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(ethylene terephthalate)n + H2O
ethylene glycol + ?
-
-
-
?
(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
-
-
?
2-hydroxyethyl benzoate + H2O
ethane-1,2-diol + benzoate
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 acetate + H2O
4-nitrophenol + acetate
4-nitrophenyl butanoate + H2O
4-nitrophenol + butanoate
4-nitrophenyl butyrate + H2O
4-nitrophenol + butyrate
4-nitrophenyl caproate + H2O
4-nitrophenol + caproate
4-nitrophenyl caprylate + H2O
4-nitrophenol + caprylate
4-nitrophenyl decanoate + H2O
4-nitrophenol + decanoate
4-nitrophenyl dodecanoate + H2O
4-nitrophenol + dodecanoate
4-nitrophenyl hexanoate
4-nitrophenol + hexanoate
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
4-nitrophenyl laurate
4-nitrophenol + laurate
-
-
-
-
?
4-nitrophenyl laurate + H2O
4-nitrophenol + laurate
4-nitrophenyl myristate + H2O
4-nitrophenol + myristate
4-nitrophenyl octanoate + H2O
4-nitrophenol + octanoate
4-nitrophenyl palmitate + H2O
4-nitrophenol + palmitate
4-nitrophenyl pentanoate + H2O
4-nitrophenol + pentanoate
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
-
?
4-nitrophenyl propionate + H2O
4-nitrophenol + propionate
4-nitrophenyl stearate + H2O
4-nitrophenol + stearate
about 28% of the activity with 4-nitrophenyl acetate
-
-
?
4-nitrophenyl valerate
4-nitrophenol + pentanoate
4-nitrophenyl valerate + H2O
4-nitrophenol + pentanoate
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
4-nitrophenylbutyrate + H2O
4-nitrophenol + butyrate
-
-
-
-
?
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
-
-
-
-
?
beta-butyrolactone
?
-
ring-opening polymerizations
-
-
?
birch bark suberin + H2O
?
-
-
-
?
bis(2-hydroxyethyl)terephthalate + H2O
?
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
butanol + butanoate
butyl butanoate + H2O
cutin + H2O
16-hydroxyhexadecanoic acid + 10,16-dihydroxyhexadecanoic acid + 9,10,18-trihydroxyoctadecanoic acid
cutin + H2O
cutin monomers
cutin + H2O
palmitate + ?
-
-
-
?
cyclohexyl hexadecanoate + H2O
hexadecanoic acid + cyclohexanol
-
-
-
-
?
delta-valerolactone
?
-
ring-opening polymerizations
-
-
?
dihexyl phthalate + H2O
1,3-isobenzofurandione + ?
-
-
-
-
?
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
-
-
?
dimethyl adipate + 1,4-butanediol
?
-
-
-
?
dimethyl adipate + 1,4-decanediol
?
-
-
-
?
dimethyl adipate + 1,4-hexanediol
?
-
-
-
?
dimethyl adipate + 1,4-octanediol
?
-
-
-
?
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
-
-
?
dipropyl phthalate + H2O
1,3-isobenzofurandione + propanol
-
-
-
-
?
epsilon-caprolactone
?
-
ring-opening polymerizations
-
-
?
ethanol + caproate
ethyl caproate + H2O
-
-
-
-
?
ethyl butyrate + H2O
butyric acid + ethanol
-
-
-
?
ethyl caprylate + H2O
caprylic acid + ethanol
-
-
-
?
hexadecyl hexadecanoate + H2O
hexadecanoic acid + hexadecanol
-
weak activity
-
-
?
malathion + H2O
?
-
-
-
-
?
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
-
?
methyl acetate + H2O
acetic acid + methanol
-
-
-
?
methyl butyrate + H2O
butyric acid + methanol
-
-
-
?
methyl caproate + H2O
caproic acid + methanol
-
-
-
?
methyl caprylate + H2O
caprylic acid + methanol
-
-
-
?
methyl decanoate + H2O
decanoic acid + methanol
-
-
-
?
methyl hexadecanoate + H2O
hexadecanoic acid + methanol
-
-
-
-
?
methyl laurate + H2O
lauric acid + methanol
-
-
-
?
methyl myristate + H2O
myristic acid + methanol
-
-
-
?
methyl propionate + H2O
propionic acid + methanol
-
-
-
?
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
-
?
omega-pentadecalactone
?
-
ring-opening polymerizations
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
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 hexanoate + H2O
p-nitrophenol + hexanoate
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-nitrophenyl valerate + H2O
p-nitrophenol + pentanoate
p-nitrophenylbutanoate + H2O
p-nitrophenol + butanoate
p-nitrophenyldecanoate + H2O
p-nitrophenol + decanoate
p-nitrophenylhexadecanoate + H2O
p-nitrophenol + hexadecanoate
-
-
-
-
?
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 succinaste) + H2O
?
-
-
-
?
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(caprolactone) + H2O
?
poly(epsilon-caprolactone) + H2O
?
poly(ethyl acrylate) + H2O
poly(acrylic acid) + ethanol
poly(ethylene terephthalate) + H2O
mono-(2-hydroxyethyl) terephthalate + terephthalic acid
poly(ethylene terephthalate) + H2O
terephthalate + ?
-
-
-
-
?
poly(methyl acrylate) + H2O
poly(acrylic acid) + methanol
polyamide + H2O
?
-
-
-
?
polybutylene succinate co-adipate + H2O
?
-
-
-
?
polyethylene terephthalate + H2O
?
polyethylene terephthalate + H2O
terephthalate + ?
-
-
-
?
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
-
-
?
suberin + H2O
?
9,10-epoxy-18-hydroxy 5 octadecanoic acid
-
-
?
tributyrin + H2O
butyric acid + 1,2-dibutyrylglycerol
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
-
-
?
trioctanoin + H2O
?
-
-
-
?
tripalmitin + H2O
?
-
-
-
?
tristearin + H2O
?
-
-
-
?
tritiated apple cutin + H2O
?
-
-
-
?
tyrosol + vinyl acetate
tyrosyl acetate + vinyl alcohol
-
-
-
-
?
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
-
-
?
cutin + H2O
additional information
-
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
-
-
-
?
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
-
low 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
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
-
-
-
?
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 acetate + H2O
4-nitrophenol + acetate
-
-
-
-
?
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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 butyrate + H2O
4-nitrophenol + butyrate
-
-
-
?
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
-
-
-
-
?
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 dodecanoate + H2O
4-nitrophenol + dodecanoate
-
-
-
-
?
4-nitrophenyl dodecanoate + H2O
4-nitrophenol + dodecanoate
-
-
-
-
?
4-nitrophenyl hexanoate
4-nitrophenol + hexanoate
-
-
-
-
?
4-nitrophenyl hexanoate
4-nitrophenol + hexanoate
-
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
-
-
?
4-nitrophenyl hexanoate + H2O
4-nitrophenol + hexanoate
-
-
-
?
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
-
-
-
?
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 octanoate + H2O
4-nitrophenol + octanoate
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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 pentanoate + H2O
4-nitrophenol + pentanoate
53% of the activity with 4-nitrophenyl butanoate
-
-
?
4-nitrophenyl pentanoate + H2O
4-nitrophenol + pentanoate
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
35% of the activity with 4-nitrophenyl butanoate
-
-
?
4-nitrophenyl valerate
4-nitrophenol + pentanoate
-
-
-
-
?
4-nitrophenyl valerate
4-nitrophenol + pentanoate
-
-
-
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + pentanoate
-
-
-
?
