CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
6 | Special |
|
6.10 | Helix non-globular |
|
6.10.250 | Single alpha-helices involved in coiled-coils or other helix-helix interfaces |
|
6.10.250.420 |
Domain Context
CATH Clusters
| Superfamily | 6.10.250.420 |
| Functional Family |
Enzyme Information
| 3.5.1.46 |
6-aminohexanoate-oligomer exohydrolase.
based on mapping to UniProt P07061
(1) (N-(6-aminohexanoyl))(n) + H(2)O = (N-(6-aminohexanoyl))(n-1) + 6-aminohexanoate. (2) N-(6-aminohexanoyl)-6-aminohexanoate + H(2)O = 2 6-aminohexanoate.
-!- The enzyme is involved in degradation of nylon-6 oligomers. -!- It degrades linear oligomers of 6-aminohexanoate with a degree of polymerization of 2-20 by exo-type cleavage, removing residues sequentially from the N-terminus. -!- Activity decreases with the increase of the polymerization number of the oligomer; cf. EC 3.5.1.117 and EC 3.5.2.12.
|
| 3.5.1.46 |
6-aminohexanoate-oligomer exohydrolase.
based on mapping to UniProt P07062
(1) (N-(6-aminohexanoyl))(n) + H(2)O = (N-(6-aminohexanoyl))(n-1) + 6-aminohexanoate. (2) N-(6-aminohexanoyl)-6-aminohexanoate + H(2)O = 2 6-aminohexanoate.
-!- The enzyme is involved in degradation of nylon-6 oligomers. -!- It degrades linear oligomers of 6-aminohexanoate with a degree of polymerization of 2-20 by exo-type cleavage, removing residues sequentially from the N-terminus. -!- Activity decreases with the increase of the polymerization number of the oligomer; cf. EC 3.5.1.117 and EC 3.5.2.12.
|
UniProtKB Entries (1)
| P07062 |
NYLC_FLASK
Flavobacterium sp. K172
6-aminohexanoate-dimer hydrolase
|
PDB Structure
| PDB | 2ZLY |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Two alternative modes for optimizing nylon-6 byproduct hydrolytic activity from a carboxylesterase with a beta-lactamase fold: X-ray crystallographic analysis of directly evolved 6-aminohexanoate-dimer hydrolase.
Protein Sci.
|