Acylphosphatase

In enzymology, an acylphosphatase is an enzyme that catalyzes the hydrolysis of the carboxyl-phosphate bond of acylphosphates, with  acylphosphate and H2O 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: