InterPro domain: IPR001792

Acylphosphatase ( 3.6.1.7 ) is an enzyme of approximately 98 amino acid residues that specifically catalyses the hydrolysis of the carboxyl-phosphate bond of acylphosphates [ 1 ], its substrates including 1,3-diphosphoglycerate and carbamyl phosphate [ 2 ]. The enzyme has a mainly beta-sheet structure with 2 short alpha-helical segments. It is distributed in a tissue-specific manner in a wide variety of species, although its physiological role is as yet unknown [ 3 ]: it may, however, play a part in the regulation of the glycolytic pathway and pyrimidine biosynthesis [ 3 ]. There are two known isozymes. One seems to be specific to muscular tissues, the other, called 'organ-common type', is found in many different tissues. A number of bacterial and archebacterial hypothetical proteins are highly similar to that enzyme and that probably possess the same activity.

An acylphosphatase-like domain is also found in some prokaryotic hydrogenase maturation HypF carbamoyltransferases [ 4 , 5 ].

1. The primary structure of two molecular species of porcine organ-common type acylphosphatase. J. Biochem. 110, 790-4
2. Identification and description of alpha-helical regions in horse muscle acylphosphatase by 1H nuclear magnetic resonance spectroscopy. J. Mol. Biol. 205, 229-39
3. The primary structure of chicken muscle acylphosphatase isozyme Ch1. J. Biochem. 102, 1213-20
4. Duplication of hyp genes involved in maturation of [NiFe] hydrogenases in Alcaligenes eutrophus H16. Arch. Microbiol. 170, 451-9
5. Crystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domain. J. Mol. Biol. 321, 785-96