optimization, overview
-
cloned and expressed in Trichoderma reesei
-
amplified DNA fragments cloned into the pGEM-T vector, cut1 isolated from a lambdaEMBL3 genomic library
A6N6J6
cloned in pMa5-L and overexpressed in Escherichia coli
-
cutinase S120A is expressed in Escherichia coli BL21(DE3)
P00590
expressed in Escherichia coli Origami B(DE3); expressed in Escherichia coli strain Origami B(DE3)
-
expressed in Pichia pastoris
-
expression in Escherichia coli WK-6 strain
-
heterologous expression in Nicotiana tabacum var. Petite Havana using chloroplast transformation vector pLD-cut, modification of chloroplast ultrastructures in cutinase transplastomic lines, phenotype, overview
-
into pPICZalphaA with the Saccharomyces cerevisiae alpha-factor signal sequence and methanol-inducible alcohol oxidase promoter, additional sequences of the c-myc epitope and (His)6-tag of the vector fused to the C-terminus of cutinase, while the other expression vector is constructed without any additional sequence. Expressed in Pichia pastoris strain X-33
-
over-expression of recombinant cutinase cloned in pMac5-8 and its variants (S54D, L153Q and T179C) are performed with Escherichia coli WK6 strain
-
overexpression of recombinant cutinase and its variants is performed with strain Escherichia coli WK-6 (delta(lac-pro) galE strA F'[lacIq ZdeltaM15 proAB+])
-
heterologous enzyme expression, mostly with secretion to the medium, in different hosts, e.g. Escherichia coli strain W6, Bacillus subtilis, Saccharomyces cerevisiae strain SU50, Pichia pastoris, Aspergillus awamori, and Fusarium venenatum, from different plasmids and using different promoters, and using different signal peptides, e.g. alkaline phosphatase (PhoA) signal peptide, LipA signal peptide, alpha-factor signal peptide, and Fusarium solani cutinase signal peptide, overview. Optimization of method and culture conditions
Fusarium solani pisi
P00590
cloned and overexpressed in Escherichia coli
-
expressed in Escherichia coli strain Origami B(DE3); mutant H204N overexpressed in Escherichia coli Origami B(DE3)
-
high-level overexpression of Glomerella cingulata cutinase, with a cutinase production of 3800 mg/l and an activity of 434 U/ml, in dense cultures of Pichia pastoris strain X-33 grown under fed-batch conditions, method evaluation, overview
-
sequence comparisons, functional recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain Origami B (DE3)
-
gene hic, recombinant expression in Pichia pastoris strain X-33 and secretion to the culture medium
-
expression of cutinase FspC in Bacillus subtilis
-
overexpression in Escherichia coli strain WK-6
-
recombinant expression of cutinase in Saccharomyces cerevisiae strain SU50
-
Expression of aggregation-prone cutinase protein using RNA polymerase sigma factor (RpoS) or glutathione transferase as fusion partners in Escherichia coli strain BL21 (DE3).
-
gene SsCut, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21, expression in Nicotiana benthamiana leaves, quantitative real-time polymerase chain reaction analysis
A7EQQ8
gene ScCut1, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant of C-terminally His-tagged codon-optimized enzyme expression in Pichia pastoris strain X-33, subcloning in Escherichia coli
S4VCH4
recombinant expression in Escherichia coli strain BL21-Gold(DE3); recombinant expression in Escherichia coli strain BL21-Gold(DE3)
E9LVH8, E9LVH9
expression of cutinase isozymes Tfu 0882 and Tfu 0883 in Escherichia coli strain BL21(DE3)
-
gene cut1, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3), secretion into periplasm and medium, method development and optimization for process for large-scale production of cutinase in soluble form; gene cut2, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3), secretion into periplasm and medium, method development and optimization for process for large-scale production of cutinase in soluble form
-
recombinant expression of C-terminally His-tagged wild-type and mutant cutinase lacking the signal peptide sequence in Escherichia coli strain BL21(DE3), the enzyme is mostly secreted to the medium. Compared to the cells expressing the inactive cutinase mutant S130A, the cells expressing the truncated cutinase show increased membrane permeability and irregular morphology
-
recombinant expression via type II secretory system in Escherichia coli strain BL21(DE3), the protein accumulates in the periplasmic space. The alpha-hemolysin secretion system can export target proteins directly from cytoplasm across both cell membrane of Escherichia coli to the culture medium and is therefore used for expression of the extracellular enzyme, method optimization for large-scale industrial production, overview
-
expressed in Pichia pastoris
A8QPD8
recombinant expression of extracellular wild-type and mutant enzymes in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CDEF1 gene is not expressed in leaves of wild-type plants. Is expressed at low levels in roots
Q9SZW7
CDEF1 gene is expressed in leaves of transgenic 35S::CDEF1 plants. CDEF1 gene is highly expressed in mature pollen
Q9SZW7
increased enzyme production in wild-type strain by induction induction with cutin, cutin hydrolysis monomers, and some lipids, e.g. olive oil
Q5AVY9
mutants carrying a DELTActf1 loss-of-function allele grown on inducing substrates fail to activate extracellular cutinolytic activity and expression of the cut1 gene, encoding a putative cutinase
A6N6J6
