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
PROSITEPDOC00068
BRENDA1.5.5.2
EC2PDB1.5.5.2
ExplorEnz1.5.5.2
PRIAM enzyme-specific profiles1.5.5.2
KEGG Ligand Database for Enzyme Nomenclature1.5.5.2
IUBMB Enzyme Nomenclature1.5.5.2
IntEnz1.5.5.2
MEDLINEFind literature relating to 1.5.5.2
MetaCyc1.5.5.2
UniProtKB/Swiss-Prot
P92983, PROD1_ARATH;  Q8RMG1, PROD1_BACNA;  O32179, PROD1_BACSU;  
Q6NKX1, PROD2_ARATH;  Q8L2I5, PROD2_BACNA;  P94390, PROD2_BACSU;  
A6QQ74, PROD2_BOVIN;  Q9UF12, PROD2_HUMAN;  Q8VCZ9, PROD2_MOUSE;  
Q2V057, PROD2_RAT;  Q6PAY6, PROD2_XENLA;  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_ENTAE;  P23725, PUTA_KLEPN;  P95629, PUTA_RHIML;  
P10503, PUTA_SALTY;  

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