H
IPR036046

Acylphosphatase-like domain superfamily

InterPro entry
Short nameAcylphosphatase-like_dom_sf
Overlapping entries
 
BLUF domain (IPR007024)
Acylphosphatase (IPR020456)

Description

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
[5]
, its substrates including 1,3-diphosphoglycerate and carbamyl phosphate
[1]
. The enzyme has a mainly β-sheet structure with 2 short α-helical segments. It is distributed in a tissue-specific manner in a wide variety of species, although its physiological role is as yet unknown
[1]
: 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, 2]
.

References

1.Identification and description of alpha-helical regions in horse muscle acylphosphatase by 1H nuclear magnetic resonance spectroscopy. Saudek V, Atkinson RA, Williams RJ, Ramponi G. J. Mol. Biol. 205, 229-39, (1989). View articlePMID: 2538623

2.Crystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domain. Rosano C, Zuccotti S, Bucciantini M, Stefani M, Ramponi G, Bolognesi M. J. Mol. Biol. 321, 785-96, (2002). View articlePMID: 12206761

3.The primary structure of chicken muscle acylphosphatase isozyme Ch1. Minowa O, Ohba Y, Mizuno Y, Shiokawa H. J. Biochem. 102, 1213-20, (1987). View articlePMID: 2830253

4.Duplication of hyp genes involved in maturation of [NiFe] hydrogenases in Alcaligenes eutrophus H16. Wolf I, Buhrke T, Dernedde J, Pohlmann A, Friedrich B. Arch. Microbiol. 170, 451-9, (1998). View articlePMID: 9799289

5.The primary structure of two molecular species of porcine organ-common type acylphosphatase. Mizuno Y, Kanesaka Y, Fujita H, Minowa O, Shiokawa H. J. Biochem. 110, 790-4, (1991). View articlePMID: 1664426

Cross References

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