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 1.5.5.2
| Accepted Name |
|---|
| Proline dehydrogenase.
|
| Reaction catalysed |
|---|
| L-proline + a quinone <=> (S)-1-pyrroline-5-carboxylate + a quinol |
| Cofactor(s) |
|---|
| FAD.
|
| Comment(s) |
|---|
- The electrons from L-proline are transferred to the FAD cofactor,
and from there to a quinone acceptor.
- In many organisms, ranging from bacteria to mammals, proline is
oxidized to glutamate in a two-step process involving this enzyme and
EC 1.2.1.88.
- Both activities are carried out by the same enzyme in enterobacteria.
- Formerly EC 1.5.99.8.
|
| Cross-references |
|---|
| PROSITE | PDOC00068 |
| BRENDA | 1.5.5.2 |
| EC2PDB | 1.5.5.2 |
| ExplorEnz | 1.5.5.2 |
| PRIAM enzyme-specific profiles | 1.5.5.2 |
| KEGG Ligand Database for Enzyme Nomenclature | 1.5.5.2 |
| IUBMB Enzyme Nomenclature | 1.5.5.2 |
| IntEnz | 1.5.5.2 |
| MEDLINE | Find literature relating to 1.5.5.2 |
| MetaCyc | 1.5.5.2 |
| UniProtKB/Swiss-Prot |
| A6QQ74, HYPDH_BOVIN; | Q9UF12, HYPDH_HUMAN; | Q8VCZ9, HYPDH_MOUSE; |
| Q2V057, HYPDH_RAT; | Q6PAY6, HYPDH_XENLA; | P92983, PROD1_ARATH; |
| Q8RMG1, PROD1_BACNA; | O32179, PROD1_BACSU; | Q6NKX1, PROD2_ARATH; |
| Q8L2I5, PROD2_BACNA; | P94390, PROD2_BACSU; | Q9RW55, PRODH_DEIRA; |
| Q72IB8, PRODH_THET2; | Q148G5, PROD_BOVIN; | O45228, PROD_CAEEL; |
| Q86H28, PROD_DICDI; | Q04499, PROD_DROME; | O43272, PROD_HUMAN; |
| Q9WU79, PROD_MOUSE; | O74524, PROD_SCHPO; | P09368, PUT1_YEAST; |
| P09546, PUTA_ECOLI; | O52485, PUTA_KLEAE; | P23725, PUTA_KLEPN; |
| P95629, PUTA_RHIML; | P10503, PUTA_SALTY; |
|
View entry in original ENZYME format
View entry in raw text format (no links)
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 1.5.5.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.5.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-