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
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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
3.1.1.74 cutinaseAdvanced search results
results (
results (Temperature Stability
Temperature Stability on EC 3.1.1.74 - cutinase
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TEMPERATURE STABILITY 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
22 - 60
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purified recombinant enzyme, stable up to 50°C with over 90% residual activity after 48 h of incubation, while the stability strongly decreases when incubated at 60°C
35
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pH 8, in a water bath with agitation, half-life without additives: 45 days, half-life with 7.5% N,N-dimethylacetamide: 48 days, half-life with 15% N,N-dimethylacetamide: 159 days, half-life with 25% N,N-dimethylacetamide: 4 days, half-life with 50% N,N-dimethylacetamide: 0.4 day, half-life in presence of 25% glycerol: 134 days, half-life with 25% sorbitol: 113 days, half-life with 25% xylitol: 31 days, half-life in presence of 50% ethylene glycol: 29 days, half-life in presence of 50% polyethylene glycol: 23 days
37
38.5
40
40 - 60
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thermostability of Fusarium solani pisi cutinase is evaluated at both 40 and 60°C. It exhibits a similar initial increase at 40°C, but a simple exponential decay at 60°C. 50% of activity retained after 85 h at 40°C or after 5 min at 60°C
42
48
0.08 mM cutinase or 0.005 mM cutinase, pH 8.0, 2 M urea, Tm-value 47.5°C
49
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at pH 4.5, cutinase unfolds with a Tm of 49.3°C. point. The Tm value increases 7.2 ºC in the presence of 1 M of trehalose
49.8
50
52.6
55
56
57
59
60
65
73
melting temperature, mutant S226P, presence of 100 mM Ca2+
75
79
melting temperature, mutants A68V/T253P, A68V/T253P/M259K, presence of Ca2+
80
denaturation of recombinant enzyme by heating the protein sample to 80 °C is to a great extent reversible
additional information
37
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purified recombinant alpha-hemolysin-cutinase retains more than 90% of its maximal activity after incubation at pH 4.0-11.0 for 24 h, which is superior to that of wild-type cutinase
37
purified recombinant enzyme, residual activity is over 75% after 125 h
40
retains 84% of its initial activity at 40°C and pH 8.0 for 5 days
50
purified wild-type enzyme and mutant L172K retain 10% activity after 2 h, mutant N177D retains 30% activity after 2 h with half-life of 30 min
50
enzyme retains 80% of its activity after 20 h incubation at 50°C, but residual activity decreases sharply at 60°C
50
1 h, 70% residual activity, wild-type. In presence of 300 mM Ca2+, no loss of activity for 20 h
55
purified recombinant enzyme, residual activity is over 38% after 125 h
56
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melting temperature. Dramatic loss in activity at 40 °C, 40% drop at 30 °C, continuous decline in activity as a function of increasing temperature
60
t1/2-value: 4.5 h (wild-type enzyme), 40 h (mutant enzymes A102D/Q105R/G106E/N133A/S140P/E161T/A166P and 102D/Q105R/G106E/N133A/S140P/E161T/A166P/K137E), 11.2 h (mutant enzyme A102D/Q105R/G106E/Q98N/A99D/E109Q)
65
t1/2-value: 10 min (wild-type enzyme), 4 h (mutant enzyme A102D/Q105R/G106E/N133A/S140P/E161T/A166P), 5 h (mutant enzyme A102D/Q105R/G106E/N133A/S140P/E161T/A166P/K137E)
75
melting temperature, mutant S226P, presence of 300 mM Ca2+
additional information
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the enzyme is unstable and functions poorly at high temperatures as well as at acidic pH conditions, differential scanning calorimetry thermograms of cutinase, overview
additional information
activity is reduced to less than 10% of the maximum activity by heating for 10 min at 99°C
additional information
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activity is reduced to less than 10% of the maximum activity by heating for 10 min at 99°C
additional information
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the enzyme is unstable and functions poorly at high temperatures as well as at acidic pH conditions, differential scanning calorimetry thermograms of cutinase, overview
additional information
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the enzyme is unstable and functions poorly at high temperatures as well as at acidic pH conditions, differential scanning calorimetry thermograms of cutinase, overview
additional information
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first order rate constants in thermal inactivation, overview
additional information
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-value by up to 7°C
additional information
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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-value by up to 7°C
additional information
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trehalose delays thermal unfolding, thus increasing the temperature at the mid-point of unfolding by 7.2°C
additional information
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presence of hexanol and the low water content lead to the enzyme stabilization in the interior of the micelles, increasing its thermostability
additional information
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the enzyme is unstable and functions poorly at high temperatures as well as at acidic pH conditions, differential scanning calorimetry thermograms of cutinase, overview
additional information
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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
additional information
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thermal stability of Humicola insolens cutinase in aqueous SDS. SDS stabilizes noticeably against irreversible aggregation
additional information
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the enzyme is unstable and functions poorly at high temperatures as well as at acidic pH conditions, differential scanning calorimetry thermograms of cutinase, overview
additional information
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thermal denaturation-induced unfolding of LC-cutinase is analyzed at pH 8.0 by circular dichroism spectroscopy, kinetics of transition of the thermal denaturation, overview. The disulfide bond formed by Cys275 and Cys292 contributes not only to the thermodynamic stability but also to the kinetic stability of LC-cutinase
