EC Tree |
3. Hydrolases |
3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
3.5.2 In cyclic amides |
ID: | 3.5.2.12 | ||
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Description: | 6-aminohexanoate-cyclic-dimer hydrolase. | ||
Prosite: | PDOC00494; | ||
PDB: |
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Cath: | 1.20.5.1730; 3.40.710.10; 3.90.1300.10; 1.20.58.710; |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 3.5.2.12 |
BRENDA Enzyme Link: | BRENDA 3.5.2.12 |
KEGG Enzyme Link: | KEGG3.5.2.12 |
BioCyc Enzyme Link: | BioCyc 3.5.2.12 |
ExPASy Enzyme Link: | ExPASy3.5.2.12 |
EC2PDB Enzyme Link: | EC2PDB 3.5.2.12 |
ExplorEnz Enzyme Link: | ExplorEnz 3.5.2.12 |
PRIAM enzyme-specific profiles Link: | PRIAM 3.5.2.12 |
IntEnz Enzyme Link: | IntEnz 3.5.2.12 |
MEDLINE Enzyme Link: | MEDLINE 3.5.2.12 |
RHEA:16225 | 1,8-diazacyclotetradecane-2,9-dione + H2O = N-(6-aminohexanoyl)-6-aminohexanoate |
RULE(radius=1) | ([*:1]-[NH2;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[OH;+0:6])>>[*:1]-[NH;+0:2]-[C;H0;+0:4](=[*:3])-[*:5].[OH2;+0:6] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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6-Aminohexanoic acid cyclic dimer hydrolase. A new cyclic amide hydrolase produced by Achromobacter guttatus KI74. | Kinoshita S, Negoro S, Muramatsu M, Bisaria VS, Sawada S, Okada H | 1977 Nov 1 | 923591 |
X-ray crystallographic analysis of the 6-aminohexanoate cyclic dimer hydrolase: catalytic mechanism and evolution of an enzyme responsible for nylon-6 byproduct degradation. | Yasuhira K, Shibata N, Mongami G, Uedo Y, Atsumi Y, Kawashima Y, Hibino A, Tanaka Y, Lee YH, Kato D, Takeo M, Higuchi Y, Negoro S | 2010 Jan 8 | 19889645 |