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
-
-
-
-
?
4-nitrophenyl valerate + H2O
4-nitrophenol + valerate
-
-
-
?
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
-
-
-
-
?
butanol + butanoate
butyl butanoate + H2O
-
-
-
?
butanol + butanoate
butyl butanoate + H2O
-
-
-
-
?
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 + H2O
cutin monomers
-
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
?
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
-
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
?
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
Helminthosporium sativum
-
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
cutin + H2O
cutin monomers
-
-
-
?
cutin + H2O
cutin monomers
apple cutin
-
-
?
cutin + H2O
cutin monomers
apple cutin
-
-
?
cutin + H2O
cutin monomers
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
concentration of substrate dispersion is 5 mM
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
-
-
-
?
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
-
-
-
?
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
-
-
?
p-nitrophenyl butyrate + H2O
p-nitrophenol + butyrate
-
-
-
-
?
p-nitrophenyl hexanoate + H2O
p-nitrophenol + hexanoate
-
-
-
-
?
p-nitrophenyl hexanoate + H2O
p-nitrophenol + hexanoate
-
-
-
-
?
p-nitrophenyl valerate + H2O
p-nitrophenol + pentanoate
concentration of substrate dispersion is 5 mM
-
-
?
p-nitrophenyl valerate + H2O
p-nitrophenol + pentanoate
-
-
-
?
p-nitrophenyl valerate + H2O
p-nitrophenol + pentanoate
-
-
-
?
p-nitrophenylbutanoate + H2O
p-nitrophenol + butanoate
-
-
-
-
?
p-nitrophenylbutanoate + H2O
p-nitrophenol + butanoate
-
-
-
-
?
p-nitrophenylbutanoate + H2O
p-nitrophenol + butanoate
-
-
-
-
?
p-nitrophenylbutanoate + H2O
p-nitrophenol + butanoate
-
-
-
-
?
p-nitrophenylbutanoate + H2O
p-nitrophenol + butanoate
-
-
-
?
p-nitrophenylbutanoate + H2O
p-nitrophenol + butanoate
-
-
-
-
?
p-nitrophenylbutanoate + H2O
p-nitrophenol + butanoate
-
-
-
-
?
p-nitrophenyldecanoate + H2O
p-nitrophenol + decanoate
-
-
-
-
?
p-nitrophenyldecanoate + H2O
p-nitrophenol + decanoate
-
-
-
-
?
poly(caprolactone) + H2O
?
-
-
-
-
?
poly(caprolactone) + H2O
?
-
-
-
?
poly(caprolactone) + H2O
?
-
-
-
?
poly(caprolactone) + H2O
?
-
-
-
-
?
poly(caprolactone) + H2O
?
-
-
-
?
poly(caprolactone) + H2O
?
-
-
-
?
poly(caprolactone) + H2O
?
-
-
-
?
poly(caprolactone) + H2O
?
-
-
-
-
?
poly(epsilon-caprolactone) + H2O
?
-
-
-
?
poly(epsilon-caprolactone) + H2O
?
-
-
-
?
poly(ethyl acrylate) + H2O
poly(acrylic acid) + ethanol
-
-
-
?
poly(ethyl acrylate) + H2O
poly(acrylic acid) + ethanol
-
-
-
?
poly(ethyl acrylate) + H2O
poly(acrylic acid) + ethanol
-
-
-
-
?
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
-
-
-
?
poly(methyl acrylate) + H2O
poly(acrylic acid) + methanol
-
-
-
?
poly(methyl acrylate) + H2O
poly(acrylic acid) + methanol
-
-
-
-
?
polyethylene terephthalate + H2O
?
-
-
-
?
polyethylene terephthalate + H2O
?
-
-
-
?
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
?
-
-
-
?
tributyrin + H2O
?
-
-
-
?
tributyrin + H2O
?
-
-
-
-
?
tributyrin + H2O
?
-
-
-
-
?
tributyrin + H2O
?
-
-
-
?
tributyrin + H2O
?
-
-
-
-
?
tributyrin + H2O
?
-
-
-
-
?
tributyrin + H2O
?
-
-
-
-
?
tributyrin + H2O
butyric acid + 1,2-dibutyrylglycerol
-
-
-
?
tributyrin + H2O
butyric acid + 1,2-dibutyrylglycerol
about 85% of the activity with tricaproin, mutant S226P
-
-
?
tributyrin + H2O
butyric acid + 1,2-dibutyrylglycerol
about 85% of the activity with tricaproin, mutant S226P
-
-
?
tricaproin + H2O
?
-
-
-
?
tricaproin + H2O
?
-
-
-
?
tricaproin + H2O
?
-
-
-
-
?
tricaproin + H2O
?
-
-
-
-
?
tricaprylin + H2O
?
-
-
-
?
tricaprylin + H2O
?
-
-
-
?
tricaprylin + H2O
?
-
-
-
-
?
triolein + H2O
?
-
-
-
?
triolein + H2O
?
-
-
-
-
?
triolein + H2O
?
-
-
-
-
?
triolein + H2O
?
-
-
-
-
?
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
-
-
-
-
-
?
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
-
-
-
-
-
?
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
-
-
-
-
-
?
cutin + H2O
additional information
-
-
-
-
?
cutin + H2O
additional information
-
-
-
-
-
?
cutin + H2O
additional information
-
-
-
dihydroxyhexadecanoic acid, cutin monomer + cutin oligomers
?
cutin + H2O
additional information
-
-
-
-
-
?
cutin + H2O
additional information
-
-
-
-
-
?
cutin + H2O
additional information
-
-
apple cutin
-
-
?
cutin + H2O
additional information
-
-
-
-
-
?
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
-
cutinases are capable of catalyzing esterification and transesterification
-
-
?
additional information
?
-
-
induced by cutin
-
-
?
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
?
-
-
constitutive enzyme
-
-
?
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
?
-
-
constitutive enzyme
-
-
?
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
?
-
-
-
-
-
?
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
-
-
?
