EC Number   |
General Information |
Reference |
|---|
   3.1.1.74 | evolution |
cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters |
-, 729450 |
| 3.1.1.74 | evolution |
cutinases are serine hydrolases that belong to the alpha/beta-hydrolase superfamily, which is divided into 2 eukaryotic and one prokaryotic subgroup, phylogenetic tree, overview. They possess a classical Ser-His-Asp catalytic triad, in which the catalytic serine is exposed to solvent. Because cutinases lack the hydrophobic lid that covers the active site serine in true lipases, the cutinase active site is large enough to accommodate the high-molecular-weight substrate cutin, and some of them can also hydrolyse high-molecular-weight synthetic polyesters. The cutinase from Thermobifida alba also adopts an alpha/beta fold, but it is larger than the ones from other family members. It contains nine sheets at the heart of the protein, two of which are antiparallel, rather than the five parallel sheets present in the fungal enzymes |
729450 |
| 3.1.1.74 | evolution |
modeling and comparison of the structures of the two closely related cutinases Thc_Cut1 and Thc_Cut2 from Thermobifida cellulosilytica DSM44535 reveal that dissimilarities in their electrostatic and hydrophobic surface properties in the vicinity to the active site might be responsible for pronounced differences in hydrolysis efficiencies of polyester (i.e., PET, polyethyleneterephthalate), isozyme Thc_Cut2 hydrolyzes PET much less efficiently than Thc_Cut1 |
-, 729454 |
| 3.1.1.74 | evolution |
modeling and comparison of the structures of the two closely related cutinases Thc_Cut1 and Thc_Cut2 from Thermobifida cellulosilytica DSM44535 reveal that dissimilarities in their electrostatic and hydrophobic surface properties in the vicinity to the active site might be responsible for pronounced differences in hydrolysis efficiencies of polyester (i.e., PET, polyethyleneterephthalate), Thc_Cut2 hydrolyzes PET much less efficiently than Thc_Cut1 |
-, 729454 |
| 3.1.1.74 | evolution |
residues N168, Q170 an N171 of Glomerella cingulata are highly conserved with all cutinases of fungal phytopathogens |
730865 |
| 3.1.1.74 | evolution |
the enzyme contains the conserved motif G-Y-S-Q-G surrounding the active site serine as well as the aspartic acid and histidine residues of the cutinase active site |
-, 729077 |
| 3.1.1.74 | malfunction |
specific inhibition of the enzyme blocks infectivity in several pathogen/host systems |
729450 |
| 3.1.1.74 | more |
a search algorithm that allows the in silico identification of PET hydrolase gene candidates from genomes and metagenomes is developed. 504 novel possible enzyme candidates in the UniProtKB and nonredundant RefSeq databases and the metagenomic database available in the NCBI database are identified |
749675 |
| 3.1.1.74 | more |
biophysical parameters of cutinase as a function of pH, overview |
713927 |
| 3.1.1.74 | more |
enzyme homology modeling |
-, 729656 |