the zinc finger transcription factor Ctf1 from Fusarium oxysporum mediates efficient transcriptional activation of cut1 and lip1 on fatty acid substrates, but not on glucose. The Ctf1 transcription factor, a functional orthologue of CTF1alpha, controls expression of cutinase genes and virulence. Strains harbouring a ctf1C allele in which the ctf1 coding region is fused to the strong constitutive Aspergillus nidulans gpdA promoter show increased induction of cutinase activity and gene expression. Higher levels of cut1 transcript in mycelia of the wild-type grown on apple cutin than in those grown on glucose. Activation of cut1 by apple cutin is even more pronounced in the ctf1C strain than in the wild-type. Low expression of cut1 in roots 10 days after inoculation of tomato plants
A6N6J6
mutants carrying a DELTActf1 loss-of-function allele grown on inducing substrates fail to activate extracellular cutinolytic activity and expression of the cut1 gene, encoding a putative cutinase
-
-
the zinc finger transcription factor Ctf1 from Fusarium oxysporum mediates efficient transcriptional activation of cut1 and lip1 on fatty acid substrates, but not on glucose. The Ctf1 transcription factor, a functional orthologue of CTF1alpha, controls expression of cutinase genes and virulence. Strains harbouring a ctf1C allele in which the ctf1 coding region is fused to the strong constitutive Aspergillus nidulans gpdA promoter show increased induction of cutinase activity and gene expression. Higher levels of cut1 transcript in mycelia of the wild-type grown on apple cutin than in those grown on glucose. Activation of cut1 by apple cutin is even more pronounced in the ctf1C strain than in the wild-type. Low expression of cut1 in roots 10 days after inoculation of tomato plants
-
-
the recombinant enzyme is induced with 0.5% v/v methanol in basal salt medium at pH 5.0 and 28C
-
cutinase genes show four differential expression patterns, indicating regulatory sub- and neo-functionalization
-
increased enzyme production in wild-type strain by induction with cutin, cutin hydrolysis monomers, and some lipids, e.g. apple cutin
-
increased enzyme production in wild-type strain by induction with cutin, cutin hydrolysis monomers, and some lipids, e.g. tomato peel
-
increased enzyme production in strain WSH03-11 by induction with cutin, cutin hydrolysis monomers, and some lipids, e.g. tomato peel
-
increased enzyme production in strain WSH03-11 by induction with cutin, cutin hydrolysis monomers, and some lipids, e.g. tomato peel
Thermobifida fusca DSM 44342
-
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A84F
P41744
mutation in the small helical flap, significantly increases the activity towards longer chain substrates like 4-nitrophenyl palmitate
I183A
P41744
mutation in the hydrophobic binding loop, drastically reduces the overall activity
L181A
P41744
mutation in the hydrophobic binding loop, drastically reduces the overall activity
F52W
Q874E9
site-directed mutagenesis, the mutant shows increased activity with 4-nitrophenyl palmitate by 4.86fold and altered substrate specificity toward substrates with longer chain lengths
L181F
Q874E9
site-directed mutagenesis, the mutant shows increased activity with 4-nitrophenyl palmitate by 4.86fold and altered substrate specificity toward substrates with longer chain lengths
A164E
-
amino acid substitution, 74% of wild-type activity
A164R
P00590
41% of the activity of the wild-type enzyme
A185L
P00590
96% of the activity of the wild-type enzyme
A185T
-
amino acid substitution, 142% of wild-type activity
A195S
P00590
38% of the activity of the wild-type enzyme
A199C
P00590
no activity
A199C
-
comparative structural analysis of native enzyme and mutant enzymes
A29S
-
64% of the activity of the wild-type enzyme
A79G
P00590
50% of the activity of the wild-type enzyme
A85F
-
crystallizes in a form different from the native enzyme
A85F
P00590
136% of the activity of the wild-type enzyme
A85F
-
optimal activity with triglyceride anolgues shifts towards slightly longer acyl ester chains
A85F/G82A
-
optimal activity with triglyceride anolgues shifts towards slightly longer acyl ester chains
A85W
-
optimal activity with triglyceride anolgues shifts towards slightly longer acyl ester chains
A85W
P00590
5% of the activity of the wild-type enzyme
D111N
P00590
39% of the activity of the wild-type enzyme
D134S
P00590
37% of the activity of the wild-type enzyme
D83S
P00590
62% of the activity of the wild-type enzyme
E201K
P00590
54% of the activity of the wild-type enzyme
G192Q
P00590
44% of the activity of the wild-type enzyme
G26A
P00590
32% of the activity of the wild-type enzyme
G26P
-
amino acid substitution, 68% of wild-type activity
G41A
-
amino acid substitution, 76% of wild-type activity
G82A
-
mutation has no influence on enzymatic properties
I183F
P00590
25% of the activity of the wild-type enzyme
I204K
P00590
66% of the activity of the wild-type enzyme
I24S
P00590
4% of the activity of the wild-type enzyme
K140D
-
amino acid substitution, 39% of wild-type activity
K151M
-
amino acid substitution, 22% of wild-type activity
K151R
P00590
29% of the activity of the wild-type enzyme
K168L
P00590
83% of the activity of the wild-type enzyme
K65P
-
amino acid substitution, 99% of wild-type activity
L114C
-
comparative structural analysis of native enzyme and mutant enzymes
L114Y
P00590
20% of the activity of the wild-type enzyme
L153A
-
amino acid substitution, 111% of wild-type activity
L153Q
-
amino acid substitution, 145% of wild-type activity
L153Q
-
L153Q mutation also reduces the development of hydrophobic solvent accessible patches
L182A
-
shows the one- and two-fold higher ability to biodegrade aliphatic polyamide substrates. Activity with polyethylene terephthalate fibers is 5.3fold higher than wild-type enzyme, activity with polyamide 6,6 fiber is 119% of wild-type activity
L182W
P00590
19% of the activity of the wild-type enzyme
L189A
-
activity with polyethylene terephthalate fibers is 78% of wild-type enzyme, activity with polyamide 6,6 fiber is 94% of wild-type activity
L189F
-
