| Type: | Conserved_site | Name: | Acylphosphatase, conserved site |
| Description: | Acylphosphatase () is an enzyme of approximately 98 amino acid residues that specifically catalyses the hydrolysis of the carboxyl-phosphate bond of acylphosphates [], its substrates including 1,3-diphosphoglycerate and carbamyl phosphate []. 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 []: it may, however, play a part in the regulation of the glycolytic pathway and pyrimidine biosynthesis []. 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. This entry represents a conserved site found in the acylphosphatase domain. It is also found in an acylphosphatase-like domain in some prokaryotic hydrogenase maturation HypF carbamoyltransferases [, ]. | Short Name: | Acylphosphatase_CS |
