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A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.
ENZYME entry: EC 4.5.1.2
| Accepted Name |
|---|
| 3-chloro-D-alanine dehydrochlorinase.
|
| Reaction catalysed |
|---|
| 3-chloro-D-alanine + H(2)O <=> pyruvate + chloride + NH(3) |
| Cofactor(s) |
|---|
| Pyridoxal 5'-phosphate.
|
| Comment(s) |
|---|
- The enzyme cleaves a carbon-chlorine bond, releasing a chloride and
an unstable enamine product that tautomerizes to an imine form, which
undergoes a hydrolytic deamination to form pyruvate and ammonia.
- The latter reaction, which can occur spontaneously, can also be
catalyzed by EC 3.5.99.10.
- The enzyme's activity can also result in beta-replacement reactions,
e.g. in the presence of hydrogen sulfide it can convert 3-chloro-D-
alanine into D-cysteine and chloride.
|
| Cross-references |
|---|
| BRENDA | 4.5.1.2 |
| EC2PDB | 4.5.1.2 |
| ExplorEnz | 4.5.1.2 |
| PRIAM enzyme-specific profiles | 4.5.1.2 |
| KEGG Ligand Database for Enzyme Nomenclature | 4.5.1.2 |
| IUBMB Enzyme Nomenclature | 4.5.1.2 |
| IntEnz | 4.5.1.2 |
| MEDLINE | Find literature relating to 4.5.1.2 |
| MetaCyc | 4.5.1.2 |
View entry in original ENZYME format
View entry in raw text format (no links)
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 4.5.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.5.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 4.-.-.-