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(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
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 7°C
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
butyl 4-nitrophenyl undecylphosphonate
in the absence of surfactant, the rate of cutinase inhibition is very low. The addition of beta-octylglucoside is required to trigger the inhibition of cutinase, which is completely inactivated after 60 min
chlorpyrifos-methyl
-
upon chloroperoxidase oxidation, chlorpyrifos-methyl shows a very strong cutinase inhibition as compared to the corresponding oxon standard
chlorpyrifos-methyl oxon
-
-
CrCl2
99% inhibition at 1 mM; 99% inhibition at 1 mM
CuSO4
26% inhibition at 1 mM; 32% inhibition at 1 mM
D-glucose
Thcut1 mRNA is repressed by glucose
deoxycholate
24% inhibition at 10 mM; 25% inhibition at 10 mM
Diethyl p-nitrophenyl phosphate
diethyl-p-nitrophenyl phosphate
-
diethyldicarbonate
54% inhibition at 1 mM; 56% inhibition at 1 mM
diisopropyl fluorophosphate
dioxan
-
23% inhibition at 75% v/v
DMSO
-
49% inhibition at 75% v/v
E600
in the absence of surfactant, no inhibition is observed with E600. The addition of beta-octylglucoside is required to trigger the inhibition of cutinase, which is completely inactivated after 12 min
EDTA
10 mM, 42% residual acivity
ethanol
-
97% inhibition at 75% v/v
ethylene glycol
cleavage product accumulation decreases the activity of cutinase during PET hydrolysis
Fe3+
10 mM, 43% residual acivity
FeSO4
55% inhibition at 1 mM; 55% inhibition at 1 mM
hexyl acetate
63% inhibition at 40% v/v; 83% inhibition at 40% v/v
HgCl2
99% inhibition at 1 mM; 99% inhibition at 1 mM
Isopropanol
-
complete inhibition at 75% v/v
K+
1 mM, 42% residual acivity
MgCl2
15% inhibition at 1 mM; 8% inhibition at 1 mM
Mn2+
-
slight inhibition at 1 mM
Na+
1 mM, 39% residual acivity
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
PbCl2
53% inhibition at 1 mM; 54% inhibition at 1 mM
phenylboronic acid
-
5 mM, 63% inhibition, competitive
RbCl
93% inhibition at 1 mM; 95% inhibition at 1 mM
sodium bis(2-ethylhexyl)ester sulfosuccinic acid
-
pseudo-competitive inhibitor
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 80
10 mM, 48% residual acivity
Tween-20
28% inhibition at 1 mM; 35% inhibition at 1 mM
Tween-80
24% inhibition at 1 mM; 60% inhibition at 1 mM
ZnSO4
59% inhibition at 1 mM; 65% inhibition at 1 mM
3-phenethylthio-1,1,1-trifluoropropan-2-one
-
3-phenethylthio-1,1,1-trifluoropropan-2-one
-
Ca2+
1 mM, 47% residual acivity
Ca2+
-
inhibits 6% at 1 mM
Ca2+
-
inhibits isozyme Tfu 0882 28% and isozyme Tfu 0883 18% at 1 mM
Cr3+
-
inhibits 72% at 1 mM
Cr3+
-
inhibits isozyme Tfu 0882 89% and isozyme Tfu 0883 90% at 1 mM
Cu2+
10 mM, 52% residual acivity
Cu2+
-
85% inhibition at 1 mM
Cu2+
-
inhibits 17% at 1 mM
Cu2+
1 mM, 82% residual activity
Dichloromethane
-
78% inhibition at 75% v/v
Dichloromethane
61% inhibition at 40% v/v; 74% inhibition at 40% v/v
Diethyl p-nitrophenyl phosphate
E600
Diethyl p-nitrophenyl phosphate
-
covalent
Diethyl p-nitrophenyl phosphate
E600
diisopropyl fluorophosphate
-
0.025 mM, complete inhibition
diisopropyl fluorophosphate
-
-
diisopropyl fluorophosphate
-
1 mM, 90% inhibition
diisopropyl fluorophosphate
-
102 nM, 90% inhibition
Fe2+
-
20% inhibition at 1 mM
Fe2+
-
slight inhibition at 1 mM
Fe2+
-
inhibits 54% at 1 mM
Fe2+
-
inhibits isozyme Tfu 0882 45% and isozyme Tfu 0883 36% at 1 mM
glycerol
-
-
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
Hg2+
-
inhibits completely at 1 mM
Hg2+
-
inhibits completely at 1 mM
Hg2+
-
inhibits isozyme Tfu 0882 and isozyme Tfu 0883 completely at 1 mM
methanol
-
90% inhibition at 75% v/v
methanol
-
inhibits the transesterification reaction of the enzyme
methanol
8% inhibition at 40% v/v
Mg2+
1 mM, 42% residual acivity
Mg2+
-
slight inhibition at 1 mM
Mg2+
-
inhibits 11% at 1 mM
Mg2+
-
inhibits isozyme Tfu 0882 34%
n-hexane
-
18.5% inhibition at 75% v/v
n-hexane
10% inhibition at 40% v/v
Ni2+
-
inhibits 7% at 1 mM
Ni2+
1 mM, 74% residual activity
paraoxon
-
0.1 mM, complete inhibition
Pb2+
-
inhibits 39% at 1 mM
Pb2+
-
inhibits isozyme Tfu 0882 48% and isozyme Tfu 0883 52% at 1 mM
PMSF
10 mM, 47% residual acivity
PMSF
1 mM, less than 20% residual activity
PMSF
-
95% inhibition at 1 mM
PMSF
48% inhibition at 1 mM; 59% inhibition at 1 mM
SDS
10 mM, 47% residual acivity
SDS
1 mM, less than 5% residual activity
SDS
30% inhibition at 1 mM; 9% inhibition at 1 mM
SDS
1 mM, 16% residual activity
Urea
17% inhibition at 1 mM; 30% inhibition at 1 mM
Zn2+
-
18% inhibition at 1 mM
Zn2+
-
inhibits 18% at 1 mM
Zn2+
-
inhibits isozyme Tfu 0882 50% and isozyme Tfu 0883 56% at 1 mM
additional information
not inhibitory: dithiothreitol, EDTA, urea
-
additional information
-
no inhibition by EDTA, Triton X-100 and Tween 80, or by 75% v/v chloroform, isooctane, isoamyl alcohol, or butanol
-
additional information
crystallization and preliminary X-ray analysis of cutinase-inhibitor complexes
-
additional information
-
crystallization and preliminary X-ray analysis of cutinase-inhibitor complexes
-
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
-
inhibition by organophosphate pesticides. Carbamate pesticides reveal an efficient cutinase inhibitor effect, though less potent than the organophosphates
-
additional information
not inhibitory: EDTA up to 10 mM
-
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
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
-
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
structure comparisons of isozymes Cut1 and Cut2 during denaturation and unfolding, overview; structure comparisons of isozymes Cut1 and Cut2 during denaturation and unfolding, overview
-
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0.00067 - 63
4-nitrophenyl acetate
0.7 - 2.34
4-nitrophenyl butanoate
0.00021 - 59.2
4-nitrophenyl butyrate
0.88
4-nitrophenyl caproate
-
pH 4.0, 50°C
7.24
4-nitrophenyl caprylate
-
pH 8.0, 25°C, recombinant enzyme
0.00029 - 0.89
4-nitrophenyl hexanoate
2.1 - 7.14
4-nitrophenyl laurate
7.25
4-nitrophenyl myristate
-
pH 8.0, 25°C, recombinant enzyme
0.207 - 1.7
4-nitrophenyl octanoate
2.246
4-nitrophenyl palmitate
-
pH 7.5, 30°C, recombinant enzyme
1.61
4-nitrophenyl pentanoate
pH 8.5, 30°C
1.41
4-nitrophenyl propionate
pH 8.5, 30°C
0.00004 - 55.3
4-nitrophenyl valerate
0.33
p-nitrophenyl acetate
-
0.000121 - 4.33
p-nitrophenyl butyrate
0.085
p-nitrophenyl palmitate
-
0.82
p-nitrophenyl valerate
-
0.27 - 1.68
p-nitrophenylbutanoate
0.36 - 3.98
p-nitrophenyldecanoate
0.45 - 3.55
p-nitrophenyldodecanoate
4.54
p-nitrophenylhexadecanoate
-
-
2.27
p-nitrophenyltetradecanoate
-
-
additional information
additional information
-
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
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
pH and temperature not specified in the publication
0.213
4-nitrophenyl acetate
pH and temperature not specified in the publication
0.8
4-nitrophenyl acetate
pH 7.0, 25°C, recombinant mutant R187K
0.9
4-nitrophenyl acetate
-
-
1.2
4-nitrophenyl acetate
pH 7.0, 25°C, recombinant mutant R19S
1.2
4-nitrophenyl acetate
pH 7.0, 25°C, recombinant mutant R19S/R29N/A30V
1.3
4-nitrophenyl acetate
pH 7.0, 25°C, recombinant mutant R29N
1.3
4-nitrophenyl acetate
pH 7.0, 25°C, recombinant mutant R29N/A30V
1.4
4-nitrophenyl acetate
wild-type, pH 7.0, 25°C
1.5
4-nitrophenyl acetate
pH 7.0, 25°C, recombinant isozyme
1.5
4-nitrophenyl acetate
pH 7.0, 25°C, recombinant mutant Q65E
1.5
4-nitrophenyl acetate
fusion protein Cut1-HFB9b, pH 7.0, 25°C
1.7
4-nitrophenyl acetate
pH 7.0, 25°C, recombinant mutant A30V
1.9
4-nitrophenyl acetate
pH 7.0, 25°C, recombinant mutant L183A
1.9
4-nitrophenyl acetate
pH 7.0, 25°C, recombinant wild-type isozyme
2.3
4-nitrophenyl acetate
fusion protein Cut1-HFB7, pH 7.0, 25°C
2.4
4-nitrophenyl acetate
fusion protein Cut1-HFB4, pH 7.0, 25°C
3
4-nitrophenyl acetate
-
without surfactant
5.4
4-nitrophenyl acetate
-
pH 6.0, 40°C
6.8
4-nitrophenyl acetate
-
cutinase I
6.88
4-nitrophenyl acetate
pH 9.0, 37°C
8.3
4-nitrophenyl acetate
-
pH 4.0, 50°C
9.7
4-nitrophenyl acetate
-
cutinase II
63
4-nitrophenyl acetate
-
pH 8.0, 25°C, recombinant enzyme
0.7
4-nitrophenyl butanoate
-
pH 6.0, 40°C
0.72
4-nitrophenyl butanoate
-
pH not specified in the publication, temperature not specified in the publication
0.8
4-nitrophenyl butanoate
wild-type, pH 7.0, 25°C
0.8
4-nitrophenyl butanoate
fusion protein Cut1-HFB9b, pH 7.0, 25°C
0.9
4-nitrophenyl butanoate
fusion protein Cut1-HFB7, pH 7.0, 25°C
1.1
4-nitrophenyl butanoate
-
pH 4.0, 50°C
1.3
4-nitrophenyl butanoate
fusion protein Cut1-HFB4, pH 7.0, 25°C
2.34
4-nitrophenyl butanoate
pH 8.5, 30°C
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, 25°C
0.00196
4-nitrophenyl butyrate
-
pH 7.5, 25°C
0.0025
4-nitrophenyl butyrate
-
pH 7.5, 25°C
0.00896
4-nitrophenyl butyrate
-
pH 7.5, 25°C
