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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1snz

E.C. namealdose 1-epimerase
SpeciesHomo sapiens (Human)
E.C. Number (IntEnz) 5.1.3.3
CSA Homologues of 1snz
CSA Entries With UniProtID Q96C23
CSA Entries With EC Number 5.1.3.3
PDBe Entry 1snz
PDBSum Entry 1snz
MACiE Entry M0351

Literature Report

IntroductionHuman galactose mutarotase catalyses the interconversion of alpha- and beta-D-glucose. The epimerisation of beta-D-glucose into alpha-D-glucose is the first of four steps in the Leloir pathway. The net result of the pathway is the conversion of beta-D-galactose into alpha-D-glucose-1-phosphate.
The enzyme shows an approximately four-fold preference for galactose over gulcose.
MechansimSimultaneous protonation of the oxygen ring by His176 and deprotonation of the hydroxyl attached to carbon-1 by Glu307 results in ring opening. Reversal of these protonation events results in ring closure and reversal of configuration about carbon-1.
Reaction

Catalytic Sites for 1snz

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
HisA176176macie:sideChainPositioned within 2.8 angstroms of the ring oxygen and may serve as the catalytic acid in the first step.
GluA307307macie:sideChainPositioned within 2.8 angstroms of the 1-hydroxyl group of galactose and may serve as the catalytic base in the first step.

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
HisB176176macie:sideChainPositioned within 2.8 angstroms of the ring oxygen and may serve as the catalytic acid in the first step.
GluB307307macie:sideChainPositioned within 2.8 angstroms of the 1-hydroxyl group of galactose and may serve as the catalytic base in the first step.

Literature References

Notes:
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