3.1.1.74: cutinase
This is an abbreviated version!
For detailed information about cutinase, go to the full flat file.
Word Map on EC 3.1.1.74
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3.1.1.74
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fusarium
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solani
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pi
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lipase
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terephthalate
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p-nitrophenyl
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lipolytic
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thermobifida
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esterases
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insolens
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fusca
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humicola
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ideonella
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polybutylene
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sakaiensis
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industry
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polycaprolactone
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tributyrin
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degradation
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sulfosuccinate
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haematococca
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monilinia
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terephthalic
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petase
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synthesis
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nectria
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hydrophobins
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saccharomonospora
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biotechnology
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environmental protection
- 3.1.1.74
- fusarium
- solani
- pi
- lipase
- terephthalate
- p-nitrophenyl
-
lipolytic
- thermobifida
- esterases
- insolens
- fusca
-
humicola
-
ideonella
-
polybutylene
- sakaiensis
- industry
-
polycaprolactone
- tributyrin
- degradation
- sulfosuccinate
- haematococca
-
monilinia
-
terephthalic
- petase
- synthesis
- nectria
-
hydrophobins
-
saccharomonospora
- biotechnology
- environmental protection
Reaction
Synonyms
acidic cutinase, CcCUT1, CDEF1, CLE, Cut 5a, cut-2.KW3, Cut1, Cut11, Cut190, Cut2, Cut5a, CUTAB1, CutB, cuticle destructing factor 1, cutin esterase, cutin hydrolase, cutinase, cutinase 1, cutinase 2, cutinase-1, cutinase-like enzyme, cutinolytic polyesterase, CutL, CutL1, FspC, fungal cutinase, HIc, LC-cutinase, More, MYCTH_2110987, PET hydrolase, Tfu_0883, Thcut1, THCUT1 protein, Thc_Cut1, Thc_Cut2, TRIREDRAFT_60489
ECTree
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Inhibitors
Inhibitors on EC 3.1.1.74 - cutinase
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(O,O)-diethyl-(3,5,6-trichloro)-2-pyridylphosphorothioate
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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
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i.e. MAT 9564
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
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
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upon chloroperoxidase oxidation, chlorpyrifos-methyl shows a very strong cutinase inhibition as compared to the corresponding oxon standard
deoxycholate
24% inhibition at 10 mM; 25% inhibition at 10 mM
diethyldicarbonate
54% inhibition at 1 mM; 56% inhibition at 1 mM
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
ethylene glycol
cleavage product accumulation decreases the activity of cutinase during PET hydrolysis
hexyl acetate
63% inhibition at 40% v/v; 83% inhibition at 40% v/v
oxidized malathion
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oxidized malathion, contrarily to malaoxon, reveals cutinase inhibition
sodium bis(2-ethylhexyl)ester sulfosuccinic acid
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pseudo-competitive inhibitor
Sodium dodecyl sulfate
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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
Dichloromethane
61% inhibition at 40% v/v; 74% inhibition at 40% v/v
glycerol
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inhibits the transesterification activity of the cutinase after 10 min of incubation
guanidine hydrochloride
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GdnHCl-induced unfolding of LC-cutinase is analyzed at pH 8.0 by circular dichroism spectroscopy, overview
not inhibitory: dithiothreitol, EDTA, urea
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additional information
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no inhibition by EDTA, Triton X-100 and Tween 80, or by 75% v/v chloroform, isooctane, isoamyl alcohol, or butanol
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additional information
crystallization and preliminary X-ray analysis of cutinase-inhibitor complexes
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additional information
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crystallization and preliminary X-ray analysis of cutinase-inhibitor complexes
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additional information
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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
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additional information
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inhibition by organophosphate pesticides. Carbamate pesticides reveal an efficient cutinase inhibitor effect, though less potent than the organophosphates
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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
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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
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additional information
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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
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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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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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