0.029
4-nitrophenyl butyrate
-
pH 7.5, 25°C
0.18
4-nitrophenyl butyrate
-
pH 8.0, 50°C, recombinant mutant C275A/C292A, absence of 1% PEG
0.19
4-nitrophenyl butyrate
-
pH 8.0, 70°C, recombinant mutant C275A/C292A, absence of 1% PEG
0.21
4-nitrophenyl butyrate
-
pH 8.0, 50°C, recombinant wild-type enzyme, absence of 1% PEG
0.22
4-nitrophenyl butyrate
-
pH 8.0, 30°C, recombinant wild-type enzyme, absence of 1% PEG
0.24
4-nitrophenyl butyrate
-
pH 8.0, 70°C, recombinant wild-type enzyme, absence of 1% PEG
0.25
4-nitrophenyl butyrate
-
pH 8.0, 30°C, recombinant mutant C275A/C292A, absence of 1% PEG
0.25
4-nitrophenyl butyrate
-
pH 8.0, 70°C, recombinant wild-type enzyme, absence of 1% PEG
0.27
4-nitrophenyl butyrate
-
pH 8.0, 30°C, recombinant wild-type enzyme, presence of 1% PEG
0.27
4-nitrophenyl butyrate
-
pH 8.0, 50°C, recombinant wild-type enzyme, presence of 1% PEG
0.272
4-nitrophenyl butyrate
-
pH 8.0, 60°C, recombinant cutinase FspC
0.454
4-nitrophenyl butyrate
-
pH 7.5, 30°C, recombinant enzyme
0.505
4-nitrophenyl butyrate
-
pH 8.0, 60°C, isozyme Tfu 0883
0.673
4-nitrophenyl butyrate
-
pH 8.0, 60°C, isozyme Tfu 0882
0.8
4-nitrophenyl butyrate
pH 7.0, 25°C, recombinant isozyme
1
4-nitrophenyl butyrate
pH 7.0, 25°C, recombinant mutant R29N/A30V
1.1
4-nitrophenyl butyrate
pH 7.0, 25°C, recombinant mutant A30V
1.4
4-nitrophenyl butyrate
pH 7.0, 25°C, recombinant mutant R19S/R29N/A30V
1.67
4-nitrophenyl butyrate
pH 4.5, 25°C, recombinant enzyme
2
4-nitrophenyl butyrate
pH 7.0, 25°C, recombinant mutant R29N
2.1
4-nitrophenyl butyrate
pH 7.0, 25°C, recombinant mutant L183A
2.2
4-nitrophenyl butyrate
pH 7.0, 25°C, recombinant mutant R19S
2.6
4-nitrophenyl butyrate
pH 7.0, 25°C, recombinant mutant Q65E
3.4
4-nitrophenyl butyrate
pH 7.0, 25°C, recombinant wild-type isozyme
4
4-nitrophenyl butyrate
pH 7.0, 25°C, recombinant mutant R187K
20
4-nitrophenyl butyrate
-
pH 8.0, 25°C, recombinant enzyme
59.2
4-nitrophenyl butyrate
pH and temperature not specified in the publication
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
2.1
4-nitrophenyl laurate
-
pH 6.0, 40°C
7.14
4-nitrophenyl laurate
-
pH 8.0, 25°C, recombinant enzyme
0.207
4-nitrophenyl octanoate
-
pH 7.5, 30°C, recombinant enzyme
0.59
4-nitrophenyl octanoate
-
cutinase II
0.88
4-nitrophenyl octanoate
-
cutinase I
1.7
4-nitrophenyl octanoate
-
-
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
55.3
4-nitrophenyl valerate
pH and temperature not specified in the publication
0.000121
p-nitrophenyl butyrate
20°C, 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
-
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
0.27
p-nitrophenylbutanoate
-
-
0.35
p-nitrophenylbutanoate
-
-
0.35
p-nitrophenylbutanoate
-
cutinase I
0.47
p-nitrophenylbutanoate
-
without surfactant
0.75
p-nitrophenylbutanoate
-
cutinase II
1.23
p-nitrophenylbutanoate
36°C, wild-type
1.45
p-nitrophenylbutanoate
36°C, mutant H173L
1.5
p-nitrophenylbutanoate
36°C, mutant S103T
1.68
p-nitrophenylbutanoate
36°C, 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
-
-
additional information
additional information
-
Km-values in presence of surfactants
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
steady-state kinetic analysis
-
additional information
additional information
-
comparison of kinetics of cutinases from different organisms, overview
-
additional information
additional information
-
comparison of kinetics of cutinases from different organisms, overview
-
additional information
additional information
-
comparison of kinetics of cutinases from different organisms, overview
-
additional information
additional information
-
comparison of kinetics of cutinases from different organisms, overview
-
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
-
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
-
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0.004
4-nitrophenyl palmitate, esterase activity of the recombinant THCUT1 protein against different chromogenic substrates
0.12
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, 50°C, purified recombinant His-tagged enzyme, 4-nitrophenyl (16-methyl sulfoyl ester) hexadecanoate
0.25
4 h cultures against 4-nitrophenyl palmitate
0.395
pH 8.0, 50°C, purified recombinant His-tagged enzyme, 4-nitrophenyl (16-methyl sulfone ester) hexadecanoate
0.4
4-nitrophenyl valerate, esterase activity of the recombinant THCUT1 protein against different chromogenic substrates
0.74
4-nitrophenyl butyrate, esterase activity of the recombinant THCUT1 protein against different chromogenic substrates
0.85
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
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
supernatant from 8 h culture on 0.2% cutin monomer 16-hydroxy-hexadecanoic acid shows slightly higher values against 4-nitrophenyl palmitate
1.3
supernatant from 8 h culture on 0.05% cutin monomer 16-hydroxy-hexadecanoic acid shows slightly higher values against 4-nitrophenyl palmitate
1.8
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
10
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
1057
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
11.4
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
114
-
purified recombinant enzyme, pH 8.0, 25°C
1148
pH 8.0, 50°C, substrate 4-nitrophenyl butanoate
1286
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
129
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
14.5
wild-type, presence of 300 mM Ca2+, pH 7.0, 37°C
145
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
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
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, 30°C
188
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
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
2.77
carrier bound CUTAB1 with tributyrin as substrate, in 40 ml of 50 mM potassium phosphate buffer, pH 5.5 containing 25% ethanol, at 8°C, for 40 H
2.84
4-nitrophenyl acetate, esterase activity of the recombinant THCUT1 protein against different chromogenic substrates
200
-
cutinase-tryptophan,proline2, after 72 h of Saccharomyces cerevisae cultivation
2019
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
257
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
277
mutant A68V/T253P, pH 7, 37°C
281
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
3.88
wild-type, pH 7, 37°C
30
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
3302
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
350
-
wild type, after 72 h of Saccharomyces cerevisae cultivation
4.2
4 h cultures against 4-nitrophenyl butyrate (6.6 and 4.2 micromol/min/mg)
40
-
cutinase-tryptophan,proline4, after 72 h of Saccharomyces cerevisae cultivation
41
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
4394
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
446.2
-
purified recombinant alpha-hemolysin-enzyme, substrate 4-nitrophenyl butyrate, pH 8.0, 50°C
454
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
47
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
5.4
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
5359
-
substrate 4-nitrophenyl butyrate, recombinant enzyme, pH 8.0, 37°C
542.5
pH 8.0, 50°C, purified recombinant His-tagged enzyme, substrate 4-nitrophenyl butyrate
586
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
6.6
4 h cultures against 4-nitrophenyl butyrate (6.6 and 4.2 micromol/min/mg)
643.4
pH 8.0, 50°C, purified recombinant His-tagged enzyme, substrate 4-nitrophenyl butyrate
66
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
7.5
supernatant from 8 h culture on 0.2% cutin monomer 16-hydroxy-hexadecanoic acid shows higher activity values against 4-nitrophenyl butyrate
77
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
833
mutant A68V/T253P, presence of 300 mM Ca2+, pH 7.0, 37°C
9.8
supernatant from 8 h culture on 0.05% cutin monomer 16-hydroxy-hexadecanoic acid shows higher activity values against 4-nitrophenyl butyrate
948
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
983
-
substrate 4-nitrophenyl butanoate, pH 4.0, 50°C
125
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
125
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
17
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
17
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
additional information
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additional information
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additional information
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additional information
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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.
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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
-
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
-
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
-
