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Gene Review

glpK  -  glycerol kinase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK3918, JW3897
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Disease relevance of glpK


High impact information on glpK

  • The crystal structure at 2.6 A resolution of one of the targets, glycerol kinase (GK), in complex with unphosphorylated IIIGlc, glycerol, and adenosine diphosphate was determined [4].
  • GK contains a region that is topologically identical to the adenosine triphosphate binding domains of hexokinase, the 70-kD heat shock cognate, and actin [4].
  • The phosphorylation site of IIIGlc, His90, is buried in a hydrophobic environment formed by the active site region of IIIGlc and a 3(10) helix of GK, suggesting that phosphorylation prevents IIIGlc binding to GK by directly disrupting protein-protein interactions [4].
  • IIIGlc binds far from the catalytic site of GK, indicating that long-range conformational changes mediate the inhibition of GK by IIIGlc [4].
  • Structural and kinetic analyses show that the complex of IIIGlc with glycerol kinase creates an intermolecular Zn(II) binding site with ligation identical to that of the zinc peptidase thermolysin [5].

Chemical compound and disease context of glpK


Biological context of glpK


Associations of glpK with chemical compounds

  • Transcriptional analysis revealed that only glpK is expressed when L. rhamnosus was grown on glycerol [3].
  • Zn(II) at 0.01 and 0.1 mM decreases the Ki of IIIGlc for glycerol kinase by factors of about 15 and 60, respectively [5].
  • Mutagenesis of Arg 236 to alanine drastically reduced the extent of inhibition of GK by FBP and lowered, but did not eliminate, the ability of FBP to promote tetramer association [6].
  • The global effect of the G-304-S substitution on the conformation and catalytic and regulatory properties of glycerol kinase is consistent with a role for the domain closure motion in the molecular mechanism for glucose control of glycerol utilization [7].
  • In contrast, fructose 1,6-bisphosphate inhibition of glycerol kinase is the dominant allosteric control mechanism, and glucose is unable to control glycerol utilization in its absence [11].

Regulatory relationships of glpK


Other interactions of glpK


Analytical, diagnostic and therapeutic context of glpK


  1. Structure and regulation of the glpFK operon encoding glycerol diffusion facilitator and glycerol kinase of Escherichia coli K-12. Weissenborn, D.L., Wittekindt, N., Larson, T.J. J. Biol. Chem. (1992) [Pubmed]
  2. Cloning of the glycerol kinase gene of Bacillus subtilis. Holmberg, C., Rutberg, B. FEMS Microbiol. Lett. (1989) [Pubmed]
  3. Glycerol metabolism of Lactobacillus rhamnosus ATCC 7469: cloning and expression of two glycerol kinase genes. Alvarez, M.d.e. .F., Medina, R., Pasteris, S.E., Strasser de Saad, A.M., Sesma, F. J. Mol. Microbiol. Biotechnol. (2004) [Pubmed]
  4. Structure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinase. Hurley, J.H., Faber, H.R., Worthylake, D., Meadow, N.D., Roseman, S., Pettigrew, D.W., Remington, S.J. Science (1993) [Pubmed]
  5. Cation-promoted association of a regulatory and target protein is controlled by protein phosphorylation. Feese, M., Pettigrew, D.W., Meadow, N.D., Roseman, S., Remington, S.J. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  6. Crystal structure of a complex of Escherichia coli glycerol kinase and an allosteric effector fructose 1,6-bisphosphate. Ormö, M., Bystrom, C.E., Remington, S.J. Biochemistry (1998) [Pubmed]
  7. A single amino acid change in Escherichia coli glycerol kinase abolishes glucose control of glycerol utilization in vivo. Pettigrew, D.W., Liu, W.Z., Holmes, C., Meadow, N.D., Roseman, S. J. Bacteriol. (1996) [Pubmed]
  8. Glycerol kinase from Escherichia coli and an Ala65-->Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation. Feese, M.D., Faber, H.R., Bystrom, C.E., Pettigrew, D.W., Remington, S.J. Structure (1998) [Pubmed]
  9. Escherichia coli glycerol kinase. Cloning and sequencing of the glpK gene and the primary structure of the enzyme. Pettigrew, D.W., Ma, D.P., Conrad, C.A., Johnson, J.R. J. Biol. Chem. (1988) [Pubmed]
  10. Structure and gene-polypeptide relationships of the region encoding glycerol diffusion facilitator (glpF) and glycerol kinase (glpK) of Pseudomonas aeruginosa. Schweizer, H.P., Jump, R., Po, C. Microbiology (Reading, Engl.) (1997) [Pubmed]
  11. Reverse genetics of Escherichia coli glycerol kinase allosteric regulation and glucose control of glycerol utilization in vivo. Holtman, C.K., Pawlyk, A.C., Meadow, N.D., Pettigrew, D.W. J. Bacteriol. (2001) [Pubmed]
  12. Glycerol kinase of Escherichia coli is activated by interaction with the glycerol facilitator. Voegele, R.T., Sweet, G.D., Boos, W. J. Bacteriol. (1993) [Pubmed]
  13. Crystallization and preliminary X-ray studies of Escherichia coli glycerol kinase. Faber, H.R., Pettigrew, D.W., Remington, S.J. J. Mol. Biol. (1989) [Pubmed]
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