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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1wgi

E.C. nameinorganic diphosphatase
SpeciesSaccharomyces cerevisiae (Baker's yeast)
E.C. Number (IntEnz) 3.6.1.1
CSA Homologues of 1wgiThere are 57 Homologs
CSA Entries With UniProtID P00817
CSA Entries With EC Number 3.6.1.1
PDBe Entry 1wgi
PDBSum Entry 1wgi
MACiE Entry 1wgi

Literature Report

IntroductionSoluble inorganic pyrophosphate is present in all organisms, and is essential for cell growth. It provides an entropic pull for biosynthetic reactions involving nucleotide triphosphates by irreversibly hydrolysing the pyrophosphate product to orthophosphate. The phosphoryltransferase activity is an ancient one, and there are functional similarities between the active site of this enzyme and alkaline phosphatase and other divalent cation containing enzymes such as exonucleases and polymerases.
MechansimThe reaction mechanism is thought to proceed via a nucleophilic attack by a hydroxide ion which bridges two metal ions.
Reaction

Catalytic Sites for 1wgi

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspA117118macie:sideChain

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspB117118macie:sideChain

Literature References

Notes:
Zyryanov AB
Rates of elementary catalytic steps for different metal forms of the family II pyrophosphatase from Streptococcus gordonii.
Biochemistry 2004 43 1065-1074
PubMed: 14744152
Shizawa N
Directed mutagenesis studies of the C-terminal fingerprint region of Bacillus subtilis pyrophosphatase.
Eur J Biochem 2001 268 5771-5775
PubMed: 11722562
Halonen P
Effects of active site mutations on the metal binding affinity, catalytic competence, and stability of the family II pyrophosphatase from Bacillus subtilis.
Biochemistry 2005 44 4004-4010
PubMed: 15751976
Fabrichniy IP
Structural studies of metal ions in family II pyrophosphatases: the requirement for a Janus ion.
Biochemistry 2004 43 14403-14411
PubMed: 15533045
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