Acylphosphatase

acylphosphatase
[1]
Identifiers
EC number	3.6.1.7
CAS number	9012-34-4
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search PMC articles PubMed articles NCBI proteins

Acylphosphatase
Structure of acylphosphatase.[2]
Identifiers
Symbol	Acylphosphatase
Pfam	PF00708
InterPro	IPR001792
PROSITE	PDOC00136
SCOP	1aps
SUPERFAMILY	1aps
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

In enzymology, an acylphosphatase (EC 3.6.1.7) is an enzyme that catalyzes the following chemical reaction:^[3]

Thus, the two substrates of this enzyme are acylphosphate and H₂O, whereas its two products are carboxylate and phosphate.

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.^[4] Most structures are monomeric ^[5]

Isozymes

Humans express the following two acylphosphatase isozymes:

acylphosphatase 1, erythrocyte (common) type Identifiers Symbol ACYP1 Entrez 97 HUGO 179 OMIM 600875 RefSeq NM_001107 UniProt P07311 Other data EC number 3.6.1.7 Locus Chr. 14 q24.3

acylphosphatase 2, muscle type Identifiers Symbol ACYP2 Entrez 98 HUGO 180 OMIM 102595 RefSeq NM_138448 UniProt P14621 Other data EC number 3.6.1.7 Locus Chr. 2 p16.2

References

1. "RCSB Protein Data Bank - Structure Summary for 2W4P - HUMAN COMMON-TYPE ACYLPHOSPHATASE VARIANT, A99G".
2. Pastore A, Saudek V, Ramponi G, Williams RJ (March 1992). "Three-dimensional structure of acylphosphatase. Refinement and structure analysis". J. Mol. Biol. 224 (2): 427–40. doi:10.1016/0022-2836(92)91005-A. PMID 1313885.
3. Stefani M, Taddei N, Ramponi G (February 1997). "Insights into acylphosphatase structure and catalytic mechanism". Cell. Mol. Life Sci. 53 (2): 141–51. doi:10.1007/PL00000585. PMID 9118002.
4. Rational stabilization of enzymes by computational redesign of surface charge-charge interactions. Gribenko et al PNAS 2009. PMID 19196981.
5. PDBe Enzyme Browser.