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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Metals Ions
Metals Ions on EC 3.1.1.74 - cutinase
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Ca2+
Co2+
Mg2+
Mn2+
Na+
NaCl
additional information
Ca2+
the binding of Ca2+ induces large conformational changes in three loops, accompanied by the formation of additional interactions. The binding of Ca2+ stabilizes a region that is flexible in the Ca2+-free state but also modifies the substrate-binding groove by stabilizing an open conformation that allows the substrate to bind easily
Ca2+
three calcium ions bind to S226P/R228S/S176A. Ca2+ binding induces the pocket to open, enabling the substrate to access the pocket more easily. Molecular dynamics simulations suggest that a postreaction state in the engaged form presumably exists between the experimentally observed forms, indicating that the substrate would be cleaved in the engaged form and then requires the enzyme to change to the open form to release the product, a process that Ca2+ can greatly accelerate
Ca2+
300 mM, about 4fold increase in specific activity. Presence of Ca2+ does not affect the secondary structure of Est1
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Ni2+ and Mn2+ do not affect enzyme activity at 1 mM
additional information
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the enzyme activity is poorly or not affected by 1 mM Li+, K+, Co2+, and Zn2+
additional information
incubating the enzyme with 5 mM CaCl2, CoCl2, CuSO4, EDTA, FeCl2, MgCl2, MnCl2, Ni(NO3)2, ZnCl2, or 10 mM dithiothreitol has no significant effect on the 4-nitrophenyl butyrate hydrolysis activity
additional information
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incubating the enzyme with 5 mM CaCl2, CoCl2, CuSO4, EDTA, FeCl2, MgCl2, MnCl2, Ni(NO3)2, ZnCl2, or 10 mM dithiothreitol has no significant effect on the 4-nitrophenyl butyrate hydrolysis activity
additional information
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Ba2+ and EDTA have no effect on enzyme activity at 1 mM and 10 mM, respectively
additional information
no effect on enzyme activity by 1 mM CoCl2, KCl, NiCl2, MgSO4, and MnCl2
additional information
no effect on enzyme activity by 1 mM CoCl2, KCl, NiCl2, MgSO4, and MnCl2
additional information
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no effect on enzyme activity by 1 mM CoCl2, KCl, NiCl2, MgSO4, and MnCl2
additional information
no effect on enzyme activity by 1 mM CoCl2, MnCl2, and MgSO4
additional information
no effect on enzyme activity by 1 mM CoCl2, MnCl2, and MgSO4
additional information
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no effect on enzyme activity by 1 mM CoCl2, MnCl2, and MgSO4