comparative structural analysis of native enzyme and mutant enzymes
L189F
P00590
109% of the activity of the wild-type enzyme
L81A
-
activity with polyethylene terephthalate fibers is 4fold higher than wild-type enzyme, activity with polyamide 6,6 fiber is 98% of wild-type activity
L81G/L182G
-
comparative structural analysis of native enzyme and mutant enzymes
L99K
P00590
78% of the activity of the wild-type enzyme
N161D
P00590
63% of the activity of the wild-type enzyme
N172K
-
comparative structural analysis of native enzyme and mutant enzymes
N172K
P00590
45% of the activity of the wild-type enzyme
N172K/R196E
-
comparative structural analysis of native enzyme and mutant enzymes, crystallizes in a form different from the native enzyme
N33S
P00590
74% of the activity of the wild-type enzyme
N84A
-
comparative structural analysis of native enzyme and mutant enzymes
N84A
P00590
5% of the activity of the wild-type enzyme
N84A
-
26.5% of the activity of the wild-type enzyme with p-nitrophenylbutanoate as substrate
N84A
-
activity with polyethylene terephthalate fibers is 1.7fold higher than wild-type enzyme, activity with polyamide 6,6 fiber is 93% of wild-type activity
N84D
P00590
no activity
N84D
-
crystallizes in a form different from the native enzyme
N84D
-
0.16% of the activity of the wild-type enzyme with p-nitrophenylbutanoate as substrate
N84L
-
comparative structural analysis of native enzyme and mutant enzymes
N84L
P00590
5% of the activity of the wild-type enzyme
N84L
-
3.0% of the activity of the wild-type enzyme with p-nitrophenylbutanoate as substrate
N84W
-
comparative structural analysis of native enzyme and mutant enzymes
N84W
-
0.11% of the activity of the wild-type enzyme with p-nitrophenylbutanoate as substrate
Q121L
-
comparative structural analysis of native enzyme and mutant enzymes
R156E
P00590
79% of the activity of the wild-type enzyme
R156K
P00590
115% of the activity of the wild-type enzyme
R156K
-
amino acid substitution, 151% of wild-type activity
R156L
-
comparative structural analysis of native enzyme and mutant enzymes
R156L
P00590
71% of the activity of the wild-type enzyme
R156N
-
amino acid substitution, 89% of wild-type activity
R158L
-
amino acid substitution, 75% of wild-type activity
R17E
P00590
34% of the activity of the wild-type enzyme
R17E/N172K
-
comparative structural analysis of native enzyme and mutant enzymes
R17N
P00590
31% of the activity of the wild-type enzyme
R17S
-
amino acid substitution, 69% of wild-type activity
R196A
-
amino acid substitution, 75% of wild-type activity
R196E
-
crystallizes in a form different from the native enzyme
R196E
P00590
45% of the activity of the wild-type enzyme
R196E
-
amino acid substitution, 21% of wild-type activity
R196K
P00590
38% of the activity of the wild-type enzyme
R196L
P00590
44% of the activity of the wild-type enzyme
R208A
P00590
64% of the activity of the wild-type enzyme
R78L
P00590
49% of the activity of the wild-type enzyme
R78N
P00590
34% of the activity of the wild-type enzyme
R88A
P00590
39% of the activity of the wild-type enzyme
R96N
P00590
57% of the activity of the wild-type enzyme
S120A
P00590
no activity
S120A
P00590
the mutant enzyme casries a 15 amino acid pro-peptide. The pro-peptide is affected by the presence of the micellar substrate
S120C
-
comparative structural analysis of native enzyme and mutant enzymes
S129C
-
comparative structural analysis of native enzyme and mutant enzymes
S213C
-
comparative structural analysis of native enzyme and mutant enzymes
S42A
P00590
no activity
S42A
-
comparative structural analysis of native enzyme and mutant enzymes
S42A
-
0.22% of the activity of the wild-type enzyme with p-nitrophenylbutanoate as substrate
S54D
-
amino acid substitution, 79% of wild-type activity
S54D
-
S54D mutant of cutinase is significantly more resistant to sodium dioctyl sulfosuccinate denaturation than the wild type
S54E
P00590
34% of the activity of the wild-type enzyme
S54E
-
amino acid substitution, 83% of wild-type activity
S54K
P00590
96% of the activity of the wild-type enzyme
S54W
-
mutation has no influence on enzymatic
S54W
P00590
89% of the activity of the wild-type enzyme
S57D
-
amino acid substitution, 61% of wild-type activity
S61D
-
amino acid substitution, 83% of wild-type activity
S82R
P00590
50% of the activity of the wild-type enzyme
S92C
-
comparative structural analysis of native enzyme and mutant enzymes
T144C
-
comparative structural analysis of native enzyme and mutant enzymes
T144C
P00590
54% of the activity of the wild-type enzyme
T167L
P00590
54% of the activity of the wild-type enzyme
T173K
P00590
119% of the activity of the wild-type enzyme
T179C
-
amino acid substitution, 90% of wild-type activity
T179C
-
T179C mutation located close to the active centre and to disulfide bond Cys171-Cys178 introduced changes in the cutinase structure that are observed even in the cutinase region around the tryptophan residue. This mutation also reduces the development of hydrophobic solvent accessible patches
T179E
-
amino acid substitution, 10% of wild-type activity
T179N
-
amino acid substitution, 119% of wild-type activity
T179Y
P00590
131% of the activity of the wild-type enzyme
T18D
-
amino acid substitution, 65% of wild-type activity
T18V
P00590
90% of the activity of the wild-type enzyme
T19V
P00590
35% of the activity of the wild-type enzyme
T45A
-
comparative structural analysis of native enzyme and mutant enzymes
T45A
P00590
98% of the activity of the wild-type enzyme
T45D
-
amino acid substitution, 54% of wild-type activity
T45K
P00590
74% of the activity of the wild-type enzyme
T50V
P00590
25% of the activity of the wild-type enzyme
T80D
P00590
32% of the activity of the wild-type enzyme
T80P
-
comparative structural analysis of native enzyme and mutant enzymes
V184A
