Acylphosphatase

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

acylphosphatase
Identifiers
EC number3.6.1.7
CAS number9012-34-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Acylphosphatase
Structure of acylphosphatase.[2]
Identifiers
SymbolAcylphosphatase
PfamPF00708
InterProIPR001792
PROSITEPDOC00136
SCOP21aps / SCOPe / SUPFAM

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:

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
SymbolACYP1
NCBI gene97
HGNC179
OMIM600875
RefSeqNM_001107
UniProtP07311
Other data
EC number3.6.1.7
LocusChr. 14 q24.3
acylphosphatase 2, muscle type
Identifiers
SymbolACYP2
NCBI gene98
HGNC180
OMIM102595
RefSeqNM_138448
UniProtP14621
Other data
EC number3.6.1.7
LocusChr. 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. S2CID 24072481.
  4. Gribenko AV, Patel MM, Liu J, McCallum SA, Wang C, Makhatadze GI (February 2009). "Rational stabilization of enzymes by computational redesign of surface charge-charge interactions". Proceedings of the National Academy of Sciences of the United States of America. 106 (8): 2601–6. Bibcode:2009PNAS..106.2601G. doi:10.1073/pnas.0808220106. PMC 2650310. PMID 19196981.
  5. "Enzyme 3.6.1.7". PDBe Enzyme Browser.


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