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Acylphosphatase

From Wikipedia, the free encyclopedia
acylphosphatase
Identifiers
EC no.3.6.1.7
CAS no.9012-34-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Acylphosphatase
Structure of acylphosphatase.[2]
Identifiers
SymbolAcylphosphatase
PfamPF00708
InterProIPR001792
PROSITEPDOC00136
SCOP21aps / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB2GV1​, 1APS​, 2FHM​, 1Y9O​, 1URR​, 1W2I​, 2ACY​, 2BJD​, 1V3Z​, 2HLT​, 2HLU​, 2BJE​, 3BR8​, 1ULR

In enzymology, an acylphosphatase (EC 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:[3]

The chemical reaction catalyzed by acylphosphatase enzymes.

Function

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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

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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

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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
Search for
StructuresSwiss-model
DomainsInterPro
acylphosphatase 2, muscle type
Identifiers
SymbolACYP2
NCBI gene98
HGNC180
OMIM102595
RefSeqNM_138448
UniProtP14621
Other data
EC number3.6.1.7
LocusChr. 2 p16.2
Search for
StructuresSwiss-model
DomainsInterPro

References

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  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. PMC 11147357. 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.