-
activity with polyethylene terephthalate fibers is 2fold higher than wild-type enzyme, activity with polyamide 6,6 fiber is 98% of wild-type activity
W69Y
P00590
12% of the activity of the wild-type enzyme
Y119H
-
comparative structural analysis of native enzyme and mutant enzymes
Y38F
-
comparative structural analysis of native enzyme and mutant enzymes
Y38F
P00590
62% of the activity of the wild-type enzyme
A164R
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 59% reduced activity in olive oil compared to the wild-type enzyme
A185L
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows unaltered activity in olive oil compared to the wild-type enzyme
A195S
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 62% reduced activity in olive oil compared to the wild-type enzyme
A199C
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows no activity in olive oil
A29S
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 36% reduced activity in olive oil compared to the wild-type enzyme
A79G
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 50% reduced activity in olive oil compared to the wild-type enzyme
A85F
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 36% increased activity in olive oil compared to the wild-type enzyme, the mutant shows higher enzyme activity with hydrophobic, low-molecular-weight substrates in olive oil emulsions than the wild-type enzyme
A85W
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 9% increased activity in olive oil compared to the wild-type enzyme, the mutant shows higher enzyme activity with hydrophobic, low-molecular-weight substrates in olive oil emulsions than the wild-type enzyme
D111N
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 61% reduced activity in olive oil compared to the wild-type enzyme
D134S
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 63% reduced activity in olive oil compared to the wild-type enzyme
D33S
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 26% reduced activity in olive oil compared to the wild-type enzyme
D83S
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 38% reduced activity in olive oil compared to the wild-type enzyme
E201K
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 46% reduced activity in olive oil compared to the wild-type enzyme
G192Q
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 56% reduced activity in olive oil compared to the wild-type enzyme
G26A
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 67% reduced activity in olive oil compared to the wild-type enzyme
I183F
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 75% reduced activity in olive oil compared to the wild-type enzyme
I204K
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 34% reduced activity in olive oil compared to the wild-type enzyme
I24S
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 96% reduced activity in olive oil compared to the wild-type enzyme
K151R
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 71% reduced activity in olive oil compared to the wild-type enzyme
K168L
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 17% reduced activity in olive oil compared to the wild-type enzyme
L114Y
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 80% reduced activity in olive oil compared to the wild-type enzyme
L182A
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows activity enhancement of 5fold toward high-molecular weight PET fibers compared to the wild-type enzyme
L182W
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 81% reduced activity in olive oil compared to the wild-type enzyme
L189F
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 9% increased activity in olive oil compared to the wild-type enzyme, the mutant shows higher enzyme activity with hydrophobic, low-molecular-weight substrates in olive oil emulsions than the wild-type enzyme
L81A
Fusarium solani pisi
P00590
the mutant shows activity enhancement of 4fold toward high-molecular weight PET fibers compared to the wild-type enzyme
L99K
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 22% reduced activity in olive oil compared to the wild-type enzyme
M98C
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 65% reduced activity in olive oil compared to the wild-type enzyme
N161D
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 37% reduced activity in olive oil compared to the wild-type enzyme
N172K
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 55% reduced activity in olive oil compared to the wild-type enzyme
N84A
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 73.5% reduced activity in olive oil compared to the wild-type enzyme, the mutant shows activity enhancement of 1.7fold toward high-molecular weight PET fibers compared to the wild-type enzyme
N84D
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows almost no activity in olive oil
N84L
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 97% reduced activity in olive oil compared to the wild-type enzyme
N84W
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows almost no activity in olive oil
R156E
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 21% reduced activity in olive oil compared to the wild-type enzyme
R156K
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 15% increased activity in olive oil compared to the wild-type enzyme
R156L
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 29% reduced activity in olive oil compared to the wild-type enzyme
R17E
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 66% reduced activity in olive oil compared to the wild-type enzyme
R17N
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 69% reduced activity in olive oil compared to the wild-type enzyme
R196E
