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CSA entry for 1q18
Original Entry
Title:
Transferase
Compound:
Glucokinase
Mutant:
No
UniProt/Swiss-Prot:
P46880-GLK_ECOLI
EC Class:
2.7.1.2
Other CSA Entries:
Overview of all sites for 1q18
Homologues of 1q18
Entries for UniProt/Swiss-Prot: P46880
Entries for EC: 2.7.1.2
Other Databases:
PDB entry: 1q18
PDBsum entry: 1q18
UniProt/Swiss-Prot: P46880
IntEnz entry: 2.7.1.2
Literature Report:
Introduction:
E. 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.
Mechanism:
Asp 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.
Sites:

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Found by:
Literature reference 

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
ASPA 100 100Sidechain
Acid/baseSubstrate
Acts as a general base to abstract proton from O6 hydroxyl group of glucose.
Evidence from paper Evidence concerns Evidence type
PubMed ID 15466045 Current protein Residue is positioned appropriately (ligand position known)
PubMed ID 15466045 Current protein Conservation of residue
PubMed ID 15466045 Related protein: UniProt P19367 Mutagenesis of residue
References:
1
Crystal structures of Escherichia coli ATP-dependent glucokinase and its complex with glucose.
V. V. Lunin and Y. Li and J. D. Schrag and P. Iannuzzi and M. Cygler and A. Matte
J Bacteriol 186, (20) 6915-27, (2004).
15466045
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