Acylphosphatase

acylphosphatase

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
Acylphosphatase

Structure of acylphosphatase.[2]
Identifiers
Symbol Acylphosphatase
Pfam PF00708
InterPro IPR001792
PROSITE PDOC00136
SCOP 1aps
SUPERFAMILY 1aps

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:

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.


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