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Catalytic Site Atlas

CSA LITERATURE entry for 1mqw

E.C. nameADP-ribose diphosphatase
SpeciesMycobacterium tuberculosis (Bacteria)
E.C. Number (IntEnz) 3.6.1.13
CSA Homologues of 1mqwThere are 28 Homologs
CSA Entries With UniProtID
CSA Entries With EC Number 3.6.1.13
PDBe Entry 1mqw
PDBSum Entry 1mqw
MACiE Entry 1mqw

Literature Report

IntroductionThe ADP-ribose-specific Nudix hydrolase from M. tuberculosis (MT-ADPRase or ADPR pyrophosphatase) is part of the family of Nudix hydrolases with the characteristic Nudix box that catalyse hydrolysis of nucleoside diphosphate derivatives. Divalent magnesium or manganese ions are required for activity.
Differences in binding sites of the M. tuberculosis enzyme and the human homologue suggest a possible target for antituberculosis drug treatment.
MechansimGlu 142, activated by a metal ion, acts as a general base catalyst in activating a water molecule for nucleophilic attack on the alpha-phosphate of the substrate. the water is also activated by binding to two manganese ions. The charges in the alpha-phosphate are stabilised by the metal ions. Charges in the beta-phosphate are stabilised by a metal ion and the Arg 64 side-chain.
Reaction

Catalytic Sites for 1mqw

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
GluA142142macie:sideChainActs as a general base catalyst to deprotonate the water molecule thus activating it as a nucleophile.
ArgA6464macie:sideChainActivates the substrate and stabilises the transition state.

Literature References

Notes:
Kang LW
Structure and mechanism of MT-ADPRase, a nudix hydrolase from Mycobacterium tuberculosis.
Structure 2003 11 1015-1023
PubMed: 12906832
Gabelli SB
Mechanism of the Escherichia coli ADP-ribose pyrophosphatase, a Nudix hydrolase.
Biochemistry 2002 41 9279-9285
PubMed: 12135348
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