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. 1991 Jul 1;277(Pt 1):159–163. doi: 10.1042/bj2770159

Expression and site-directed mutagenesis of hepatic glucokinase.

A J Lange 1, L Z Xu 1, F Van Poelwijk 1, K Lin 1, D K Granner 1, S J Pilkis 1
PMCID: PMC1151205  PMID: 1854332

Abstract

Soluble rat liver glucokinase was expressed at high levels at 22 degrees C in the BL21(DE3)pLysS strain of Escherichia coli. Aspartate-211 of yeast hexokinase has been implicated as a catalytic residue from crystallographic data. The corresponding residue in rat liver glucokinase, aspartate-205, was mutated to alanine and the expressed mutant had 1/500th of the activity of the wild type, with no change in the Km values for glucose or ATP. The results support a role for this residue as a base catalyst in the glucokinase reaction and, most probably, a similar role in the reactions of all members of the hexokinase family.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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