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 55% reduced activity in olive oil compared to the wild-type enzyme
R196K
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 62% reduced activity in olive oil compared to the wild-type enzyme
R196L
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 56% reduced activity in olive oil compared to the wild-type enzyme
R208A
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 36% reduced activity in olive oil compared to the wild-type enzyme
R78L
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 51% reduced activity in olive oil compared to the wild-type enzyme
R78N
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 66% reduced activity in olive oil compared to the wild-type enzyme
R88A
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 61% reduced activity in olive oil compared to the wild-type enzyme
R96N
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 43% reduced activity in olive oil compared to the wild-type enzyme
S120A
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows no activity in olive oil
S42A
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows almost no activity in olive oil
S54E
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 66% reduced activity in olive oil compared to the wild-type enzyme
S54K
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows unaltered activity in olive oil compared to the wild-type enzyme
S54W
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 11% reduced activity in olive oil compared to the wild-type enzyme
S92R
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 50% reduced activity in olive oil compared to the wild-type enzyme
T144C
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 46% reduced activity in olive oil compared to the wild-type enzyme
T167L
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 46% reduced activity in olive oil compared to the wild-type enzyme
T173K
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 19% increased activity in olive oil compared to the wild-type enzyme, the mutant shows higher enzyme activity with hydrophobic, low-molecular-weight substrates in olive oil emulsions than the wild-type enzyme
T179Y
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 31% increased activity in olive oil compared to the wild-type enzyme, the mutant shows higher enzyme activity with hydrophobic, low-molecular-weight substrates in olive oil emulsions than the wild-type enzyme
T18V
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 10% reduced activity in olive oil compared to the wild-type enzyme
T19V
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 65% reduced activity in olive oil compared to the wild-type enzyme
T45A
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows unaltered activity in olive oil compared to the wild-type enzyme
T45K
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 26% reduced activity in olive oil compared to the wild-type enzyme
T50V
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 75% reduced activity in olive oil compared to the wild-type enzyme
T80D
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 68% reduced activity in olive oil compared to the wild-type enzyme
V184A
Fusarium solani pisi
P00590
the mutant shows activity enhancement of 2fold toward high-molecular weight PET fibers compared to the wild-type enzyme
W69Y
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 88% reduced activity in olive oil compared to the wild-type enzyme
Y38F
Fusarium solani pisi
P00590
site-directed mutagenesis, the mutant shows 38% reduced activity in olive oil compared to the wild-type enzyme
H204N
-
site-directed mutant, constructed, overexpressed, and purified, is catalytically inactive. Is not covalently modified by a 4fold excess of diethyl p-nitrophenyl phosphate, in contrast to the wild-type
L172K
-
site-directed mutagenesis, compared to the wild-type enzyme, the mutant exhibits higher enzymatic performance towards phenyl ester substrates of longer carbon chain length, yet its thermal stability is inversely affected
N177D
-
site-directed mutagenesis, the mutation aims to alter the surface electrostatics as well as to remove a potentially deamidation-prone asparagine residue. The mutant is more resilient to temperature increase with a 2.7fold increase in half-life at 50C, accompanied by an increase in optimal temperature, as compared with wild-type enzyme, while the activity at 25C is not compromised
H137L
Q2VF46
site-directed mutageneis, the mutant exhibits a slightly increased Km value with the soluble substrate 4-nitrophenyl butyrate compared to the wild-type enzyme
H173L
Q8TGB8
36% of wild-type activity
S103A
Q8TGB8
231% of wild-type activity
S103A
Q2VF46
site-directed mutageneis, the mutant exhibits a slightly increased Km value and a 2.3fold higher kcat with the soluble substrate 4-nitrophenyl butyrate compared to the wild-type enzyme
S103T
Q8TGB8
38% of wild-type activity
S103T
Q2VF46
site-directed mutageneis, the mutant exhibits a slightly increased Km valuet with the soluble substrate 4-nitrophenyl butyrate compared to the wild-type enzyme
S54D
-
site-directed mutagenesis, the mutant shows reduced transesterification activity compared to the wild-type enzyme
T179C
-
site-directed mutagenesis, the mutant shows transesterification activity similar to the wild-type enzyme, T179C displays high stability in the presence of methanol with an activity loss of only 16% as compared to 90% loss of wild-type activity, the mutant is also more stable microencapsulated in reversed micelles of bis(2-ethylhexyl) sodium sulfosuccinate in isooctane
cutinase-tryptophan,proline2
-
tryptophan tag, cutinase with varying length tryptophan tag (WP)2
cutinase-tryptophan,proline4
-
tryptophan tag, cutinase with varying length tryptophan tag (WP)4
S117A
A7EQQ8
