6-aminohexanoate-dimer hydrolase
6-aminohexanoate-dimer hydrolase | |||||||||
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Identifiers | |||||||||
EC number | 3.5.1.46 | ||||||||
CAS number | 75216-15-8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / EGO | ||||||||
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In enzymology, a 6-aminohexanoate-dimer hydrolase (EC 3.5.1.46) is an enzyme that catalyzes the chemical reaction
- N-(6-aminohexanoyl)-6-aminohexanoate + H2O 2 6-aminohexanoate
Thus, the two substrates of this enzyme are N-(6-aminohexanoyl)-6-aminohexanoate and H2O, whereas its product is 6-aminohexanoate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-(6-aminohexanoyl)-6-aminohexanoate amidohydrolase. This enzyme is also called 6-aminohexanoic acid oligomer hydrolase.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1WYB, 1WYC, and 2DCF.
See also
References
- Okada H; Terada, T; Taniguchi, T; Takene, Y; Masuda, S; Matsunaga, N; Okada, H (1981). "Purification and characterization of 6-aminohexanoic-acid-oligomer hydrolase of Flavobacterium sp. Ki72". Eur. J. Biochem. 116 (3): 547–51. doi:10.1111/j.1432-1033.1981.tb05371.x. PMID 7262074.
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