EC Tree |
3. Hydrolases |
3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
3.5.4 In cyclic amidines |
ID: | 3.5.4.22 |
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Description: | 1-pyrroline-4-hydroxy-2-carboxylate deaminase. |
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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 3.5.4.22 |
BRENDA Enzyme Link: | BRENDA 3.5.4.22 |
KEGG Enzyme Link: | KEGG3.5.4.22 |
BioCyc Enzyme Link: | BioCyc 3.5.4.22 |
ExPASy Enzyme Link: | ExPASy3.5.4.22 |
EC2PDB Enzyme Link: | EC2PDB 3.5.4.22 |
ExplorEnz Enzyme Link: | ExplorEnz 3.5.4.22 |
PRIAM enzyme-specific profiles Link: | PRIAM 3.5.4.22 |
IntEnz Enzyme Link: | IntEnz 3.5.4.22 |
MEDLINE Enzyme Link: | MEDLINE 3.5.4.22 |
RHEA:10560 | 4-hydroxy-1-pyrroline-2-carboxylate + H(+) + H2O = 2,5-dioxopentanoate + NH4(+) |
RULE(radius=1) | [*:1]=[C;H0;+0:2](-[OH;+0:3])-[C;H0;+0:4]1=[N;H0;+0:5]-[CH2;+0:6]-[CH;+0:7](-[OH;+0:8])-[*:9]-1.[H+;H0:10].[OH2;+0:11]>>[*:1]=[CH;+0:2]-[CH2;+0:4]-[*:9]-[C;H0;+0:7](=[O;H0;+0:8])-[C;H0;+0:6](=[O;H0;+0:3])-[OH;+0:11].[NH3;+0:5] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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Isolation and identification of 2,5-dioxovalerate, an intermediate in the bacterial oxidation of hydroxyproline. | Singh RM, Adams E | 1965 Nov | 5845839 |
Enzymatic deamination of delta-1-pyrroline-4-hydroxy-2-carboxylate to 2,5-dioxovalerate (alpha-ketoglutaric semialdehyde). | Singh RM, Adams E | 1965 Nov | 5845838 |