site-directed mutagenesis, the mutation causes a 99% reduction in enzyme activity and also completely abolishes the elicitor activity of the protein
A30V
E9LVH8, E9LVH9
site-directed mutagenesis, mutation of isozyme Cut2 to the analogue residue of isozyme Cut1, the mutant shows increased catalytic efficiency with polyethyleneterephthalate and higher kcat/KM values on soluble substrates compared to the wild-type enzyme
Q65E
E9LVH8, E9LVH9
site-directed mutagenesis, mutation of isozyme Cut2 to the analogue residue of isozyme Cut1, the mutant shows slightly reduced catalytic efficiency with 4-nitrophenyl ester substrates compared to the wild-type enzyme
R187K
E9LVH8, E9LVH9
site-directed mutagenesis, mutation of isozyme Cut2 to the analogue residue of isozyme Cut1, the mutant shows increased catalytic efficiency with 4-nitrophenyl ester substrates compared to the wild-type enzyme
R19S
E9LVH8, E9LVH9
site-directed mutagenesis, mutation of isozyme Cut2 to the analogue residue of isozyme Cut1
R19S/R29N/A30V
E9LVH8, E9LVH9
site-directed mutagenesis, mutation of isozyme Cut2 to the analogue residue of isozyme Cut1, the mutant shows increased catalytic efficiency with 4-nitrophenyl ester substrates compared to the wild-type enzyme
R19SS
-
the mutant shows strongly increased PET hydrolysis activity compared to the wild-type enzyme
R29N
E9LVH8, E9LVH9
site-directed mutagenesis, mutation of isozyme Cut2 to the analogue residue of isozyme Cut1, the mutant shows increased catalytic efficiency with polyethyleneterephthalate and higher kcat/KM values on soluble substrates compared to the wild-type enzyme
R29N/A30V
E9LVH8, E9LVH9
site-directed mutagenesis, mutation of isozyme Cut2 to the analogue residue of isozyme Cut1, the mutant shows increased catalytic efficiency with polyethyleneterephthalate and higher kcat/KM values on soluble substrates compared to the wild-type enzyme
R29SS
-
the mutant shows strongly increased PET hydrolysis activity compared to the wild-type enzyme
Q65E
Thermobifida cellulosilytica DSM 44535
-
site-directed mutagenesis, mutation of isozyme Cut2 to the analogue residue of isozyme Cut1, the mutant shows slightly reduced catalytic efficiency with 4-nitrophenyl ester substrates compared to the wild-type enzyme
-
R187K
Thermobifida cellulosilytica DSM 44535
-
site-directed mutagenesis, mutation of isozyme Cut2 to the analogue residue of isozyme Cut1, the mutant shows increased catalytic efficiency with 4-nitrophenyl ester substrates compared to the wild-type enzyme
-
R19S
Thermobifida cellulosilytica DSM 44535
-
site-directed mutagenesis, mutation of isozyme Cut2 to the analogue residue of isozyme Cut1
-
S130A
-
site-directed mutagenesis, catalytically inactive active site mutant, which is mostly located in the cytoplasm. Compared to the cells expressing the inactive cutinase mutant S130A, the cells expressing the truncated cutinase show increased membrane permeability and irregular morphology
T101A/Q132A
-
engineering by site-directed mutagenesis modifying the active site, the mutant cutinase shows increased activity on polyester substrates. The double mutation Q132A/T101A both creates space and increases hydrophobicity. The activity of the double mutant on the soluble substrate p-nitrophenyl butyrate increased 2fold compared to wild-type cutinase, while on poly(ethylene terephthalate) the double mutant exhibits considerably higher hydrolysis efficiency
W86L
-
site-directed mutagenesis, the mutant exhibits an improvement in binding and catalytic efficiency of 1.4fold toward PET fiber compared with the wild-type enzyme
W86L
Thermobifida fusca DSM 44342
-
site-directed mutagenesis, the mutant exhibits an improvement in binding and catalytic efficiency of 1.4fold toward PET fiber compared with the wild-type enzyme
-
W86Y
Thermobifida fusca DSM 44342
-
site-directed mutagenesis, the mutant exhibits an improvement in binding and catalytic efficiency of 1.5fold toward PET fiber compared with the wild-type enzyme
-
C275A/C292A
-
site-directed mutagenesis, the mutant lacks the disulfide bond formed by Cys275 and Cys292, resulting in increased instability
L80A
P41744
mutation in the hydrophobic binding loop, drastically reduces the overall activity
additional information
Q9SZW7
CDEF1-deficient mutant (SALK-014093) that carries a T-DNA insertion in the coding region of CDEF1, shows no abnormal phenotypes, such as reduced fertility or reduced lateral root emergence
additional information
-
because the organism has a low but significant FAE activity, it may be easier to introduce a high level of FAE activity in cutinases through point mutations
M98C
P00590
35% of the activity of the wild-type enzyme
additional information
P00590
the insertion mutant 49aILe shows 52% of the activity of the wild-type enzyme
additional information
-
a complete saturation mutagenesis approach to search cutinase for amino acids contributing to increased stability in the presence of the anionic surfactant. Mutants showing substitutions in the large hydrophobic crevice (S54D, S57D, S61D, K65P, R196A), that is thought to be the region more involved in the unfolding by anionics, will be very important to obtain an enzyme less sensitive to AOT
additional information
-
stability of cutinase may be increased through mutations designed to avoid the transient formation of hydrophobic groups during protein movement. Because the organism has a low but significant ferulic acid esterase activity, it may be easier to introduce a high level of ferulic acid esterase activity in cutinases through point mutations
N177D/L172K
-
site-directed mutagenesis, the double mutant shows enhanced activity towards phenyl ester substrates and enhanced thermal stability
additional information
-
