title: Acylphosphatase
text: # Acylphosphatase
  
  In enzymology, an acylphosphatase (EC 3.6.1.7) is an enzyme that catalyzes the hydrolysis of the carboxyl-phosphate bond of acylphosphates, with acylphosphate and $H_2O$ as the two substrates of this enzyme, and carboxylate and phosphate as its two products:
  
  ## Function
  
  This enzyme belongs to the family of hydrolases, specifically those acting on acid anhydrides in phosphorus-containing anhydrides. The systematic name of this enzyme class is acylphosphate phosphohydrolase. Other names in common use include acetylphosphatase, 1,3-diphosphoglycerate phosphatase, acetic phosphatase, Ho 1-3, and GP 1-3.
  
  This enzyme participates in 3 metabolic pathways:
  
  * glycolysis / gluconeogenesis
  * pyruvate metabolism, and
  * benzoate degradation via coa ligation.
  
  ## Structural studies
  
  Structures of this enzyme have been solved by both NMR and X-ray crystallography. See the links to PDB structures in the info boxes on the right for a current list of structures available in the PDB. The protein contains a beta sheet stacked on two alpha helices described by CATH as an Alpha-Beta Plait fold. The active site sits between sheet and helices and contains an arginine and an asparagine. Most structures are monomeric
  
  ## Isozymes
  
  Humans express the following two acylphosphatase isozymes:
  
  | acylphosphatase 1, erythrocyte (common) typeIdentifiersSymbolACYP1NCBI gene97HGNC179OMIM600875RefSeqNM_001107UniProtP07311Other dataEC number3.6.1.7LocusChr. 14 q24.3Search forStructuresSwiss-modelDomainsInterPro | acylphosphatase 2, muscle typeIdentifiersSymbolACYP2NCBI gene98HGNC180OMIM102595RefSeqNM_138448UniProtP14621Other dataEC number3.6.1.7LocusChr. 2 p16.2Search forStructuresSwiss-modelDomainsInterPro |
  | - | - |
  