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
-
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
-
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
Helminthosporium sativum
-
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
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
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
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
-
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
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. 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
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
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
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
-
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
-
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
-
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
-
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
-
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
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malfunction
-
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
-
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
-
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
-
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
-
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
-
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems
malfunction
Helminthosporium sativum
-
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
-
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
-
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
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
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
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
physiological function
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
-
cutinases are hydrolytic enzymes that share properties of lipases and esterases, they are 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
-
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
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
-
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
-
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
-
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
Helminthosporium sativum
-
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
-
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
-
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
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
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
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
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
physiological function
Aspergillus oryzae hydrophobin RolA adheres to the substrate polybutylene succinate co-adipate and promotes degradation by interacting with polyesterase CutL1 and recruiting it to the substrate surface. Residue D30 of CutL is involved in the CutL1-RolA interaction
physiological function
expression of cutinase fused to pelB signal peptide in a secB knockout strain, defective in type II secretion pathway, still leads to accumulation of cutinase in the culture medium. The phospholipid hydrolase activity of pelB-cutinase plays a role in its extracellular production
physiological function
in a liquid medium containing the polybutylene succinate co-adipate, Aspergillus oryzae produces RolA, a hydrophobin, and cutinase CutL1, which degrades polybutylene succinate co-adipate. Secreted RolA attaches to the surface of the polybutylene succinate co-adipate particles and recruits CutL1. Residues Asp142, Asp171 and Glu31, located on the hydrophilic molecular surface of CutL1, and His32 and Lys34, located in the N-terminus of RolA, play crucial roles in the RolA-CutL1 interaction via ionic interactions
physiological function
-
isoform CUT11 protein induces cell death and triggers defense responses in Nicotiana benthamiana, cotton, and tomato plants. CUT11 induces plant defense responses in Nicotiana benthamania in a BAK1 and SOBIR-dependent manner. The carbohydrate-binding module family 1 protein suppresses CUT11-induced cell death and other defense responses in Nicothiana benthamiana
physiological function
-
isoform CUT11 protein induces cell death and triggers defense responses in Nicotiana benthamiana, cotton, and tomato plants. CUT11 induces plant defense responses in Nicotiana benthamania in a BAK1 and SOBIR-dependent manner. The carbohydrate-binding module family 1 protein suppresses CUT11-induced cell death and other defense responses in Nicothiana benthamiana
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additional information
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biophysical parameters of cutinase as a function of pH, overview
additional information
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biophysical parameters of cutinase as a function of pH, overview
additional information
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biophysical parameters of cutinase as a function of pH, overview
additional information
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biophysical parameters of cutinase as a function of pH, overview
additional information
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biophysical parameters of cutinase as a function of pH, overview
additional information
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enzyme homology modeling
additional information
residues Ser117, Asp169, and His182 form the active site
additional information
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residues Ser117, Asp169, and His182 form the active site
additional information
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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
structure analysis, structure comparisons of isozymes Cut1 and Cut2 during denaturation and unfolding, homology modeling, overview
additional information
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
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the enzyme has a Ser130-His208-Asp176 catalytic triad in which Ser130 is critical to the hydrolytic activity
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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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
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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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
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
Helminthosporium sativum
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
additional information
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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
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
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
-
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
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
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
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
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
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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
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
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
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
additional information
E5BBQ3
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
additional information
E9LVI0
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
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
additional information
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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
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additional information
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the enzyme possesses a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent
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additional information
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enzyme homology modeling
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A84F
mutation in the small helical flap, significantly increases the activity towards longer chain substrates like 4-nitrophenyl palmitate
I183A
mutation in the hydrophobic binding loop, drastically reduces the overall activity
L181A
mutation in the hydrophobic binding loop, drastically reduces the overall activity
L80A
mutation in the hydrophobic binding loop, drastically reduces the overall activity
A102D/Q105R/G106E
pH-optima for activity and stability are identical to wild-type enzym. Improvement in Tm-value of 3.4°C. Increased half-life at 6°C relative to the wild-type enzyme of approximately 3fold
A102D/Q105R/G106E/N133A/S140P/E161T/A166P
large improvement of stability at 60°C
A102D/Q105R/G106E/N133A/S140P/E161T/A166P/K137E