mutant myHiC, obtained by localised random mutagenesis, shows increased activity and decreased surfactanct sensitivity
additional information
-
because the organism has a low but significant FAE activity, it may be easier to introduce a high level of FAE activity in cutinases through point mutations
additional information
-
establishment of immobilized cutinase as a novel biocatalyst for the synthesis of functionalized acryclic esters by transesterification with transesterification of methyl acrylate with 6-mercapto-1-hexanol at a high molar ratio in a solvent free system as model reaction, overview
L153Q
-
site-directed mutagenesis, the mutant shows transesterification activity similar to the wild-type enzyme
additional information
-
cutinase is microencapsulated in reversed micelles of bis(2-ethylhexyl) sodium sulfosuccinate in isooctane for the production of alkyl esters, known as biodiesel, evaluation of the system stability using wild-type enzyme and three mutants, L153Q, T179C and S54D, method evaluation, overview. Loss of 45% of wild-type cutinase activity when incubated in the micellar system for 3 h, and an additional loss of 90% of the activity is observed in the presence of methanol after 10 min of incubation
Y116A
A7EQQ8
site-directed mutagenesis, the mutation causes a 97% reduction in enzyme activity and also abolishes the elicitor activity of the protein
additional information
S4VCH4
generation of codon-optimized enzyme for expression in Pichia pastoris
additional information
Sirococcus conigenus VTT D-04989
-
generation of codon-optimized enzyme for expression in Pichia pastoris
-
L183A
E9LVH8, E9LVH9
site-directed mutagenesis, mutation of isozyme Cut2 to the analogue residue of isozyme Cut1, the mutant shows slightly increased catalytic efficiency with 4-nitrophenyl ester substrates compared to the wild-type enzyme
additional information
E9LVH8, E9LVH9
exchange of the positively charged arginine (Arg19 and Arg29) located on the enzyme surface to the non-charged amino acids serine and asparagine strongly increased the hydrolysis activity for bis(benzoyloxyethyl)terephthalate and polyethyleneterephthalate. In contrast, exchange of the uncharged glutamine (Glu65) by the negatively charged glutamic acid lead to a complete loss of hydrolysis activity on polyethyleneterephthalate films
additional information
E9LVH8, E9LVH9
the cutinase id fused with binding modules from Hypocrea jecorina cellobiohydrolase I (CBM) and Alcaligenes faecalis polyhydroxyalkanoate depolymerase (PBM), respectively. The adsorption of the fusion enzymes to PET is increased, and PET hydrolysis activity of one of the fusions (Thc_Cut1 + CBM) is enhanced 3.8fold
additional information
E9LVH8, E9LVH9
the cutinase is fused with binding modules from Hypocrea jecorina cellobiohydrolase I (CBM) and Alcaligenes faecalis polyhydroxyalkanoate depolymerase (PBM), respectively. The adsorption of the fusion enzymes to PET is increased, and PET hydrolysis activity of one of the fusions (Thc_Cut1 + CBM) is enhanced 3.8fold
L183A
Thermobifida cellulosilytica DSM 44535
-
site-directed mutagenesis, mutation of isozyme Cut2 to the analogue residue of isozyme Cut1, the mutant shows slightly increased catalytic efficiency with 4-nitrophenyl ester substrates compared to the wild-type enzyme
-
additional information
Thermobifida cellulosilytica DSM 44535
-
exchange of the positively charged arginine (Arg19 and Arg29) located on the enzyme surface to the non-charged amino acids serine and asparagine strongly increased the hydrolysis activity for bis(benzoyloxyethyl)terephthalate and polyethyleneterephthalate. In contrast, exchange of the uncharged glutamine (Glu65) by the negatively charged glutamic acid lead to a complete loss of hydrolysis activity on polyethyleneterephthalate films
-
I218A
-
engineering by site-directed mutagenesis modifying the active site, the mutant cutinase shows increased activity on polyester substrates. Mutation I218A creates space, activity on poly(ethylene terephthalate) is increased compared to the wild-type enzyme, with considerably higher hydrolysis efficiency
additional information
-
generation of a fusion protein, fusing cellobiohydrolase Is from Thermobifida fusca cellulase Cel6A (CBMCel6A) and Cellulomonas fimi cellulase CenA (CBMCenA), separately, to Thermobifida fusca cutinase. Both fusion proteins display catalytic properties and pH stabilities similar to those of Thermobifida fusca cutinase. Addition of pectinase enhances the cotton fiber binding activities of cutinase-CBMCel6A and cutinase-CBMCenA by 40%, and 45%, respectively. A dramatic increase of up to 3fold is observed in the amount of fatty acids released from cotton fiber by the combination of cutinase-CBM fusion proteins with pectinase
W86Y
-
site-directed mutagenesis, the mutant exhibits an improvement in binding and catalytic efficiency of 1.5fold toward PET fiber compared with the wild-type enzyme
additional information
Thermobifida fusca DSM 44342
-
generation of a fusion protein, fusing cellobiohydrolase Is from Thermobifida fusca cellulase Cel6A (CBMCel6A) and Cellulomonas fimi cellulase CenA (CBMCenA), separately, to Thermobifida fusca cutinase. Both fusion proteins display catalytic properties and pH stabilities similar to those of Thermobifida fusca cutinase. Addition of pectinase enhances the cotton fiber binding activities of cutinase-CBMCel6A and cutinase-CBMCenA by 40%, and 45%, respectively. A dramatic increase of up to 3fold is observed in the amount of fatty acids released from cotton fiber by the combination of cutinase-CBM fusion proteins with pectinase
-
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
refolding from the pH-denatured state. Existence of two distinct intermediate states in cutinase folding: an unfolding intermediate and an off-pathway folding intermediate.
