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
-
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
- 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
Advanced search results
Renatured
Renatured on EC 3.1.1.74 - cutinase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
after unfolding cutinase at 80°C, cooling at 20°C restores the initial conformation
refolding from the pH-denatured state. Existence of two distinct intermediate states in cutinase folding: an unfolding intermediate and an off-pathway folding intermediate.
-