ArticleDiabetologia1996
Effect of mutations on the sensitivity of human beta-cell glucokinase to liver regulatory protein.
Article in Diabetologia, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 41 citations in OpenAlex.
- Phenotypic Characterization of Congenital Hyperinsulinism Due to Novel Activating Glucokinase Mutations.Diabetes · 2023Article
- Prevalence ofJournal of obesity · 2023Article
- Glucokinase regulatory protein: complexity at the crossroads of triglyceride and glucose metabolism.Current opinion in lipidology · 2015Review
- Article
- Mutational analysis of allosteric activation and inhibition of glucokinase.The Biochemical journal · 2011Article
- GCKR gene functional variants in type 2 diabetes and metabolic syndrome: do the rare variants associate with increased carotid intima-media thickness?Cardiovascular diabetology · 2010Article
- The P446L variant in GCKR associated with fasting plasma glucose and triglyceride levels exerts its effect through increased glucokinase activity in liver.Human molecular genetics · 2009Article
- Functional analysis of human glucokinase gene mutations causing MODY2: exploring the regulatory mechanisms of glucokinase activity.Diabetologia · 2007Article
- Effects of novel maturity-onset diabetes of the young (MODY)-associated mutations on glucokinase activity and protein stability.The Biochemical journal · 2006Article
- Differences in regulatory properties between human and rat glucokinase regulatory protein.The Biochemical journal · 2004Article
- Glucokinase and glucokinase regulatory protein: mutual dependence for nuclear localization.The Biochemical journal · 2000Article
- Investigation on the mechanism by which fructose, hexitols and other compounds regulate the translocation of glucokinase in rat hepatocytes.The Biochemical journal · 1997Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human beta-cell glucokinase and its liver counterpart displayed a half-saturating concentration of glucose (S0.5) of about 8 mmol/l and a Hill coefficient of 1.7, and were as sensitive to inhibition by the rat liver regulatory protein as the rat liver enzyme. These results indicate that the N-terminal region of glucokinase, which differs among these three enzymes, is not implicated in the recognition of the regulatory protein. They also suggest that the regulatory protein, or a related protein, could modulate the affinity of glucokinase for glucose in beta cells. We have also tested the effect of several mutations, many of which are implicated in maturity onset diabetes of the young. The mutations affected the affinity for glucose and for the regulatory protein to different degrees, indicating that the binding site for these molecules is different. An Asp158 Ala mutation, found in the expression plasmid previously thought to encode the wild-type enzyme, increased the affinity for glucose by about 2.5-fold without changing the affinity for the regulatory protein. The mutations that were found to decrease the affinity for the regulatory protein (Asn166 Arg. Val203 Ala, Asn204 Gln, Lys414 Ala) clustered in the hinge region of glucokinase and nearby in the large and small domains. These results are in agreement with the concept that part of the binding site for the regulatory protein is situated in the hinge region of this enzyme.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.