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
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lipolytic
- thermobifida
- esterases
- insolens
- fusca
-
humicola
-
ideonella
-
polybutylene
- sakaiensis
- industry
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polycaprolactone
- tributyrin
- degradation
- sulfosuccinate
- haematococca
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monilinia
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terephthalic
- petase
- synthesis
- nectria
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hydrophobins
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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
3.1.1.74 cutinaseAdvanced search results
results (
results (KM Value
KM Value on EC 3.1.1.74 - cutinase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
7.24
4-nitrophenyl caprylate
-
pH 8.0, 25°C, recombinant enzyme
7.25
4-nitrophenyl myristate
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pH 8.0, 25°C, recombinant enzyme
0.00067
4-nitrophenyl acetate
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in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol
0.00496
4-nitrophenyl acetate
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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
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
1.5
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
0.72
4-nitrophenyl butanoate
Bacillus sp. KY0701
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pH not specified in the publication, temperature not specified in the publication
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
1.3
4-nitrophenyl butanoate
fusion protein Cut1-HFB4, pH 7.0, 25°C
0.00021
4-nitrophenyl butyrate
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in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol
0.00126
4-nitrophenyl butyrate
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in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol
0.18
4-nitrophenyl butyrate
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pH 8.0, 50°C, recombinant mutant C275A/C292A, absence of 1% PEG
0.19
4-nitrophenyl butyrate
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pH 8.0, 70°C, recombinant mutant C275A/C292A, absence of 1% PEG
0.21
4-nitrophenyl butyrate
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pH 8.0, 50°C, recombinant wild-type enzyme, absence of 1% PEG
0.22
4-nitrophenyl butyrate
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pH 8.0, 30°C, recombinant wild-type enzyme, absence of 1% PEG
0.24
4-nitrophenyl butyrate
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pH 8.0, 70°C, recombinant wild-type enzyme, absence of 1% PEG
0.25
4-nitrophenyl butyrate
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pH 8.0, 30°C, recombinant mutant C275A/C292A, absence of 1% PEG
0.25
4-nitrophenyl butyrate
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pH 8.0, 70°C, recombinant wild-type enzyme, absence of 1% PEG
0.27
4-nitrophenyl butyrate
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pH 8.0, 30°C, recombinant wild-type enzyme, presence of 1% PEG
0.27
4-nitrophenyl butyrate
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pH 8.0, 50°C, recombinant wild-type enzyme, presence of 1% PEG
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
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
59.2
4-nitrophenyl butyrate
pH and temperature not specified in the publication
0.00029
4-nitrophenyl hexanoate
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in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol
0.0015
4-nitrophenyl hexanoate
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in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol
0.00004
4-nitrophenyl valerate
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in 14.5 mM Tris-HCl buffer, pH 7.5, 0.75% glycerol
0.00148
4-nitrophenyl valerate
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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
0.2
p-nitrophenyl butyrate
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T179C mutant, sodium dioctyl sulfosuccinate concentration = 0 mM
0.31
p-nitrophenyl butyrate
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L153Q mutant, sodium dioctyl sulfosuccinate concentration = 0 mM
0.33
p-nitrophenyl butyrate
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S54D mutant, sodium dioctyl sulfosuccinate concentration = 0 mM
0.35
p-nitrophenyl butyrate
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wild type, sodium dioctyl sulfosuccinate concentration = 0 mM
0.48
p-nitrophenyl butyrate
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wild type, sodium dioctyl sulfosuccinate concentration = 0.5 mM
0.49
p-nitrophenyl butyrate
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T179Cmutant, sodium dioctyl sulfosuccinate concentration = 0.5 mM
0.66
p-nitrophenyl butyrate
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T179C mutant, sodium dioctyl sulfosuccinate concentration = 1 mM
0.69
p-nitrophenyl butyrate
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L153Q mutant, sodium dioctyl sulfosuccinate concentration = 0.5 mM
0.72
p-nitrophenyl butyrate
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S54D mutant, sodium dioctyl sulfosuccinate concentration = 1 mM
0.74
p-nitrophenyl butyrate
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S54D mutant, sodium dioctyl sulfosuccinate concentration = 0.5 mM
0.85
p-nitrophenyl butyrate
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wild type, sodium dioctyl sulfosuccinate concentration = 1 mM
1.08
p-nitrophenyl butyrate
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wild type, sodium dioctyl sulfosuccinate concentration = 2 mM
1.09
p-nitrophenyl butyrate
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T179C mutant, sodium dioctyl sulfosuccinate concentration = 1.5 mM
1.12
p-nitrophenyl butyrate
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wild type, sodium dioctyl sulfosuccinate concentration = 1.5 mM
1.14
p-nitrophenyl butyrate
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S54D mutant, sodium dioctyl sulfosuccinate concentration = 1.5 mM
1.31
p-nitrophenyl butyrate
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L153Q mutant, sodium dioctyl sulfosuccinate concentration = 1 mM
1.56
p-nitrophenyl butyrate
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T179C mutant, sodium dioctyl sulfosuccinate concentration = 2 mM
1.74
p-nitrophenyl butyrate
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S54D mutant, sodium dioctyl sulfosuccinate concentration = 2 mM
3.57
p-nitrophenyl butyrate
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L153Q mutant, sodium dioctyl sulfosuccinate concentration = 1.5 mM
4.33
p-nitrophenyl butyrate
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L153Q mutant, sodium dioctyl sulfosuccinate concentration = 2 mM
additional information
additional information
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Km-values in presence of surfactants
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
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steady-state kinetic analysis
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additional information
additional information
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comparison of kinetics of cutinases from different organisms, overview
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additional information
additional information
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comparison of kinetics of cutinases from different organisms, overview
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additional information
additional information
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comparison of kinetics of cutinases from different organisms, overview
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additional information
additional information
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comparison of kinetics of cutinases from different organisms, overview
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additional information
additional information
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comparison of kinetics of cutinases from different organisms, overview
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additional information
additional information
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kinetic model of transesterification of triolein and methanol, overview
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additional information
additional information
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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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