Structure/function studies of human beta-cell glucokinase. Enzymatic properties of a sequence polymorphism, mutations associated with diabetes, and other site-directed mutants-Reference-Cited by-同舟云学术

Structure/function studies of human beta-cell glucokinase. Enzymatic properties of a sequence polymorphism, mutations associated with diabetes, and other site-directed mutants

Published:1993-07 Issue:20 Volume:268 Page:15200-15204
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Takeda J.,Gidh-Jain M.,Xu L.Z.,Froguel P.,Velho G.,Vaxillaire M.,Cohen D.,Shimada F.,Makino H.,Nishi S.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference27 articles.

1. Regulation of Glucokinase in Liver* *This review will be limited in scope to only the high Km glucose–ATP phosphotransferase found in liver of many animal species, and will dwell mainly on regulatory aspects. For a broader perspective on other hexokinase types, the reader is referred to the comprehensive review by Walker (165). Further material will be found in a recent review by Ureta (155a) on the phylogeny and ontogenesis of vertebrate hexokinase.

2. Pancreatic islet glucose metabolism and regulation of insulin secretion

3. The genes of hepatic glucose metabolism.

4. Nonsense mutation in the glucokinase gene causes early-onset non-insulin-dependent diabetes mellitus

5. Human glucokinase gene: isolation, characterization, and identification of two missense mutations linked to early-onset non-insulin-dependent (type 2) diabetes mellitus.

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