large improvement of stability at 60°C
A102D/Q105R/G106E/Q98N/A99D/E109Q
thermodynamically most stable variant, improving on wild-type enzyme by 6.7 kJ/mol
A178P/V179P
loss of stability and activity
D30S
mutation increases the KD value for interaction with hydrophobin RolA
D30S/E31S/D142S/D171S
mutation D30S increases the KD value for interaction with hydrophobin RolA in comparison with mutant E31S/D142S/D171S
K174R/Y176F/A178E/D200R/G202E/D203E/D206R
mutant enzyme shows an increased kinetic stability
L26D/G28E/D30R/K67R
improvement in Tm-value of 0.7°C
N133A/S140P/E161T/A166P
proline mutations contribute to themostabilization by decreasing the entropy lost upon folding. Improvement in Tm of 1.7°C. Increased half-life at 6°C relative to the wild-type enzyme of approximately 2fold
Q110W/K114W
the mutant enzyme is retained in the endoplasmic reticulum whereas wild-type enzyme is secreted
R46P
the Tm-value is 3°C below that of wild-type enzyme
T84R/D86L/A99E/A100S
decrease in thermostability relative to the wild-type enzyme. Large losses in 4-nitrophenyl butyrate (about 70%) and poly(epsilon-caprolactone) (about 90%) activities
V150I/I136V
mutation do not provide any improvement in stability
A102D/Q105R/G106E
-
pH-optima for activity and stability are identical to wild-type enzym. Improvement in Tm-value of 3.4°C. Increased half-life at 6°C relative to the wild-type enzyme of approximately 3fold
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L26D/G28E/D30R/K67R
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improvement in Tm-value of 0.7°C
-
Q110W/K114W
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the mutant enzyme is retained in the endoplasmic reticulum whereas wild-type enzyme is secreted
-
V150I/I136V
-
mutation do not provide any improvement in stability
-
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 50°C, accompanied by an increase in optimal temperature, as compared with wild-type enzyme, while the activity at 25°C is not compromised
N177D/L172K
site-directed mutagenesis, the double mutant shows enhanced activity towards phenyl ester substrates and enhanced thermal stability
F52W
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
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
F52W
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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
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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
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A164E
-
amino acid substitution, 74% of wild-type activity
A185T
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amino acid substitution, 142% of wild-type activity
A85F/G82A
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optimal activity with triglyceride anolgues shifts towards slightly longer acyl ester chains
D33S
site-directed mutagenesis, the mutant shows 26% reduced activity in olive oil compared to the wild-type enzyme
G26P
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amino acid substitution, 68% of wild-type activity
G41A
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amino acid substitution, 76% of wild-type activity
G82A
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mutation has no influence on enzymatic properties
K140D
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amino acid substitution, 39% of wild-type activity
K151M
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amino acid substitution, 22% of wild-type activity
K65P
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amino acid substitution, 99% of wild-type activity
L114C
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comparative structural analysis of native enzyme and mutant enzymes
L153A
-
amino acid substitution, 111% of wild-type activity
L189A
activity with polyethylene terephthalate fibers is 78% of wild-type enzyme, activity with polyamide 6,6 fiber is 94% of wild-type activity
L81G/L182G
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comparative structural analysis of native enzyme and mutant enzymes
N33S
74% of the activity of the wild-type enzyme
Q121L
-
comparative structural analysis of native enzyme and mutant enzymes
R156N
-
amino acid substitution, 89% of wild-type activity
R158L
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amino acid substitution, 75% of wild-type activity
R17E/N172K
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comparative structural analysis of native enzyme and mutant enzymes
R17S
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amino acid substitution, 69% of wild-type activity
R196A
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amino acid substitution, 75% of wild-type activity
S120C
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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
S57D
-
amino acid substitution, 61% of wild-type activity
S61D
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amino acid substitution, 83% of wild-type activity
S82R
50% of the activity of the wild-type enzyme
S92C
-
comparative structural analysis of native enzyme and mutant enzymes
S92R
site-directed mutagenesis, the mutant shows 50% reduced activity in olive oil compared to the wild-type enzyme
T179E
-
amino acid substitution, 10% of wild-type activity
T179N
-
amino acid substitution, 119% of wild-type activity
T18D
-
amino acid substitution, 65% of wild-type activity
T45D
-
amino acid substitution, 54% of wild-type activity
T80P
-
comparative structural analysis of native enzyme and mutant enzymes
Y119H
-
comparative structural analysis of native enzyme and mutant enzymes
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
I36N/F70S
mutant engineered for cellulose acetate deacetylation, almost 2fold improvement in catalytic efficiency with both cellulose acetate and 4-nitrophenyl butanoate
I36S/F70A
mutant engineered for cellulose acetate deacetylation, 2fold improvement in catalytic efficiency with cellulose acetate and 4-nitrophenyl butanoate
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
H173L
36% of wild-type activity
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
S226P/R228S/S176A
inactive mutant enzyme
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
-
S226P/R228S/S176A
-
inactive mutant enzyme
-
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
site-directed mutagenesis, the mutation causes a 99% reduction in enzyme activity and also completely abolishes the elicitor activity of the protein
Y116A
site-directed mutagenesis, the mutation causes a 97% reduction in enzyme activity and also abolishes the elicitor activity of the protein
A30V
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
L183A
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
Q65E
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
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
site-directed mutagenesis, mutation of isozyme Cut2 to the analogue residue of isozyme Cut1
R19S/R29N/A30V
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
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
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
L183A
-
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
-
Q65E
-
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
-
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
-
site-directed mutagenesis, mutation of isozyme Cut2 to the analogue residue of isozyme Cut1
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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
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
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
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
-
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
-
C275A/C292A
-
site-directed mutagenesis, the mutant lacks the disulfide bond formed by Cys275 and Cys292, resulting in increased instability
H204N
site-directed mutant, constructed, overexpressed, and purified
H204N
is catalytically inactive. Is not covalently modified by a 4fold excess of diethyl p-nitrophenyl phosphate, in contrast to the wild-type
A164R
41% of the activity of the wild-type enzyme
A164R
site-directed mutagenesis, the mutant shows 59% reduced activity in olive oil compared to the wild-type enzyme
A185L
96% of the activity of the wild-type enzyme
A185L
site-directed mutagenesis, the mutant shows unaltered activity in olive oil compared to the wild-type enzyme
A195S
38% of the activity of the wild-type enzyme
A195S
site-directed mutagenesis, the mutant shows 62% reduced activity in olive oil compared to the wild-type enzyme
A199C
no activity
A199C
-
comparative structural analysis of native enzyme and mutant enzymes
A199C
site-directed mutagenesis, the mutant shows no activity in olive oil
A29S
-
64% of the activity of the wild-type enzyme
A29S
