EC Tree |
3. Hydrolases |
3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
3.5.3 In linear amidines |
ID: | 3.5.3.5 |
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Description: | Formimidoylaspartate deiminase. |
Alternative Name: |
Formiminoaspartate deiminase. |
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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 3.5.3.5 |
BRENDA Enzyme Link: | BRENDA 3.5.3.5 |
KEGG Enzyme Link: | KEGG3.5.3.5 |
BioCyc Enzyme Link: | BioCyc 3.5.3.5 |
ExPASy Enzyme Link: | ExPASy3.5.3.5 |
EC2PDB Enzyme Link: | EC2PDB 3.5.3.5 |
ExplorEnz Enzyme Link: | ExplorEnz 3.5.3.5 |
PRIAM enzyme-specific profiles Link: | PRIAM 3.5.3.5 |
IntEnz Enzyme Link: | IntEnz 3.5.3.5 |
MEDLINE Enzyme Link: | MEDLINE 3.5.3.5 |
RHEA:13661 | H2O + N-formimidoyl-L-aspartate = N-formyl-L-aspartate + NH4(+) |
RULE(radius=1) | [*:1]-[CH;+0:2]=[NH;+0:3].[OH2;+0:4]>>[*:1]-[CH;+0:2]=[O;H0;+0:4].[NH3;+0:3] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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N-formimino-L-aspartic acid as an intermediate in the enzymatic conversion of imidazoleacetic acid to formylaspartic acid. | HAYAISHI O, TABOR H, HAYAISHI T | 1957 Jul | 13449062 |