6-aminohexanoate-dimer hydrolase | |||||||||
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Identifiers | |||||||||
EC no. | 3.5.1.46 | ||||||||
CAS no. | 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 / QuickGO | ||||||||
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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 two molecules of 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
- Kinoshita S, Terada T, Taniguchi T, Takene Y, Masuda S, Matsunaga N, Okada H (June 1981). "Purification and characterization of 6-aminohexanoic-acid-oligomer hydrolase of Flavobacterium sp. Ki72". European Journal of Biochemistry. 116 (3): 547–51. doi:10.1111/j.1432-1033.1981.tb05371.x. PMID 7262074.
Hydrolases: carbon-nitrogen non-peptide (EC 3.5) | |
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3.5.1: Linear amides / Amidohydrolases | |
3.5.2: Cyclic amides/ Amidohydrolases | |
3.5.3: Linear amidines/ Ureohydrolases | |
3.5.4: Cyclic amidines/ Aminohydrolases | |
3.5.5: Nitriles/ Aminohydrolases | |
3.5.99: Other |
Enzymes | |
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Activity | |
Regulation | |
Classification | |
Kinetics | |
Types |
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