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:
[Image:Acylphosphate_rxn.png|500px|The chemical reaction catalyzed by acylphosphatase enzymes.]

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:

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: