EC Tree |
3. Hydrolases |
3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
3.5.4 In cyclic amidines |
ID: | 3.5.4.20 |
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Description: | Pyrithiamine deaminase. |
Click one PDB to see exact 3D structure provided by NGL.
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 3.5.4.20 |
BRENDA Enzyme Link: | BRENDA 3.5.4.20 |
KEGG Enzyme Link: | KEGG3.5.4.20 |
BioCyc Enzyme Link: | BioCyc 3.5.4.20 |
ExPASy Enzyme Link: | ExPASy3.5.4.20 |
EC2PDB Enzyme Link: | EC2PDB 3.5.4.20 |
ExplorEnz Enzyme Link: | ExplorEnz 3.5.4.20 |
PRIAM enzyme-specific profiles Link: | PRIAM 3.5.4.20 |
IntEnz Enzyme Link: | IntEnz 3.5.4.20 |
MEDLINE Enzyme Link: | MEDLINE 3.5.4.20 |
RHEA:14537 | 1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(2-hydroxyethyl)-2-methylpyridinium + H(+) + H2O = 1-(4-hydroxy-2-methylpyrimid-5-ylmethyl)-3-(2-hydroxyethyl)-2-methylpyridinium + NH4(+) |
RULE(radius=1) | [*:1]:[c;H0;+0:2](:[*:3])-[NH2;+0:4].[H+;H0:5].[OH2;+0:6]>>[*:1]:[c;H0;+0:2](:[*:3])-[OH;+0:6].[NH3;+0:4] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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Metabolism of pyrithiamine by the pyrithiamine-requiring mutant of Staphylococcus aureus. | Sinha AK, Chatterjee GC | 1968 Mar | 5641872 |