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
-
solani
-
pi
-
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
-
nectria
-
hydrophobins
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saccharomonospora
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biotechnology
-
environmental protection
- 3.1.1.74
- fusarium
- solani
- pi
- lipase
- terephthalate
- p-nitrophenyl
-
lipolytic
- thermobifida
- esterases
- insolens
- fusca
-
humicola
-
ideonella
-
polybutylene
- sakaiensis
- industry
-
polycaprolactone
- tributyrin
- degradation
- sulfosuccinate
- haematococca
-
monilinia
-
terephthalic
- petase
- synthesis
- nectria
-
hydrophobins
-
saccharomonospora
- biotechnology
- environmental protection
Reaction
Synonyms
acidic cutinase, CcCUT1, CDEF1, CLE, Cut 5a, cut-2.KW3, Cut1, Cut11, Cut190, Cut2, Cut5a, CUTAB1, CutB, cuticle destructing factor 1, cutin esterase, cutin hydrolase, cutinase, cutinase 1, cutinase 2, cutinase-1, cutinase-like enzyme, cutinolytic polyesterase, CutL, CutL1, FspC, fungal cutinase, HIc, LC-cutinase, More, MYCTH_2110987, PET hydrolase, Tfu_0883, Thcut1, THCUT1 protein, Thc_Cut1, Thc_Cut2, TRIREDRAFT_60489
ECTree
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pH Optimum
pH Optimum on EC 3.1.1.74 - cutinase
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10
7.3
the enzyme exhibits two local pH optima, one at pH 4.0 and the other one at pH 7.3
7.5 - 8
8.5
4
the enzyme exhibits two local pH optima, one at pH 4.0 and the other one at pH 7.3
5
-
substrate poly(caprolactone) , recombinant glycosylated enzyme
and a second optimum at 8.0, but retains activity over a wide pH range
8
and a second optimum at 7.0, but retains activity over a wide pH range
8.5
-
study of thermal unfolding of enzyme as a function of pH-value in different buffers. At pH-optimum of 8.5, enzyme also has high thermal stability