acylphosphatase
{{Short description|Enzyme}}
{{enzyme
| Name = acylphosphatase
| EC_number = 3.6.1.7
| CAS_number = 9012-34-4
| IUBMB_EC_number =
| GO_code = 0003998
| image = PDB.png
| width =
}}
{{Pfam_box
| Symbol = Acylphosphatase
| Name = Acylphosphatase
| image = PDB 1aps EBI.jpg
| width =
| caption = Structure of acylphosphatase.{{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}}
| 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 catalyzes the hydrolysis of the carboxyl-phosphate bond of acylphosphates, with acylphosphate and H2O as the two substrates of this enzyme, and carboxylate and phosphate as its two products:{{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 | s2cid = 24072481 | pmc = 11147357 }}
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.{{cite journal | vauthors = Gribenko AV, Patel MM, Liu J, McCallum SA, Wang C, Makhatadze GI | title = Rational stabilization of enzymes by computational redesign of surface charge-charge interactions | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 106 | issue = 8 | pages = 2601–6 | date = February 2009 | pmid = 19196981 | pmc = 2650310 | doi = 10.1073/pnas.0808220106 | bibcode = 2009PNAS..106.2601G | doi-access = free }} Most structures are monomeric {{cite web | url = http://www.ebi.ac.uk/pdbe-srv/PDBeXplore/enzyme/?ec=3.6.1.7&tab=assemblies | title = Enzyme 3.6.1.7 | work = PDBe Enzyme Browser }}
Isozymes
Humans express the following two acylphosphatase isozymes:
| valign="top"
|{{infobox protein | Name = 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 = 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|Biology|border=no}}
Category:Enzymes of known structure
{{3.6-enzyme-stub}}