3.1.1.74: cutinase
This is an abbreviated version!
For detailed information about cutinase, go to the full flat file.
Word Map on EC 3.1.1.74
-
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
- 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
Reaction
Synonyms
acidic cutinase, CcCUT1, CDEF1, CLE, Cut 5a, cut-2.KW3, Cut1, Cut11, Cut190, Cut2, Cut5a, CUTAB1, CutB, cuticle destructing factor 1, cutin esterase, cutin hydrolase, cutinase, cutinase 1, cutinase 2, cutinase-1, cutinase-like enzyme, cutinolytic polyesterase, CutL, CutL1, FspC, fungal cutinase, HIc, LC-cutinase, More, MYCTH_2110987, PET hydrolase, Tfu_0883, Thcut1, THCUT1 protein, Thc_Cut1, Thc_Cut2, TRIREDRAFT_60489
ECTree
3.1.1.74 cutinaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.1.1.74 - cutinase
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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
(ethylene terephthalate)n + H2O
terephthalic acid + mono(2-hydroxyethyl)terephthalate + ?
hydrolysis of poly(ethylene terephthalate) (PET) is shown for all three enzymes (native Thc_Cut1 and two glycosylation site knockout mutants (Thc_Cut1_koAsn and Thc_Cut1_koST)) based on quantification of released products by HPLC and similar concentrations of released terephthalic acid (TPA) and mono(2-hydroxyethyl) terephthalate (MHET)
-
-
?
1,4-butanediol + adipic acid
?
-
polycondensation reaction, degree of polymerization is 13
-
-
?
1,4-cyclohexanedimethanol + adipic acid
?
-
polycondensation reaction, degree of polymerization is 16
-
-
?
1,4-cyclohexanedimethanol + sebacic acid
?
-
polycondensation reaction, degree of polymerization is 61
-
-
?
1,4-cyclohexanedimethanol + suberic acid
?
-
polycondensation reaction, degree of polymerization is 18
-
-
?
1,4-cyclohexanedimethanol + succinic acid
?
-
polycondensation reaction, degree of polymerization is 4
-
-
?
1,8-octanediol + adipic acid
?
-
polycondensation reaction, degree of polymerization is 47
-
-
?
4-mercapto-1-butanol + methyl acrylate
4-mercaptobutyl acrylic ester + methanol
-
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
-
-
?
4-mercapto-1-butanol + methyl methacrylate
4-mercaptobutyl methacrylic ester + methanol
-
-
-
-
?
4-nitrophenyl (16-methyl sulfone ester) hexadecanoate + H2O
?
-
-
-
?
4-nitrophenyl (16-methyl sulfonyl ester) hexadecanoate + H2O
4-nitrophenol + (16-methyl sulfonyl ester) hexadecanoate
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
about 28% of the activity with 4-nitrophenyl acetate
-
-
?
6-mercapto-1-hexanol + methyl acrylate
6-mercaptohexyl acrylic ester
-
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
-
-
-
-
?
6-mercapto-1-hexanol + methyl propionate
6-mercaptohexyl propionic ester
-
-
-
-
?
bis(benzoyloxyethyl) terephthalate + H2O
terephthalate + benzoic acid + 2-hydroxyethylbenzoate + mono-(2-hydroxyethyl) terephthalate + bis-(2-hydroxyethyl) terephthalate
bisbenzoyloxyethyl terephthalate + H2O
terephthalic acid + mono(2-hydroxyethyl) terephthalate + bis(2-hydroxyethyl)terephthalate + benzoic acid + 2-hydroxyethyl benzoate
cutin + H2O
16-hydroxyhexadecanoic acid + 10,16-dihydroxyhexadecanoic acid + 9,10,18-trihydroxyoctadecanoic acid
dihexylphthalate + H2O
?
-
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
-
-
?
dipentyl phthalate + H2O
?