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
-
biotechnological applications of cutinases for synthetic polyester degradation
biotechnology
-
engineering new cutinase-inspired biocatalysts with tailor-made properties
degradation
-
biotechnological applications of cutinases for synthetic polyester degradation
degradation
-
efficient degradation of n-butyl benzyl phthalate by enzyme, degradation of 60% of initial amount within 7.5 h. Major product is 1,3-isobenzofurandione
degradation
-
enzyme degrades 60% of initial 500 mg/l malathion within 0.5 h, major degradation product is malathion diacid
degradation
-
enzyme shows significant degradation of dipropyl phthalate to non-toxic 1,3-isobenzofurandione, with 70% degradation of initial 500 mg/l within 2.5 h
environmental protection
-
application of cutinase for degradationof dihexyl phthalate in the dihexyl phthalate-contaminated environments may be possible
industry
-
useful as biocatalysts in systems involving hydrolysis, esterification, and transesterification reactions
biotechnology
-
use of enzyme in a membrane reactor in presence of 1-hexanol, operational half-life of 674 days
biotechnology
-
engineering new cutinase-inspired biocatalysts with tailor-made properties
biotechnology
-
high-level secretion of cutinase in Pichia pastoris may be a promising alternative to many expression systems previously used for the large-scale production of cutinase in Saccharomyces cerevisiae as well as Escherichia coli. The functional expression of a large amount of extracellular cutinase offers the opportunity for developing an efficient high-throughput screening procedure for the improvement of enzymatic property and the development of novel biocatalysis of cutinase
degradation
-
biotechnological applications of cutinases for synthetic polyester degradation
industry
-
key for the design of biocatalysts with sufficient stability for practical applications in detergent industry
degradation
-
biotechnological applications of cutinases for synthetic polyester degradation
industry
-
useful as biocatalysts in systems involving hydrolysis, esterification, and transesterification reactions, useful as biocatalysts in systems involving hydrolysis, esterification, and transesterification reactions. Displays a stability profile that is well-fitted to the industrial process
synthesis
-
immobilized cutinase HiC from the ascomycete Humicola insolens is applied as a biocatalyst for the synthesis of functionalized acryclic esters by transesterification using transesterification of methyl acrylate with 6-mercapto-1-hexanol at a high molar ratio in a solvent free system as a model reaction
biotechnology
-
adsorption of enzyme onto the surface of poly(methyl methacrylate) latex particles. Up to 50% decrease in specific activity at pH-values 4.5 and 5.2. Almost no inactivation upon adsorption at pH 7.0 and 9.2. 60% increase in maximum adsorption with temperature raising from 25 to 50C
biotechnology
-
immobilization of enzyme on sodium form of zeolite Y, half-life 590 days at 30C. Immobilization on zolite A, halft-life of 54 days at 30C. Half-lives after immobilization on Alumina and Accurel-PA6 are 109 and 10 days, resp. Higher temperatures induce a remarkable stability loss in all preparations. At 30C, enzymatic activities obtained wit the immobilization on zeolite A are the highest ones
biotechnology
-
study on enzyme encapsulated in sol-gel matrices prepared with alkyl-alkoxysilane precursors of different chain length. Specific activity of entrapped enzyme is comparable to enzyme immobilized on zeolite Y, with incorporation of different additives bringing about an enhancement of enzyme activity and operational stability
synthesis
-
a high enzyme production, high specific enzyme activity, and high enzyme yield are obtained upon expression with a 5% air saturation of oxygen. At low dissolved oxygen concentration, enzyme yield and specific activity increase with increase of culture pH-value from 5.25 to 6.25
industry
-
the enzyme is mainly utilized in textile industry
synthesis
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application of enginered mutant T101A/Q132A/I218A in synthetic fiber biotransformation
industry
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useful as biocatalysts in systems involving hydrolysis, esterification, and transesterification reactions. Displays a stability profile that is well-fitted to the industrial process
additional information
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can be exploited in treating agricultural, food, and forest raw materials as well as their processing by-products
industry
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useful as biocatalysts in systems involving hydrolysis, esterification, and transesterification reactions. Cutinase proves to be the most well fitted enzyme for the detection of pesticide residues in foods even at very low levels. Use in fiber modification due to its hydrophobic nature and activity against biopolyesters present in plant cuticle. Use of cutinase to improve the wetting of cotton fibers. Cutinase is potentially useful for the removal of fats in laundry, but the unfolding of the enzyme in the presence of anionic surfactants limits its widespread use as an additive in industrial laundry detergents. Displays a stability profile that is well-fitted to the industrial process
additional information
Fusarium solani pisi
P00590
cutinase combined with alkaline pectinase or xylanase, can improve the degradation of cotton seed coat during the cotton fabric bioscouring process. The cutinase can modify the surface of synthetic fibers, like polyesters, polyamides, acrylics, and cellulose acetate, and improve their wettability and dyeability
synthesis
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recombinant cutinase from Fusarium solani pisi is used as a catalyst in enzymatic transesterification between a mixture of triglyceride oils and methanol for biodiesel production in a bis(2-ethylhexyl) sodium sulfosuccinate (AOT)/isooctane reversed micellar system, kinetics, overview
additional information
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cutinase combined with alkaline pectinase or xylanase, can improve the degradation of cotton seed coat during the cotton fabric bioscouring process
industry
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Cutinase is used as a lipolytic enzyme in the composition of laundry and dishwashing detergents to more efficiently remove immobilized fats. The oleochemistry industries and pollutant degradation represent other potential uses of cutinase.
additional information
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cutinase combined with alkaline pectinase or xylanase, can improve the degradation of cotton seed coat during the cotton fabric bioscouring process. The cutinase can modify the surface of synthetic fibers, like polyesters, polyamides, acrylics, and cellulose acetate, and improve their wettability and dyeability