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Information on EC 3.1.1.74 - cutinase and Organism(s) Fusarium vanettenii and UniProt Accession P00590

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.74 cutinase
IUBMB Comments
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.
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Fusarium vanettenii
UNIPROT: P00590
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The taxonomic range for the selected organisms is: Fusarium vanettenii
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
cutinase, cutl1, cut190, fungal cutinase, thc_cut1, pet hydrolase, cutinase-like enzyme, lc-cutinase, cutinase 1, cdef1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cutin esterase
-
-
-
-
additional information
-
the cutinase is an esterase that belongs to the alpha/beta hydrolases family
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic ester hydrolysis
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-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
51377-41-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(ethylene terephthalate)n + H2O
ethylene glycol + ?
show the reaction diagram
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
show the reaction diagram
-
-
-
-
?
4-nitrophenylbutyrate + H2O
4-nitrophenol + butyrate
show the reaction diagram
-
-
-
-
?
poly(ethyl acrylate) + H2O
poly(acrylic acid) + ethanol
show the reaction diagram
-
-
-
?
poly(methyl acrylate) + H2O
poly(acrylic acid) + methanol
show the reaction diagram
-
-
-
?
tributyrin + H2O
?
show the reaction diagram
-
-
-
-
?
triolein + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
activates 7% at 1 mM
Mn2+
-
activates 36% at 1 mM
Ni2+
-
activates isozyme Tfu 0882 5% and isozyme Tfu 0883 7% at 1 mM
additional information
-
EDTA has no effect on enzyme activity at 10 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
-
inhibits 6% at 1 mM
Cr3+
-
inhibits 72% at 1 mM
Cu2+
-
inhibits 17% at 1 mM
ethylene glycol
cleavage product accumulation decreases the activity of cutinase during PET hydrolysis
Fe2+
-
inhibits 54% at 1 mM
glycerol
Hg2+
-
inhibits completely at 1 mM
Mg2+
-
inhibits 11% at 1 mM
Pb2+
-
inhibits 39% at 1 mM
Zn2+
-
inhibits 18% at 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.272
4-nitrophenyl butyrate
-
pH 8.0, 60°C, recombinant cutinase FspC
additional information
additional information
-
kinetic model of transesterification of triolein and methanol, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
837
4-nitrophenyl butyrate
-
pH 8.0, 60°C, recombinant cutinase FspC
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3200
4-nitrophenyl butyrate
-
pH 8.0, 60°C, recombinant cutinase FspC
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
170
-
lyophilized cutinase, pH 8.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
evaluation of temperature and pH effect on protein conformation and dynamics by study of fluorescence of the single tryptophan
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
evaluation of temperature and pH effect on protein conformation and dynamics by study of fluorescence of the single tryptophan
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CUTI1_FUSVN
230
0
23982
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22800
-
x * 22800, x * 24900, two differently glycosylated forms, SDS-PAGE
24900
-
x * 22800, x * 24900, two differently glycosylated forms, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 22800, x * 24900, two differently glycosylated forms, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
two differently glycosylated forms of 22800 and 24900 Da
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L153Q
-
site-directed mutagenesis, the mutant shows transesterification activity similar 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
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 20°C for 18 h, overview
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
22°C, high stability
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant cutinase FspC from Bacillus subtilis
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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
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of cutinase FspC in Bacillus subtilis
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overexpression in Escherichia coli strain WK-6
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recombinant expression of cutinase in Saccharomyces cerevisiae strain SU50
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
degradation
enzyme decreases the turbidity of poly(methyl acrylate) and poly(ethyl acrylate) dispersions
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fernandes, S.; Johansson, G.; Hatti-Kaul, R.
Purification of recombinant cutinase by extraction in an aqueous two-phase system facilitated by a fatty acid substrate
Biotechnol. Bioeng.
73
465-475
2001
Fusarium vanettenii
Manually annotated by BRENDA team
Serralha, F.N.; Lopes, J.M.; Ferreira, L.F.V.; Lemos, F.; Prazeres, D.M.F.; Aires-Barros, M.R.; Cabral, J.M.S.; Ribeiro, F.R.
