EC number:3.5.2.18

Enzyme

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EC Tree
     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.2 In cyclic amides
ID:3.5.2.18
Description:Enamidase.
Cath: 1.10.1040.10; 1.10.150.120; 3.20.20.140; 3.30.365.10; 3.30.390.50; 3.30.465.10; 3.40.50.720; 2.30.40.10; 3.40.50.12340; 3.10.20.30;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.2.18
BRENDA Enzyme Link: BRENDA 3.5.2.18
KEGG Enzyme Link: KEGG3.5.2.18
BioCyc Enzyme Link: BioCyc 3.5.2.18
ExPASy Enzyme Link: ExPASy3.5.2.18
EC2PDB Enzyme Link: EC2PDB 3.5.2.18
ExplorEnz Enzyme Link: ExplorEnz 3.5.2.18
PRIAM enzyme-specific profiles Link: PRIAM 3.5.2.18
IntEnz Enzyme Link: IntEnz 3.5.2.18
MEDLINE Enzyme Link: MEDLINE 3.5.2.18

EC number:3.5.2.18

MSA:

3.5.2.18;
Phylogenetic Tree:

3.5.2.18;
Uniprot:
M-CSA:
RHEA:17209 1,4,5,6-tetrahydro-6-oxonicotinate + 2 H2O = 2-formylglutarate + NH4(+)
RULE(radius=1) [*:1]=[C;H0;+0:2](-[OH;+0:3])-[*:4]-[*:5]-[CH;+0:6](-[*:7])-[CH;+0:8]=[O;H0;+0:9].[NH3;+0:10]>>[*:1]=[C;H0;+0:2]1-[*:4]-[*:5]-[C;H0;+0:6](-[*:7])=[CH;+0:8]-[NH;+0:10]-1.[OH2;+0:3].[OH2;+0:9]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
The crystal structure of enamidase: a bifunctional enzyme of the nicotinate catabolism.Kress D, Alhapel A, Pierik AJ, Essen LO2008 Dec 2618805424
Molecular and functional analysis of nicotinate catabolism in Eubacterium barkeri.Alhapel A, Darley DJ, Wagener N, Eckel E, Elsner N, Pierik AJ2006 Aug 1516894175