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Gene Review

glk  -  glucokinase

Escherichia coli UTI89

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Disease relevance of glk


High impact information on glk


Chemical compound and disease context of glk


Biological context of glk

  • In hepatocytes, GKA1 and GKA2 stimulated glucose phosphorylation, glycolysis, and glycogen synthesis to a similar extent as sorbitol, a precursor of fructose 1-phosphate, which indirectly activates GK through promoting its dissociation from GKRP [5].
  • Using the N-terminal amino acid sequence of the previously purified ADP-dependent glucokinase, the corresponding gene as well as a related open reading frame were detected in the genome of P. furiosus [10].
  • Taken together, these results illustrate that the MODY-2 phenotype may be linked not only to kinetic alterations but also to the regulation of GK activity [6].
  • To determine whether differences in protein structure brought about by alternative RNA splicing have an effect on glucose phosphorylating activity, we expressed cDNAs encoding four different hepatic and islet glucokinase isoforms and determined the Km and Vmax of each [11].
  • These missense mutations were shown to have variable effects on GK kinetic activity [6].

Anatomical context of glk


Associations of glk with chemical compounds


Other interactions of glk

  • The induced protein identified as glucokinase (EC is produced at a level > or = 20-fold higher than the level in wild-type E. coli when foreign proteins are expressed under the control of the alkaline phosphatase (phoA) promoter [16].

Analytical, diagnostic and therapeutic context of glk

  • Messenger RNAs encoding both the B2 and L2 isoforms of glucokinase were detected in islet and liver by polymerase chain reaction amplification of total cDNA, indicating that mRNAs utilizing this weak alternate splice acceptor site in the fourth exon are normally present in both the liver and islet but as minor components [11].


  1. Bacillus subtilis GlcK activity requires cysteines within a motif that discriminates microbial glucokinases into two lineages. Mesak, L.R., Mesak, F.M., Dahl, M.K. BMC Microbiol. (2004) [Pubmed]
  2. The crystal structure of Mlc, a global regulator of sugar metabolism in Escherichia coli. Schiefner, A., Gerber, K., Seitz, S., Welte, W., Diederichs, K., Boos, W. J. Biol. Chem. (2005) [Pubmed]
  3. Characterization of the Zymomonas mobilis glucose facilitator gene product (glf) in recombinant Escherichia coli: examination of transport mechanism, kinetics and the role of glucokinase in glucose transport. Parker, C., Barnell, W.O., Snoep, J.L., Ingram, L.O., Conway, T. Mol. Microbiol. (1995) [Pubmed]
  4. ATP-dependent glucokinase from the hyperthermophilic bacterium Thermotoga maritima represents an extremely thermophilic ROK glucokinase with high substrate specificity. Hansen, T., Schönheit, P. FEMS Microbiol. Lett. (2003) [Pubmed]
  5. Stimulation of hepatocyte glucose metabolism by novel small molecule glucokinase activators. Brocklehurst, K.J., Payne, V.A., Davies, R.A., Carroll, D., Vertigan, H.L., Wightman, H.J., Aiston, S., Waddell, I.D., Leighton, B., Coghlan, M.P., Agius, L. Diabetes (2004) [Pubmed]
  6. Characterization of glucokinase mutations associated with maturity-onset diabetes of the young type 2 (MODY-2): different glucokinase defects lead to a common phenotype. Miller, S.P., Anand, G.R., Karschnia, E.J., Bell, G.I., LaPorte, D.C., Lange, A.J. Diabetes (1999) [Pubmed]
  7. Crystal structures of Escherichia coli ATP-dependent glucokinase and its complex with glucose. Lunin, V.V., Li, Y., Schrag, J.D., Iannuzzi, P., Cygler, M., Matte, A. J. Bacteriol. (2004) [Pubmed]
  8. Unique phylogenetic relationships of glucokinase and glucosephosphate isomerase of the amitochondriate eukaryotes Giardia intestinalis, Spironucleus barkhanus and Trichomonas vaginalis. Henze, K., Horner, D.S., Suguri, S., Moore, D.V., Sánchez, L.B., Müller, M., Embley, T.M. Gene (2001) [Pubmed]
  9. Mutations that confer resistance to 2-deoxyglucose reduce the specific activity of hexokinase from Myxococcus xanthus. Youderian, P., Lawes, M.C., Creighton, C., Cook, J.C., Saier, M.H. J. Bacteriol. (1999) [Pubmed]
  10. Molecular and biochemical characterization of the ADP-dependent phosphofructokinase from the hyperthermophilic archaeon Pyrococcus furiosus. Tuininga, J.E., Verhees, C.H., van der Oost, J., Kengen, S.W., Stams, A.J., de Vos, W.M. J. Biol. Chem. (1999) [Pubmed]
  11. Effects of alternate RNA splicing on glucokinase isoform activities in the pancreatic islet, liver, and pituitary. Liang, Y., Jetton, T.L., Zimmerman, E.C., Najafi, H., Matschinsky, F.M., Magnuson, M.A. J. Biol. Chem. (1991) [Pubmed]
  12. Alteration of enzyme function of the type II hexokinase C-terminal half on replacements of restricted regions by corresponding regions of glucokinase. Kogure, K., Yamamoto, K., Majima, E., Shinohara, Y., Yamashita, K., Terada, H. J. Biol. Chem. (1996) [Pubmed]
  13. Structure of yeast glucokinase, a strongly diverged specific aldo-hexose-phosphorylating isoenzyme. Albig, W., Entian, K.D. Gene (1988) [Pubmed]
  14. Engineering of carbon distribution between glycolysis and sugar nucleotide biosynthesis in Lactococcus lactis. Boels, I.C., Kleerebezem, M., de Vos, W.M. Appl. Environ. Microbiol. (2003) [Pubmed]
  15. Two genes for carbohydrate catabolism are divergently transcribed from a region of DNA containing the hexC locus in Pseudomonas aeruginosa PAO1. Temple, L., Sage, A., Christie, G.E., Phibbs, P.V. J. Bacteriol. (1994) [Pubmed]
  16. Glucokinase of Escherichia coli: induction in response to the stress of overexpressing foreign proteins. Arora, K.K., Pedersen, P.L. Arch. Biochem. Biophys. (1995) [Pubmed]
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