-
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
-
-
?
hexadecyl hexadecanoate + H2O
hexadecanoic acid + hexadecanol
-
weak activity
-
-
?
malathion + H2O
malathion monoacid + malathion diacid + ethanol
-
60% of initial 500 mg/l malathion are degraded within 0.5 h
diacid is the major degradation product
-
?
n-butyl benzyl phthalate + H2O
1,3-isobenzofurandione + n-butanol + benzyl alcohol
-
-
major product, less than 5% of byproducts such as dimethyl phthalate, butyl methyl phthalate
-
?
p-nitrophenyl caprate + H2O
p-nitrophenol + ?
concentration of substrate dispersion is 5 mM
-
-
?
p-nitrophenyl caproate + H2O
p-nitrophenol + ?
concentration of substrate dispersion is 5 mM
-
-
?
p-nitrophenyl laurate + H2O
p-nitrophenol + ?
concentration of substrate dispersion is 5 mM
-
-
?
p-nitrophenyl myristate + H2O
p-nitrophenol + ?
concentration of substrate dispersion is 5 mM
-
-
?
p-nitrophenyl palmitate + H2O
p-nitrophenol + ?
concentration of substrate dispersion is 5 mM
-
-
?
p-nitrophenyl propionate + H2O
p-nitrophenol + ?
concentration of substrate dispersion is 5 mM
-
-
?
p-nitrophenyl stearate + H2O
p-nitrophenol + ?
a lower concentration of p-nitrophenyl stearate (2.5 mM) is used due to its lower solubility
-
-
?
p-nitrophenyltetradecanoate + H2O
p-nitrophenol + tetradecanoate
-
-
-
-
?
poly(3-hydroxybutyrate-co-3-hydroxyvalerate) + H2O
3-hydroxybutyric acid + ?
poly(butylene succinate) is hydrolyzed to significantly higher extent than poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
-
-
?
poly(butylene succinate) + H2O
succinic acid + 1,4-butanediol + ?
poly(butylene succinate) is hydrolyzed to significantly higher extent than poly(3-hydroxybutyrate-co-3-hydroxyvalerate)
-
-
?
poly(ethylene terephthalate) + H2O
mono-(2-hydroxyethyl) terephthalate + terephthalic acid
polyethyleneterephthalate + H2O
terephthalate + benzoic acid + 2-hydroxyethylbenzoate + mono-(2-hydroxyethyl)terephthalate + bis-(2-hydroxyethyl)terephthalate
polyvinyl acetate + H2O
?
substrate used in papermaking and in synthetic toner or ink
-
-
?
triglyceride + H2O
?
-
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
-
-
?
tyrosol + vinyl butanoate
tyrosyl butanoate + vinyl alcohol
-
41.8% yield
-
-
?
tyrosol + vinyl decanoate
tyrosyl decanoate + vinyl alcohol
-
poor substrate
-
-
?
tyrosol + vinyl laurate
tyrosyl laurate + vinyl alcohol
-
poor substrate
-
-
?
tyrosol + vinyl propionate
tyrosyl propionate + vinyl alcohol
-
38.6% yield
-
-
?
2-hydroxyethyl benzoate + H2O
ethane-1,2-diol + benzoate
-
is hydrolyzed after 24 h of incubation of bisbenzoyloxyethyl terephthalate
-
-
?
2-hydroxyethyl benzoate + H2O
ethane-1,2-diol + benzoate
-
is hydrolyzed after 24 h of incubation of bisbenzoyloxyethyl terephthalate
-
-
?
4-nitrophenyl (16-methyl sulfonyl ester) hexadecanoate + H2O
4-nitrophenol + (16-methyl sulfonyl ester) hexadecanoate
-
-
-
-
?
4-nitrophenyl (16-methyl sulfonyl ester) hexadecanoate + H2O
4-nitrophenol + (16-methyl sulfonyl ester) hexadecanoate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
low activity
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
high activity
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
high activity
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
high activity
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
high activity
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
about 55% of the activity with 4-nitrophenyl acetate
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
about 55% of the activity with 4-nitrophenyl acetate
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
Thermothelomyces thermophilus DSM 1799
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
-
?
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
best 4-nitrophenyl ester substrate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
best 4-nitrophenyl ester substrate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
low activity
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
best 4-nitrophenyl ester substrate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
best 4-nitrophenyl ester substrate
-
-
?
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
-
-
-
?
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
-
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
-
-
-
?
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
-
high activity
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
-
-
-
?
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
low activity
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
-
high activity
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
low activity
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
about 50% of the activity with 4-nitrophenyl acetate
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
about 50% of the activity with 4-nitrophenyl acetate
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
high activity
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
-
-
-
?
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
low activity
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
-
-
-
?
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
about 30% of the activity with 4-nitrophenyl acetate
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
about 30% of the activity with 4-nitrophenyl acetate
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
low activity
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
low activity
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
low activity
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
low activity
-
-
?
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
-
-
-
?
4-nitrophenyl pentanoate + H2O
4-nitrophenol + pentanoate
53% of the activity with 4-nitrophenyl butanoate
-
-
?
