EC Number   |
Natural Substrates |
|---|
   3.1.1.74 | cutin + H2O |
- |
| 3.1.1.74 | cutin + H2O |
cutinases perform their catalysis in two discrete steps, with a covalent intermediate that links the catalytic serine to the carbonyl group of the ester being hydrolyzed |
| 3.1.1.74 | cutin + H2O |
hydrolysis of tritiated apple cutin, and GC-MS analysis of the hydrolysis products, overview |
| 3.1.1.74 | more |
constitutive enzyme |
| 3.1.1.74 | more |
induced by cutin |
| 3.1.1.74 | more |
Cutinase is known for its hydrolytic activity for a variety of esters ranging from soluble p-nitrophenyl esters to insoluble long-chain triglycerides. The hydrolytic activity of cutinase, especially on p-nitrophenyl esters of fatty acids, is extremely sensitive to fatty acid chain length. |
| 3.1.1.74 | more |
cutinase is an esterase, whose active site, located at the middle of a sharp turn between beta-strand and alpha-helix, is composed by the triad Ser120, Asp175 and His188 |
| 3.1.1.74 | more |
the enzyme exhibits a broad substrate specificity against plant cutin, synthetic polyesters, insoluble triglycerides, and soluble esters |
| 3.1.1.74 | more |
cutinase is a multi-functional esterase, which shows hydrolytic activity (cutin and a variety of soluble synthetic esters, insoluble triglycerides and polyesters), synthetic activity and transester activity |
| 3.1.1.74 | more |
cutinases are capable of catalyzing esterification and transesterification |
