Enzyme

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     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.2 In cyclic amides
ID:3.5.2.12
Description:6-aminohexanoate-cyclic-dimer hydrolase.
Prosite: PDOC00494;
PDB:
PDBScop
Cath: 1.20.5.1730; 3.40.710.10; 3.90.1300.10; 1.20.58.710;

3D structure

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References

External Links

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
MSA:

3.5.2.12;

Phylogenetic Tree:

3.5.2.12;

Uniprot:
M-CSA:
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

References

TitleAuthorsDatePubMed ID
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 H1977 Nov 1923591
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 S2010 Jan 819889645