CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.40 | 3-Layer(aba) Sandwich | |
3.40.710 | Beta-lactamase | |
3.40.710.10 | DD-peptidase/beta-lactamase superfamily |
Domain Context
CATH Clusters
Superfamily | DD-peptidase/beta-lactamase superfamily |
Functional Family | 6-aminohexanoate-dimer hydrolase |
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.
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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.
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UniProtKB Entries (1)
P07062 |
NYLC_FLASK
Flavobacterium sp. K172
6-aminohexanoate-dimer hydrolase
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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.
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