Characterization of Glucokinase Catalysis from a Pseudo-Dimeric View.

Abstract

Glucose phosphorylation by glucokinase exhibits a sigmoidal dependency on substrate concentration regardless of its simple structure. Dimorph mechanism suggested the existence of two enzymatic states with different catalytic properties, which has been shown to be plausible by structural analysis. However, the dimorph mechanism gives rise to a complicated or non-explicit non-closed mathematical form. It is neither feasible to apply the dimorph mechanism in effector characterizations. To improve the area of glucokinase study with stronger theoretical support and less complication in computation, we proposed the investigation of the enzyme from a pseudo-dimeric angle. The proposed mechanism started from the idealization of two monomeric glucokinase as a dimeric complex, which significantly simplified the glucose phosphorylation kinetics, while the differences in enzyme reconfiguration caused by variable substrates and effectors have been successfully characterized. The study presented a simpler and more reliable way in studying the properties of glucokinase and its effectors, providing guidelines of effector developments for hyperglycemia and hypoglycemia treatment.

• Authors: Hanchi Chen, Xiaoqing Cai, Anjie Xu, Linjiang Zhu, Yuele Lu, Xiaolong Chen, Shijie Liu
• Journal: Applied biochemistry and biotechnology (Appl Biochem Biotechnol) Vol. 189 Issue 2 Pg. 345-358 (Oct 2019) ISSN: 1559-0291 [Electronic] United States
• PMID: 31011989 (Publication Type: Journal Article)

Chemical References

• Glucokinase
• Glucose

Topics

• Catalysis
• Glucokinase (chemistry)
• Glucose (chemistry)
• Humans
• Models, Chemical
• Phosphorylation
• Protein Multimerization