site-directed mutagenesis, the mutant shows 36% reduced activity in olive oil compared to the wild-type enzyme
A79G
50% of the activity of the wild-type enzyme
A79G
site-directed mutagenesis, the mutant shows 50% reduced activity in olive oil compared to the wild-type enzyme
A85F
-
crystallizes in a form different from the native enzyme
A85F
136% of the activity of the wild-type enzyme
A85F
-
optimal activity with triglyceride anolgues shifts towards slightly longer acyl ester chains
A85F
site-directed mutagenesis, the mutant shows 36% increased activity in olive oil compared to the wild-type enzyme
A85F
the mutant shows higher enzyme activity with hydrophobic, low-molecular-weight substrates in olive oil emulsions than the wild-type enzyme
A85W
-
optimal activity with triglyceride anolgues shifts towards slightly longer acyl ester chains
A85W
5% of the activity of the wild-type enzyme
A85W
site-directed mutagenesis, the mutant shows 9% increased activity in olive oil compared to the wild-type enzyme
A85W
the mutant shows higher enzyme activity with hydrophobic, low-molecular-weight substrates in olive oil emulsions than the wild-type enzyme
D111N
39% of the activity of the wild-type enzyme
D111N
site-directed mutagenesis, the mutant shows 61% reduced activity in olive oil compared to the wild-type enzyme
D134S
37% of the activity of the wild-type enzyme
D134S
site-directed mutagenesis, the mutant shows 63% reduced activity in olive oil compared to the wild-type enzyme
D83S
62% of the activity of the wild-type enzyme
D83S
site-directed mutagenesis, the mutant shows 38% reduced activity in olive oil compared to the wild-type enzyme
E201K
54% of the activity of the wild-type enzyme
E201K
site-directed mutagenesis, the mutant shows 46% reduced activity in olive oil compared to the wild-type enzyme
G192Q
44% of the activity of the wild-type enzyme
G192Q
site-directed mutagenesis, the mutant shows 56% reduced activity in olive oil compared to the wild-type enzyme
G26A
32% of the activity of the wild-type enzyme
G26A
site-directed mutagenesis, the mutant shows 67% reduced activity in olive oil compared to the wild-type enzyme
I183F
25% of the activity of the wild-type enzyme
I183F
site-directed mutagenesis, the mutant shows 75% reduced activity in olive oil compared to the wild-type enzyme
I204K
66% of the activity of the wild-type enzyme
I204K
site-directed mutagenesis, the mutant shows 34% reduced activity in olive oil compared to the wild-type enzyme
I24S
4% of the activity of the wild-type enzyme
I24S
site-directed mutagenesis, the mutant shows 96% reduced activity in olive oil compared to the wild-type enzyme
K151R
29% of the activity of the wild-type enzyme
K151R
site-directed mutagenesis, the mutant shows 71% reduced activity in olive oil compared to the wild-type enzyme
K168L
83% of the activity of the wild-type enzyme
K168L
site-directed mutagenesis, the mutant shows 17% reduced activity in olive oil compared to the wild-type enzyme
L114Y
20% of the activity of the wild-type enzyme
L114Y
site-directed mutagenesis, the mutant shows 80% reduced activity in olive oil compared to the wild-type enzyme
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
L182A
site-directed mutagenesis, the mutant shows activity enhancement of 5fold toward high-molecular weight PET fibers compared to the wild-type enzyme
L182W
19% of the activity of the wild-type enzyme
L182W
site-directed mutagenesis, the mutant shows 81% reduced activity in olive oil compared to the wild-type enzyme
L189F
-
comparative structural analysis of native enzyme and mutant enzymes
L189F
109% of the activity of the wild-type enzyme
L189F
site-directed mutagenesis, the mutant shows 9% increased activity in olive oil compared to the wild-type enzyme
L189F
the mutant shows higher enzyme activity with hydrophobic, low-molecular-weight substrates in olive oil emulsions than 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
L81A
the mutant shows activity enhancement of 4fold toward high-molecular weight PET fibers compared to the wild-type enzyme
L99K
78% of the activity of the wild-type enzyme
L99K
site-directed mutagenesis, the mutant shows 22% reduced activity in olive oil compared to the wild-type enzyme
M98C
35% of the activity of the wild-type enzyme
M98C
site-directed mutagenesis, the mutant shows 65% reduced activity in olive oil compared to the wild-type enzyme
N161D
63% of the activity of the wild-type enzyme
N161D
site-directed mutagenesis, the mutant shows 37% reduced activity in olive oil compared to the wild-type enzyme
N172K
-
comparative structural analysis of native enzyme and mutant enzymes
N172K
45% of the activity of the wild-type enzyme
N172K
site-directed mutagenesis, the mutant shows 55% reduced activity in olive oil compared to the wild-type enzyme
N172K/R196E
-
comparative structural analysis of native enzyme and mutant enzymes
N172K/R196E
-
crystallizes in a form different from the native enzyme
N84A
-
comparative structural analysis of native enzyme and mutant enzymes
N84A
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
N84A
site-directed mutagenesis, the mutant shows 73.5% reduced activity in olive oil compared to the wild-type enzyme
N84A
the mutant shows activity enhancement of 1.7fold toward high-molecular weight PET fibers compared to the wild-type enzyme
N84D
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
N84D
site-directed mutagenesis, the mutant shows almost no activity in olive oil
N84L
-
comparative structural analysis of native enzyme and mutant enzymes
N84L
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
N84L
site-directed mutagenesis, the mutant shows 97% reduced activity in olive oil compared to the wild-type enzyme
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
N84W
site-directed mutagenesis, the mutant shows almost no activity in olive oil
R156E
79% of the activity of the wild-type enzyme
R156E
site-directed mutagenesis, the mutant shows 21% reduced activity in olive oil compared to the wild-type enzyme
R156K
115% of the activity of the wild-type enzyme
R156K
-
amino acid substitution, 151% of wild-type activity
R156K
site-directed mutagenesis, the mutant shows 15% increased activity in olive oil compared to the wild-type enzyme
R156L
-
comparative structural analysis of native enzyme and mutant enzymes
R156L
71% of the activity of the wild-type enzyme
R156L
site-directed mutagenesis, the mutant shows 29% reduced activity in olive oil compared to the wild-type enzyme
R17E
34% of the activity of the wild-type enzyme
R17E
site-directed mutagenesis, the mutant shows 66% reduced activity in olive oil compared to the wild-type enzyme
R17N
31% of the activity of the wild-type enzyme
R17N
site-directed mutagenesis, the mutant shows 69% reduced activity in olive oil compared to the wild-type enzyme
R196E
-
crystallizes in a form different from the native enzyme
R196E
45% of the activity of the wild-type enzyme
R196E
-
amino acid substitution, 21% of wild-type activity
R196E
site-directed mutagenesis, the mutant shows 55% reduced activity in olive oil compared to the wild-type enzyme
R196K
38% of the activity of the wild-type enzyme
R196K
site-directed mutagenesis, the mutant shows 62% reduced activity in olive oil compared to the wild-type enzyme
R196L
44% of the activity of the wild-type enzyme
R196L
site-directed mutagenesis, the mutant shows 56% reduced activity in olive oil compared to the wild-type enzyme
R208A
64% of the activity of the wild-type enzyme
R208A
site-directed mutagenesis, the mutant shows 36% reduced activity in olive oil compared to the wild-type enzyme
R78L
49% of the activity of the wild-type enzyme
R78L
site-directed mutagenesis, the mutant shows 51% reduced activity in olive oil compared to the wild-type enzyme
R78N
34% of the activity of the wild-type enzyme
R78N
site-directed mutagenesis, the mutant shows 66% reduced activity in olive oil compared to the wild-type enzyme
R88A
39% of the activity of the wild-type enzyme
R88A
site-directed mutagenesis, the mutant shows 61% reduced activity in olive oil compared to the wild-type enzyme
R96N
57% of the activity of the wild-type enzyme
R96N
site-directed mutagenesis, the mutant shows 43% reduced activity in olive oil compared to the wild-type enzyme
S120A
no activity
S120A
the mutant enzyme casries a 15 amino acid pro-peptide. The pro-peptide is affected by the presence of the micellar substrate
S120A
site-directed mutagenesis, the mutant shows no activity in olive oil
S42A
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
S42A
site-directed mutagenesis, the mutant shows almost no activity in olive oil
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
34% of the activity of the wild-type enzyme
S54E
-
amino acid substitution, 83% of wild-type activity
S54E
site-directed mutagenesis, the mutant shows 66% reduced activity in olive oil compared to the wild-type enzyme
