View source for Acylphosphatase

{{enzyme
| Name = acylphosphatase
| EC_number = 3.6.1.7
| CAS_number = 9012-34-4
| IUBMB_EC_number = 
| GO_code = 0003998
| image = PDB.png
| width = 
| caption = <ref name="urlRCSB Protein Data Bank - Structure Summary for 2W4P - HUMAN COMMON-TYPE ACYLPHOSPHATASE VARIANT, A99G">{{cite web |url=http://www.rcsb.org/pdb/explore/explore.do?structureId=2W4P |title=RCSB Protein Data Bank - Structure Summary for 2W4P - HUMAN COMMON-TYPE ACYLPHOSPHATASE VARIANT, A99G |format= |work= |accessdate=}}</ref>
}}
{{Pfam_box
| Symbol = Acylphosphatase
| Name = Acylphosphatase
| image = PDB 1aps EBI.jpg
| width = 
| caption = Structure of acylphosphatase.<ref name="pmid1313885">{{cite journal |vauthors =Pastore A, Saudek V, Ramponi G, Williams RJ |title=Three-dimensional structure of acylphosphatase. Refinement and structure analysis |journal=J. Mol. Biol. |volume=224 |issue=2 |pages=427–40 |date=March 1992 |pmid=1313885 |doi= 10.1016/0022-2836(92)91005-A|url=}}</ref>
| Pfam = PF00708
| InterPro=IPR001792
| SMART=
| PROSITE= PDOC00136
| SCOP = 1aps
| TCDB =
| OPM family =
| OPM protein =
| PDB = {{PDB2|2GV1}}, {{PDB2|1APS}}, {{PDB2|2FHM}}, {{PDB2|1Y9O}}, {{PDB2|1URR}}, {{PDB2|1W2I}}, {{PDB2|2ACY}}, {{PDB2|2BJD}}, {{PDB2|1V3Z}}, {{PDB2|2HLT}}, {{PDB2|2HLU}}, {{PDB2|2BJE}}, {{PDB2|3BR8}}, {{PDB2|1ULR}}
}}

In [[enzymology]], an '''acylphosphatase''' ({{EC number|3.6.1.7}}) is an [[enzyme]] that [[catalysis|catalyzes]] the following [[chemical reaction]]:<ref name="pmid9118002">{{cite journal | vauthors = Stefani M, Taddei N, Ramponi G | title = Insights into acylphosphatase structure and catalytic mechanism | journal = Cell. Mol. Life Sci. | volume = 53 | issue = 2 | pages = 141–51 |date=February 1997 | pmid = 9118002 | doi = 10.1007/PL00000585 | url =  }}</ref>

[[Image:Acylphosphate_rxn.png|500px|The chemical reaction catalyzed by acylphosphatase enzymes.]]

Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[acylphosphate]] and [[water|H<sub>2</sub>O]], whereas its two [[product (chemistry)|products]] are [[carboxylate]] and [[phosphate]].

==Function==
This enzyme belongs to the family of [[hydrolase]]s, specifically those acting on acid anhydrides in phosphorus-containing anhydrides.  The [[List of enzymes|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 [[metabolism|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 [[Protein Data Bank|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.<ref>Rational stabilization of enzymes by computational redesign of surface charge-charge interactions. Gribenko et al. PNAS 2009. {{PMID|19196981}}.</ref> Most structures are monomeric <ref>[http://www.ebi.ac.uk/pdbe-srv/PDBeXplore/enzyme/?ec=3.6.1.7&tab=assemblies PDBe Enzyme Browser].</ref>

== Isozymes ==
Humans express the following two acylphosphatase isozymes:
{|
|- valign="top"
|{{infobox protein
| Name = [[ACYP1|acylphosphatase 1, erythrocyte (common) type]]
| caption = 
| image = 
| width = 
| HGNCid = 179
| Symbol = [[ACYP1]]
| AltSymbols = 
| EntrezGene = 97
| OMIM = 600875
| RefSeq = NM_001107
| UniProt = P07311
| PDB = 
| ECnumber = 3.6.1.7
| Chromosome = 14
| Arm = q
| Band = 24.3
| LocusSupplementaryData = 
}}
|{{infobox protein
| Name = [[ACYP2|acylphosphatase 2, muscle type]]
| caption = 
| image = 
| width = 
| HGNCid = 180
| Symbol = [[ACYP2]]
| AltSymbols = 
| EntrezGene = 98
| OMIM = 102595
| RefSeq = NM_138448
| UniProt = P14621
| PDB = 
| ECnumber = 3.6.1.7
| Chromosome = 2
| Arm = p
| Band = 16.2
| LocusSupplementaryData = 
}}
|}

==References==
{{reflist}}

{{Acid anhydride hydrolases}}
{{Enzymes}}
{{Portal bar|Molecular and Cellular Biology|border=no}}

[[Category:EC 3.6.1]]
[[Category:Enzymes of known structure]]


{{3.6-enzyme-stub}}