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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 3.1.3.76

Accepted Name
Lipid-phosphate phosphatase.
Alternative Name(s)
Dihydroxy fatty acid phosphatase.
Hydroxy fatty acid phosphatase.
Hydroxy lipid phosphatase.
Soluble epoxide hydrolase.
Reaction catalysed
(9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H(2)O <=> (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate
Cofactor(s)
Mg(2+).
Comment(s)
  • The enzyme from mammals is a bifunctional enzyme: the N-terminal domain exhibits lipid-phosphate-phosphatase activity and the C-terminal domain has the activity of EC 3.3.2.10.
  • The best substrates for this enzyme are 10-hydroxy-9- (phosphonooxy)octadecanoates, with the threo- form being a better substrate than the erythro- form.
  • The phosphatase activity is not found in plant EC 3.3.2.10 or in mammalian EC 3.3.2.9.
Cross-references
BRENDA3.1.3.76
EC2PDB3.1.3.76
ExplorEnz3.1.3.76
PRIAM enzyme-specific profiles3.1.3.76
KEGG Ligand Database for Enzyme Nomenclature3.1.3.76
IUBMB Enzyme Nomenclature3.1.3.76
IntEnz3.1.3.76
MEDLINEFind literature relating to 3.1.3.76
MetaCyc3.1.3.76
UniProtKB/Swiss-Prot
P34913, HYES_HUMAN;  P34914, HYES_MOUSE;  Q6Q2C2, HYES_PIG;  
P80299, HYES_RAT;  

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.1.3.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-