Any feedback?
Information on EC 3.1.1.74 - cutinase and Organism(s) Monilinia fructicola and UniProt Accession Q8TGB8
for references in articles please use BRENDA:EC3.1.1.74Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.1.1.74 cutinaseIUBMB 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.
Specify your search results
Word Map
- 3.1.1.74
- fusarium
- solani
- pi
- lipase
- terephthalate
- p-nitrophenyl
-
lipolytic
- thermobifida
- esterases
- insolens
- fusca
-
humicola
-
ideonella
-
polybutylene
- sakaiensis
- industry
-
polycaprolactone
- tributyrin
- degradation
- sulfosuccinate
- haematococca
-
monilinia
-
terephthalic
- petase
- synthesis
- nectria
-
hydrophobins
-
saccharomonospora
- biotechnology
- environmental protection
The taxonomic range for the selected organisms is: Monilinia fructicola
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cutin esterase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylic ester 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.
CAS REGISTRY NUMBER
COMMENTARY
51377-41-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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
malfunction
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
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
additional information
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CUTI_MONFR
201
0
20227
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18134
x * 20227, precursor protein, x * 18134, mature form, calculated
20227
x * 20227, precursor protein, x * 18134, mature form, calculated
18600
-
x * 18600, protein bands of 18600 Da and 20800 Da show cutinase activity
20800
-
x * 20800, protein bands of 18600 Da and 20800 Da show cutinase activity
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 20227, precursor protein, x * 18134, mature form, calculated
?
-
x * 18600, protein bands of 18600 Da and 20800 Da show cutinase activity
?
-
x * 20800, protein bands of 18600 Da and 20800 Da show cutinase activity
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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
additional information
-
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H137L
site-directed mutageneis, the mutant exhibits a slightly increased Km value with the soluble substrate 4-nitrophenyl butyrate compared to the wild-type enzyme
S103A
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
site-directed mutageneis, the mutant exhibits a slightly increased Km valuet with the soluble substrate 4-nitrophenyl butyrate compared to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, G.Y.; Michailides, T.J.; Hammock, B.D.; Lee, Y.M.; Bostock, R.M.
Affinity purification and characterization of a cutinase from the fungal plant pathogen Monilinia fructicola (Wint.) Honey
Arch. Biochem. Biophys.
382
31-38
2000
Monilinia fructicola
Wang, G.Y.; Michailides, T.J.; Hammock, B.D.; Lee, Y.M.; Bostock, R.M.
Molecular cloning, characterization, and expression of a redox-responsive cutinase from Monilinia fructicola (Wint.) Honey
Fungal Genet. Biol.
35
261-276
2002
Monilinia fructicola (Q8TGB8), Monilinia fructicola
Chen, S.; Su, L.; Chen, J.; Wu, J.
Cutinase: characteristics, preparation, and application
Biotechnol. Adv.
31
1754-1767
2013
Alternaria brassicicola, Alternaria consortialis, Aspergillus nidulans (Q5AVY9), Aspergillus niger, Aspergillus oryzae (P52956), Bipolaris maydis, Botrytis cinerea (Q00298), Colletotrichum gloeosporioides, Colletotrichum gloeosporioides (P11373), Coprinopsis cinerea (B9U443), Cryptococcus sp. (in: Fungi) (Q874E9), Cryptococcus sp. (in: Fungi) S-2 (Q874E9), Fusarium oxysporum, Fusarium sambucinum, Fusarium solani (P00590), Helminthosporium sativum, Humicola insolens, Moesziomyces antarcticus (M9M134), Monilinia fructicola (Q2VF46), Penicillium citrinum, Penicillium sp., Pseudomonas aeruginosa, Pseudomonas mendocina, Pseudomonas putida, Pyrenopeziza brassicae (Q9Y7G8), Pyricularia grisea (P30272), Rhizoctonia solani, Streptomyces acidiscabies, Streptomyces badius, Streptomyces scabiei, Thermoactinomyces vulgaris, Thermobifida alba (E9LVH7), Thermobifida cellulosilytica (E9LVH8), Thermobifida cellulosilytica (E9LVH9), Thermobifida fusca, Thermobifida fusca DSM 44342, Thermothielavioides terrestris, Venturia inaequalis
EXTERNAL LINKS (specific for EC-Number 3.1.1.74)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