S54K
96% of the activity of the wild-type enzyme
S54K
site-directed mutagenesis, the mutant shows unaltered activity in olive oil compared to the wild-type enzyme
S54W
-
mutation has no influence on enzymatic
S54W
89% of the activity of the wild-type enzyme
S54W
site-directed mutagenesis, the mutant shows 11% reduced activity in olive oil compared to the wild-type enzyme
T144C
-
comparative structural analysis of native enzyme and mutant enzymes
T144C
54% of the activity of the wild-type enzyme
T144C
site-directed mutagenesis, the mutant shows 46% reduced activity in olive oil compared to the wild-type enzyme
T167L
54% of the activity of the wild-type enzyme
T167L
site-directed mutagenesis, the mutant shows 46% reduced activity in olive oil compared to the wild-type enzyme
T173K
119% of the activity of the wild-type enzyme
T173K
site-directed mutagenesis, the mutant shows 19% increased activity in olive oil compared to the wild-type enzyme
T173K
the mutant shows higher enzyme activity with hydrophobic, low-molecular-weight substrates in olive oil emulsions than 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
T179Y
131% of the activity of the wild-type enzyme
T179Y
site-directed mutagenesis, the mutant shows 31% increased activity in olive oil compared to the wild-type enzyme
T179Y
the mutant shows higher enzyme activity with hydrophobic, low-molecular-weight substrates in olive oil emulsions than the wild-type enzyme
T18V
90% of the activity of the wild-type enzyme
T18V
site-directed mutagenesis, the mutant shows 10% reduced activity in olive oil compared to the wild-type enzyme
T19V
35% of the activity of the wild-type enzyme
T19V
site-directed mutagenesis, the mutant shows 65% reduced activity in olive oil compared to the wild-type enzyme
T45A
-
comparative structural analysis of native enzyme and mutant enzymes
T45A
98% of the activity of the wild-type enzyme
T45A
site-directed mutagenesis, the mutant shows unaltered activity in olive oil compared to the wild-type enzyme
T45K
74% of the activity of the wild-type enzyme
T45K
site-directed mutagenesis, the mutant shows 26% reduced activity in olive oil compared to the wild-type enzyme
T50V
25% of the activity of the wild-type enzyme
T50V
site-directed mutagenesis, the mutant shows 75% reduced activity in olive oil compared to the wild-type enzyme
T80D
32% of the activity of the wild-type enzyme
T80D
site-directed mutagenesis, the mutant shows 68% reduced activity in olive oil compared to the wild-type enzyme
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
V184A
the mutant shows activity enhancement of 2fold toward high-molecular weight PET fibers compared to the wild-type enzyme
W69Y
12% of the activity of the wild-type enzyme
W69Y
site-directed mutagenesis, the mutant shows 88% reduced activity in olive oil compared to the wild-type enzyme
Y38F
-
comparative structural analysis of native enzyme and mutant enzymes
Y38F
62% of the activity of the wild-type enzyme
Y38F
site-directed mutagenesis, the mutant shows 38% reduced activity in olive oil compared to the wild-type enzyme
S103A
231% of wild-type activity
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
38% of wild-type activity
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
A68V/T253P
increase in both activity and thermostabililty, stable for 1 h below 60°C. Mutant is able to degrade various aliphatic and aliphatic coaromatic polyesters and hydrophilizes an amorphous PET film
A68V/T253P
-
increase in both activity and thermostabililty, stable for 1 h below 60°C. Mutant is able to degrade various aliphatic and aliphatic coaromatic polyesters and hydrophilizes an amorphous PET film
-
S130A
catalytically inactive
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
additional information
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
-
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
additional information
mutational analysis toward the thermostabilization of the enzyme. Mutants with increased thermal unfolding temperature and increase in the half-life of the enzyme activity at 60°C do not display improved rate or temperature optimum of enzyme activity. Surface salt bridge optimization produces enthalpic stabilization. Mutations to proline reduces the entropy loss upon folding. The lack of a correlative increase in the temperature optimum of catalytic activity with thermodynamic stability suggests that the active site is locally denatured at a temperature below the thermal unfolding temperature of the global structure
additional information
-
mutational analysis toward the thermostabilization of the enzyme. Mutants with increased thermal unfolding temperature and increase in the half-life of the enzyme activity at 60°C do not display improved rate or temperature optimum of enzyme activity. Surface salt bridge optimization produces enthalpic stabilization. Mutations to proline reduces the entropy loss upon folding. The lack of a correlative increase in the temperature optimum of catalytic activity with thermodynamic stability suggests that the active site is locally denatured at a temperature below the thermal unfolding temperature of the global structure
additional information
-
mutational analysis toward the thermostabilization of the enzyme. Mutants with increased thermal unfolding temperature and increase in the half-life of the enzyme activity at 60°C do not display improved rate or temperature optimum of enzyme activity. Surface salt bridge optimization produces enthalpic stabilization. Mutations to proline reduces the entropy loss upon folding. The lack of a correlative increase in the temperature optimum of catalytic activity with thermodynamic stability suggests that the active site is locally denatured at a temperature below the thermal unfolding temperature of the global structure
-
additional information
the insertion mutant 49aILe shows 52% of the activity of the wild-type enzyme
additional information
-
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
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
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
additional information
generation of codon-optimized enzyme for expression in Pichia pastoris
additional information
-
generation of codon-optimized enzyme for expression in Pichia pastoris
additional information
-
generation of codon-optimized enzyme for expression in Pichia pastoris
-
additional information
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
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
-
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
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
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
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
additional information
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
additional information
fusion of enzyme to the class II hydrophobins HFB4 and HFB7 or the pseudo-class I hydrophobin HFB9b. The fusion enzymes exhibit decreased kcat values on soluble substrates and strongly decreased the hydrophilicity of glass but cause only small changes in the hydrophobicity of polyethylene terephthalate. Upon fusion to HFB4 or HFB7, the hydrolysis of polyethylene terephthalate is enhanced over16fold over the level with the free enzyme. Fusion with the non-class II hydrophobin HFB9b does not increase the rate of hydrolysis over that of the enzyme-hydrophobin mixture, but HFB9b performs best when polyethylene terephthalate is preincubated with the hydrophobins before enzyme treatment. The pattern of hydrolysis by the fusion shows an increase in the concentration of the product mono(2-hydroxyethyl) terephthalate relative to that of the main product, terephthalic acid
additional information
-
fusion of enzyme to the class II hydrophobins HFB4 and HFB7 or the pseudo-class I hydrophobin HFB9b. The fusion enzymes exhibit decreased kcat values on soluble substrates and strongly decreased the hydrophilicity of glass but cause only small changes in the hydrophobicity of polyethylene terephthalate. Upon fusion to HFB4 or HFB7, the hydrolysis of polyethylene terephthalate is enhanced over16fold over the level with the free enzyme. Fusion with the non-class II hydrophobin HFB9b does not increase the rate of hydrolysis over that of the enzyme-hydrophobin mixture, but HFB9b performs best when polyethylene terephthalate is preincubated with the hydrophobins before enzyme treatment. The pattern of hydrolysis by the fusion shows an increase in the concentration of the product mono(2-hydroxyethyl) terephthalate relative to that of the main product, terephthalic acid
additional information
-
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
-
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
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
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