4-nitrophenyl pentanoate + H2O
4-nitrophenol + pentanoate
Thermothelomyces thermophilus DSM 1799
53% of the activity with 4-nitrophenyl butanoate
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
high activity
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
high activity
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
35% of the activity with 4-nitrophenyl butanoate
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
Thermothelomyces thermophilus DSM 1799
35% of the activity with 4-nitrophenyl butanoate
-
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + pentanoate
-
-
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
-
-
-
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
-
-
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
-
-
-
?
bis(2-hydroxyethyl)terephthalate + H2O
?
-
fast hydrolysis after treatment for 30 min
-
-
?
bis(2-hydroxyethyl)terephthalate + H2O
?
-
hydrolysis after treatment for 5 h
-
-
?
bis(benzoyloxyethyl) terephthalate + H2O
terephthalate + benzoic acid + 2-hydroxyethylbenzoate + mono-(2-hydroxyethyl) terephthalate + bis-(2-hydroxyethyl) terephthalate
-
-
-
?
bis(benzoyloxyethyl) terephthalate + H2O
terephthalate + benzoic acid + 2-hydroxyethylbenzoate + mono-(2-hydroxyethyl) terephthalate + bis-(2-hydroxyethyl) terephthalate
-
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
-
-
-
?
bis(benzoyloxyethyl) terephthalate + H2O
terephthalate + benzoic acid + 2-hydroxyethylbenzoate + mono-(2-hydroxyethyl) terephthalate + bis-(2-hydroxyethyl) terephthalate
-
product ratios of wild-type and mutant enzymes, overview
-
?
bisbenzoyloxyethyl terephthalate + H2O
terephthalic acid + mono(2-hydroxyethyl) terephthalate + bis(2-hydroxyethyl)terephthalate + benzoic acid + 2-hydroxyethyl benzoate
-
-
-
-
?
bisbenzoyloxyethyl terephthalate + H2O
terephthalic acid + mono(2-hydroxyethyl) terephthalate + bis(2-hydroxyethyl)terephthalate + benzoic acid + 2-hydroxyethyl benzoate
-
-
-
-
?
cutin + H2O
16-hydroxyhexadecanoic acid + 10,16-dihydroxyhexadecanoic acid + 9,10,18-trihydroxyoctadecanoic acid
-
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
16-hydroxyhexadecanoic acid + 10,16-dihydroxyhexadecanoic acid + 9,10,18-trihydroxyoctadecanoic acid
-
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
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
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
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
-
-
main products: hexadecaoic acid, octadecaoic acid, and 10,16-dihydroxyhexadecaoic acid
-
?
cutin + H2O
cutin monomers
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
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
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
-
-
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
-
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
-
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
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
concentration of substrate dispersion is 5 mM
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
concentration of substrate dispersion is 5 mM
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
-
-
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
-
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 valerate + H2O
p-nitrophenol + pentanoate
concentration of substrate dispersion is 5 mM
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-
?
p-nitrophenyl valerate + H2O
p-nitrophenol + pentanoate
-
-
-
?
p-nitrophenylbutanoate + H2O
p-nitrophenol + butanoate
-
-
-
-
?
poly(ethylene terephthalate) + H2O
mono-(2-hydroxyethyl) terephthalate + terephthalic acid
-
-
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
-
?
poly(ethylene terephthalate) + H2O
mono-(2-hydroxyethyl) terephthalate + terephthalic acid
-
-
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
-
?
poly(ethylene terephthalate) + H2O
mono-(2-hydroxyethyl) terephthalate + terephthalic acid
-
-
no formation of bis(2-hydroxyethyl) terephthalate. Terephthalic acid is the major hydrolysis product for Thf42_Cut1
-
?
poly(ethylene terephthalate) + H2O
mono-(2-hydroxyethyl) terephthalate + terephthalic acid
-
-
no formation of bis(2-hydroxyethyl) terephthalate. Terephthalic acid is the major hydrolysis product for Thf42_Cut1
-
?
poly(methyl acrylate) + H2O
poly(acrylic acid) + methanol
-
-
-
?
polyethyleneterephthalate + H2O
terephthalate + benzoic acid + 2-hydroxyethylbenzoate + mono-(2-hydroxyethyl)terephthalate + bis-(2-hydroxyethyl)terephthalate
-
-
-
?
polyethyleneterephthalate + H2O
terephthalate + benzoic acid + 2-hydroxyethylbenzoate + mono-(2-hydroxyethyl)terephthalate + bis-(2-hydroxyethyl)terephthalate
-
product ratios of wild-type and mutant enzymes, overview
-
?
