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Search The CSA
PDB ID
UNIPROT ID
EC Number

Catalytic Site Atlas

CSA LITERATURE entry for 1q18

E.C. nameglucokinase
SpeciesEscherichia coli (Bacteria)
E.C. Number (IntEnz) 2.7.1.2
CSA Homologues of 1q18There are 19 Homologs
CSA Entries With UniProtID P0A6V9
CSA Entries With EC Number 2.7.1.2
PDBe Entry 1q18
PDBSum Entry 1q18
MACiE Entry 1q18

Literature Report

IntroductionE. coli glucokinase is a cytoplasmic enzyme that uses ATP to phosphorylate glucose imported into the cell to glucose 6-phosphate. It is classified as a glucokinase (EC 2.7.1.2) rather than a hexokinase (EC 2.7.1.1) on the basis of its substrate specificity: the enzyme shows much greater activity with glucose than with either mannose or galactose, and no activity with fructose.
MechansimAsp 100 acts as a general base to remove a proton from the O6 hydroxyl group of glucose, which can then attack the gamma phosphous of ATP.
Reaction

Catalytic Sites for 1q18

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspA100100macie:sideChainActs as a general base to abstract proton from O6 hydroxyl group of glucose.

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspB100100macie:sideChainActs as a general base to abstract proton from O6 hydroxyl group of glucose.

Literature References

Notes:
Lunin VV
Crystal structures of Escherichia coli ATP-dependent glucokinase and its complex with glucose.
J Bacteriol 2004 186 6915-6927
PubMed: 15466045
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