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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Activating Compound
Activating Compound on EC 3.1.1.74 - cutinase
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16-hydroxyhexadecanoic acid
is strongly induced in vitro by cutin monomer 16-hydroxyhexadecanoic acid
N,N-diethyl-2-phenylacetamide
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increases hydrolysis rates of semi-crystalline poly(ethylene terephthalate) films and fabrics for cutinase. The outer layers of the polymer will be better exposed to the enzyme in the presence of N,N-diethyl-2-phenylacetamide. Overall enhancement in colour depth of 300%
olive oil
Thcut1 mRNA is strongly induced in vitro by olive oil
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sodium 2-{[(3alpha,5beta,12alpha)-3,12-dihydroxy-24-oxocholan-24-yl]amino}ethane-1-sulfonate
sodium dioctyl sulfosuccinate
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in the absence of surfactant the S54D variant catalytic activity is similar to that of the wild type cutinase, whereas L153Q and T179C variants show a lower activity
activates 10% at 10 mM
sodium 2-{[(3alpha,5beta,12alpha)-3,12-dihydroxy-24-oxocholan-24-yl]amino}ethane-1-sulfonate
activates 24% at 10 mM
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pseudo-activation in presence of sodium bis(2-ethylhexyl)ester sulfosuccinic acid and hexadecyltrimethyl-ammoniumbromide
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additional information
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no activation in the presence of Triton X-100 due to the absence of a lid covering the active site pocket
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additional information
Pichia pastoris expressing the native non-tagged cutinase exhibits about 2- and 3fold higher values of protein amount and cutinase activity in the culture supernatant, respectively, than those containing the C-terminal tagged cutinase
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additional information
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Pichia pastoris expressing the native non-tagged cutinase exhibits about 2- and 3fold higher values of protein amount and cutinase activity in the culture supernatant, respectively, than those containing the C-terminal tagged cutinase
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additional information
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water:surfactant molar rate has a marked influence on the enzyme activity, with the best results in the range between 5 and 8. The use of detergents improves the reaction yield during wetting of cotton fibers. Increase in the stereoselectivity of the primary hydroxyl group acylation is obtained through the preincubation of the enzyme in the presence of the substrate diol 1, there is no correlation with the incubation time
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additional information
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no activation in the presence of Triton X-100 due to the absence of a lid covering the active site pocket
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