polyethyleneterephthalate + H2O
terephthalate + benzoic acid + 2-hydroxyethylbenzoate + mono-(2-hydroxyethyl)terephthalate + bis-(2-hydroxyethyl)terephthalate
-
-
-
?
polyethyleneterephthalate + H2O
terephthalate + benzoic acid + 2-hydroxyethylbenzoate + mono-(2-hydroxyethyl)terephthalate + bis-(2-hydroxyethyl)terephthalate
-
product ratios of wild-type and mutant enzymes, overview
-
?
tributyrin + H2O
butyric acid + 1,2-dibutyrylglycerol
about 85% of the activity with tricaproin, mutant S226P
-
-
?
tributyrin + H2O
butyric acid + 1,2-dibutyrylglycerol
Saccharomonospora viridis AHK190
about 85% of the activity with tricaproin, mutant S226P
-
-
?
cutin + H2O
additional information
-
-
-
dihydroxyhexadecanoic acid, cutin monomer + cutin oligomers
?
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
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
?
-
-
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
-
-
?
additional information
?
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
enzyme preferably hydrolyzes short-chain length esters (C2-C4), but it also displays a slight affinity for long-chain length esters (C14-C18)
-
-
?
additional information
?
-
-
enzyme preferably hydrolyzes short-chain length esters (C2-C4), but it also displays a slight affinity for long-chain length esters (C14-C18)
-
-
?
additional information
?
-
enzyme preferably hydrolyzes short-chain length esters (C2-C4), but it also displays a slight affinity for long-chain length esters (C14-C18)
-
-
?
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
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
?
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
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
-
-
?
additional information
?
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
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
?
-
-
the enzyme prefers 4-nitrophenyl ester substrates with chain lengths of C4-C6, production and assay method optimization, overview
-
-
?
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
?
-
-
the enzyme prefers 4-nitrophenyl ester substrates with chain lengths of C4-C6, production and assay method optimization, overview
-
-
?
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)
-
-
?
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)
-
-
?
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
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
-
-
?
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
-
the enzyme is capable of hydrolyzing polyethylene terephthalate model substrates and synthetic polymers
-
-
?
additional information
?
-
-
no hydrolysis of p-nitrophenyl palmitate
-
-
?
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
-
catalytic triad: S120, H188, D175. Presence of a preformed oxyanion hole
-
-
?
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)
-
-
?
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)
-
-
?
additional information
?
-
cutinases are capable of catalyzing esterification and transesterification. The enzyme prefers triacylglyceride substrates with short acyl groups
-
-
?
additional information
?
-
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
?
-
-
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 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
-
-
?
additional information
?
-
-
the enzyme catalyzes the transesterification of triolein and methanol, overview
-
-
?
additional information
?
-
Helminthosporium sativum
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
-
shows promising activity in polymerization reactions
-
-
?
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
?
-
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
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
?
-
enzyme additionally shows cellulose acetate deacylation activity
-
-
?
additional information
?
-
-
enzyme additionally shows cellulose acetate deacylation activity
-
-
?
additional information
?
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
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
-
-
?
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
-
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
?
-
-
does not act on tripalmitoyl glycerol or trioleoyl glycerol
-
-
?
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
?
-
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
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
-
-
?
additional information
?
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
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 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 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
?
-
-
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
?
-
-
the optimum ratio of butyrate, acetate, and lactate is 4:1:3
-
-
?
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
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
?
-
-
substrate binding, modelling and docking study, overview
-
-
?
additional information
?
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
-
substrate binding, modelling and docking study, overview
-
-
?
additional information
?
-
-
the enzyme exhibits a broad substrate specificity against plant cutin, synthetic polyesters, insoluble triglycerides, and soluble esters
-
-
?
additional information
?
-
-
substrate binding, modelling and docking study,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
-
-
?
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
-
the enzyme has hydrolytic activity toward phospholipids of the cell membrane, cf. EC 3.1.1.3
-
-
?
additional information
?
-
-
enzyme additionally catalyzes the transesterification reaction of cellulose with triolein
-
-
?
additional information
?
-
-
enzyme catalyzes esterification reactions of acids of C3-C8 and alcohols of C1-C6 chain length
-
-
?
additional information
?
-
-
substrate binding, modelling and docking study,overview
-
-
?
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
-
the enzyme shows polyethylene terephthalate-degrading activity
-
-
?
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
