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Information on EC 3.1.1.74 - cutinase
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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.
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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 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
tributyrin + H2O
butyric acid + 1,2-dibutyrylglycerol
about 85% of the activity with tricaproin, mutant S226P
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
the binding of Ca2+ induces large conformational changes in three loops, accompanied by the formation of additional interactions. The binding of Ca2+ stabilizes a region that is flexible in the Ca2+-free state but also modifies the substrate-binding groove by stabilizing an open conformation that allows the substrate to bind easily
Ca2+
three calcium ions bind to S226P/R228S/S176A. Ca2+ binding induces the pocket to open, enabling the substrate to access the pocket more easily. Molecular dynamics simulations suggest that a postreaction state in the engaged form presumably exists between the experimentally observed forms, indicating that the substrate would be cleaved in the engaged form and then requires the enzyme to change to the open form to release the product, a process that Ca2+ can greatly accelerate
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
a search algorithm that allows the in silico identification of PET hydrolase gene candidates from genomes and metagenomes is developed. 504 novel possible enzyme candidates in the UniProtKB and nonredundant RefSeq databases and the metagenomic database available in the NCBI database are identified
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). W0TJ64_9PSEU
304
0
32969
TrEMBL
Mitochondrion (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of S226P mutant in the Ca2+-bound and free states at 1.75 and 1.45 A resolution, respectively. A Ca2+ ion is coordinated by four residues within loop regions (the Ca2+ site) and two water molecules in a tetragonal bipyramidal array. The binding of Ca2+ induces large conformational changes in three loops, accompanied by the formation of additional interactions. The binding of Ca2+ stabilizes a region that is flexible in the Ca2+-free state but also modifies the substrate-binding groove by stabilizing an open conformation that allows the substrate to bind easily
hanging drop vapor diffusion method at 20°C, crystal structure of the inactive form of a Cut190 mutant, S226P/R228S/S176A, in complex with calcium ions and/or substrates
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S226P
mutant shows the highest activities toward tricaproin and tributyrin, the activity is greatly reduced toward tricaprylin
S226P/R228S
increase in PET degradation, improved activity and thermostability
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
73
melting temperature, mutant S226P, presence of 100 mM Ca2+
75
melting temperature, mutant S226P, presence of 300 mM Ca2+
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stability is regulated by Ca2+ binding. One Ca2+ binds to the enzyme, which induces large conformational changes in several loop regions to stabilize an open conformation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
S226P/R228S/S176A with an N-terminal polyhistidine tag is overexpressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Danso, D.; Schmeisser, C.; Chow, J.; Zimmermann, W.; Wei, R.; Leggewie, C.; Li, X.; Hazen, T.; Streit, W.R.
New insights into the function and global distribution of polyethylene terephthalate (PET)-degrading bacteria and enzymes in marine and terrestrial metagenomes
Appl. Environ. Microbiol.
84
e02773-17
2018
Saccharomonospora viridis (W0TJ64), Thermobifida alba (E9LVH7), Thermobifida cellulosilytica (E9LVH9), Thermobifida fusca (E5BBQ3), Thermobifida fusca (E9LVI0)
Miyakawa, T.; Mizushima, H.; Ohtsuka, J.; Oda, M.; Kawai, F.; Tanokura, M.
Structural basis for the Ca2+-enhanced thermostability and activity of PET-degrading cutinase-like enzyme from Saccharomonospora viridis AHK190
Appl. Microbiol. Biotechnol.
99
4297-4307
2015
Saccharomonospora viridis (W0TJ64), Saccharomonospora viridis, Saccharomonospora viridis AHK190 (W0TJ64)
Numoto, N.; Kamiya, N.; Bekker, G.J.; Yamagami, Y.; Inaba, S.; Ishii, K.; Uchiyama, S.; Kawai, F.; Ito, N.; Oda, M.
Structural dynamics of the PET-degrading cutinase-like enzyme from Saccharomonospora viridis AHK190 in substrate-bound states elucidates the Ca2+-driven catalytic cycle
Biochemistry
57
5289-5300
2018
Saccharomonospora viridis (W0TJ64), Saccharomonospora viridis, Saccharomonospora viridis AHK190 (W0TJ64)
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Release 2023.1 (January 2023)
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