| ID: | 4.3.1.3 | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Description: | Histidine ammonia-lyase. | ||||||||||
| Alternative Name: |
Histidine alpha-deaminase. Histidinase. Histidase. | ||||||||||
| Prosite: | PDOC00424; | ||||||||||
| PDB: |
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| Cath: | 1.10.274.20; 1.10.275.10; 1.20.200.10; |
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 4.3.1.3 |
| BRENDA Enzyme Link: | BRENDA 4.3.1.3 |
| KEGG Enzyme Link: | KEGG4.3.1.3 |
| BioCyc Enzyme Link: | BioCyc 4.3.1.3 |
| ExPASy Enzyme Link: | ExPASy4.3.1.3 |
| EC2PDB Enzyme Link: | EC2PDB 4.3.1.3 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.3.1.3 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.3.1.3 |
| IntEnz Enzyme Link: | IntEnz 4.3.1.3 |
| MEDLINE Enzyme Link: | MEDLINE 4.3.1.3 |
| RHEA:21232 | L-histidine = NH4(+) + trans-urocanate |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[NH2;+0:3])-[CH2;+0:4]-[*:5]>>[*:1]-[CH;+0:2]=[CH;+0:4]-[*:5].[NH3;+0:3] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Friedel-Crafts-type mechanism for the enzymatic elimination of ammonia from histidine and phenylalanine. | Poppe L, Rétey J | 2005 Jun 13 | 15906398 |
| Characterization of the active site of histidine ammonia-lyase from Pseudomonas putida. | Röther D, Poppe L, Viergutz S, Langer B, Rétey J | 2001 Dec | 11732994 |