Acylphosphatase

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acylphosphatase
PDB.png
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
PDB 1aps EBI.jpg
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]

The chemical reaction catalyzed by acylphosphatase enzymes.

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

Function[edit]

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[edit]

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[edit]

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
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
Locus Chr. 2 p16.2

References[edit]

  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.