Conformational changes induced by immobilization of a recombinant cutinase on zeolites
Catal. Lett.
73
63-66
2001
Fusarium vanettenii
-
Manually annotated by BRENDA team
Calado, C.R.C.; Taipa, M.A.; Cabral, J.M.S.; Fonseca, L.P.
Optimisation of culture conditions and characterisation of cutinase produced by recombinant Saccharomyces cerevisiae
Enzyme Microb. Technol.
31
161-170
2002
Fusarium vanettenii
-
Manually annotated by BRENDA team
Petersen, S.B.; Fojan, P.; Petersen, E.I.; Neves Petersen, M.T.
The thermal stability of the Fusarium solani pisi cutinase as a function of pH
J. Biomed. Biotechnol.
1
62-69
2001
Fusarium vanettenii
Manually annotated by BRENDA team
Baptista, R.P.; Santos, A.M.; Fedorov, A.; Martinho, J.M.; Pichot, C.; Elaissari, A.; Cabral, J.M.; Taipa, M.A.
Activity, conformation and dynamics of cutinase adsorbed on poly(methyl methacrylate) latex particles
J. Biotechnol.
102
241-249
2003
Fusarium vanettenii
Manually annotated by BRENDA team
Vidinha, P.; Augusto, V.; Almeida, M.; Fonseca, I.; Fidalgo, A.; Ilharco, L.; Cabral, J.M.; Barreiros, S.
Sol-gel encapsulation: an efficient and versatile immobilization technique for cutinase in non-aqueous media
J. Biotechnol.
121
23-33
2006
Fusarium vanettenii
Manually annotated by BRENDA team
Martinho, J.M.; Santos, A.M.; Fedorov, A.; Baptista, R.P.; Taipa, M.A.; Cabral, J.M.
Fluorescence of the single tryptophan of cutinase: temperature and pH effect on protein conformation and dynamics
Photochem. Photobiol.
78
15-22
2003
Fusarium vanettenii
Manually annotated by BRENDA team
Badenes, S.; Lemos, F.; Cabral, J.
Kinetics and mechanism of the cutinase-catalyzed transesterification of oils in AOT reversed micellar system
Bioprocess Biosyst. Eng.
34
1133-1142
2011
Fusarium vanettenii
Manually annotated by BRENDA team
Badenes, S.; Lemos, F.; Cabral, J.
Stability of cutinase, wild type and mutants, in AOT reversed micellar system-effect of mixture components of alkyl esters production
J. Chem. Technol. Biotechnol.
86
34-41
2011
Fusarium vanettenii
-
Manually annotated by BRENDA team
Chen, S.; Su, L.; Billig, S.; Zimmermann, W.; Chen, J.; Wu, J.
Biochemical characterization of the cutinases from Thermobifida fusca
J. Mol. Catal. B
63
121-127
2010
Thermobifida fusca, Fusarium vanettenii
-
Manually annotated by BRENDA team
De Barros, D.; Lemos, F.; Fonseca, L.; Cabral, J.
Kinetic cutinase-catalyzed esterification of caproic acid in organic solvent system
J. Mol. Catal. B
66
285-293
2010
Fusarium vanettenii
-
Manually annotated by BRENDA team
Gross, C.; Hamacher, K.; Schmitz, K.; Jager, S.
Cleavage product accumulation decreases the activity of cutinase during PET hydrolysis
J. Chem. Inf. Model.
57
243-255
2017
Fusarium vanettenii (P00590)
Manually annotated by BRENDA team
Hong, R.; Su, L.; Wu, J.
Cutinases catalyze polyacrylate hydrolysis and prevent their aggregation
Polym. Degrad. Stab.
159
23-30
2019
Thermobifida fusca, Humicola insolens (A0A075B5G4), Fusarium vanettenii (P00590)
-
Manually annotated by BRENDA team