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Gene Review

adk  -  adenylate kinase

Escherichia coli O157:H7 str. EDL933

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Disease relevance of adk


High impact information on adk


Chemical compound and disease context of adk


Biological context of adk


Anatomical context of adk


Associations of adk with chemical compounds

  • From five independently isolated strains analysed, two contain a CCG to TCG transition changing proline 87 to serine (P87S), another two have a TCT to TTT transition that mutates serine 129 to phenylalanine (S129F), and the last one was found not to contain a mutation in the adk gene [20].
  • Replacement of arginine-88 of adk with glycine resulted in the loss of enzymic activity [21].
  • Adenosine diphosphopyridoxal, which specifically modifies Lys-21 in adenylate kinase (Tagaya, M., Yagami, T., and Fukui, T. (1987) J. Biol. Chem. 262, 8257-8261), inactivated the wild-type and mutant enzymes at almost the same rates [22].
  • Norleucine-substituted adenylate kinase shows structural and catalytic properties similar to the wild-type protein as indicated by circular dichroism spectroscopy and kinetic experiments but exhibits a much higher resistance to hydrogen peroxide inactivation under denaturing conditions [12].
  • When mixed, C1 and C2 fragments reassociated into structures resembling native, uncleaved adenylate kinase [23].

Other interactions of adk


Analytical, diagnostic and therapeutic context of adk


  1. Identification and purification of an adenylate kinase-associated protein that influences the thermolability of adenylate kinase from a temperature-sensitive adk mutant of Escherichia coli. Huss, R.J., Glaser, M. J. Biol. Chem. (1983) [Pubmed]
  2. Zinc, a novel structural element found in the family of bacterial adenylate kinases. Glaser, P., Presecan, E., Delepierre, M., Surewicz, W.K., Mantsch, H.H., Bârzu, O., Gilles, A.M. Biochemistry (1992) [Pubmed]
  3. Structural and physico-chemical characteristics of Bordetella pertussis adenylate kinase, a tryptophan-containing enzyme. Gilles, A.M., Sismeiro, O., Munier, H., Fabian, H., Mantsch, H.H., Surewicz, W.K., Craescu, C.C., Barzu, O., Danchin, A. Eur. J. Biochem. (1993) [Pubmed]
  4. Cloning and sequencing of the secY gene homolog from Mycobacterium bovis BCG. Kim, J.K., Kim, J.H., Kim, S.J., Bai, G.H., Cho, S.H., Kang, S.W., Kim, Y.S., Kim, J.W., Lee, Y., Lim, J.S., Lee, H.G., Choe, I.S., Chung, T.W., Park, S.N., Ahn, J.S., Choe, Y.K. Biochem. Mol. Biol. Int. (1997) [Pubmed]
  5. Adenylate kinase of Escherichia coli, a component of the phage T4 dNTP synthetase complex. Kim, J., Shen, R., Olcott, M.C., Rajagopal, I., Mathews, C.K. J. Biol. Chem. (2005) [Pubmed]
  6. Genetically engineered zinc-chelating adenylate kinase from Escherichia coli with enhanced thermal stability. Perrier, V., Burlacu-Miron, S., Bourgeois, S., Surewicz, W.K., Gilles, A.M. J. Biol. Chem. (1998) [Pubmed]
  7. Primary structural constraints of P-loop of mitochondrial F1-ATPase from yeast. Shen, H., Yao, B.Y., Mueller, D.M. J. Biol. Chem. (1994) [Pubmed]
  8. Molecular analysis of the essential gene for adenylate kinase from the fission yeast Schizosaccharomyces pombe. Konrad, M. J. Biol. Chem. (1993) [Pubmed]
  9. Structural and catalytic properties of a deletion derivative (delta 133-157) of Escherichia coli adenylate kinase. Rose, T., Brune, M., Wittinghofer, A., Le Blay, K., Surewicz, W.K., Mantsch, H.H., Bârzu, O., Gilles, A.M. J. Biol. Chem. (1991) [Pubmed]
  10. Structural and catalytic characteristics of Escherichia coli adenylate kinase. Saint Girons, I., Gilles, A.M., Margarita, D., Michelson, S., Monnot, M., Fermandjian, S., Danchin, A., Bârzu, O. J. Biol. Chem. (1987) [Pubmed]
  11. Structural and catalytic role of arginine 88 in Escherichia coli adenylate kinase as evidenced by chemical modification and site-directed mutagenesis. Reinstein, J., Gilles, A.M., Rose, T., Wittinghofer, A., Saint Girons, I., Bârzu, O., Surewicz, W.K., Mantsch, H.H. J. Biol. Chem. (1989) [Pubmed]
  12. Conservative replacement of methionine by norleucine in Escherichia coli adenylate kinase. Gilles, A.M., Marlière, P., Rose, T., Sarfati, R., Longin, R., Meier, A., Fermandjian, S., Monnot, M., Cohen, G.N., Bârzu, O. J. Biol. Chem. (1988) [Pubmed]
  13. Spectinomycin operon of Micrococcus luteus: evolutionary implications of organization and novel codon usage. Ohama, T., Muto, A., Osawa, S. J. Mol. Evol. (1989) [Pubmed]
  14. The Escherichia coli dnaW mutation is an allele of the adk gene. Henson, J.M., Blinkowa, A., Walker, J.R. Mol. Gen. Genet. (1982) [Pubmed]
  15. Use of helper enzymes for ADP removal in infrared spectroscopic experiments: application to Ca2+-ATPase. Liu, M., Karjalainen, E.L., Barth, A. Biophys. J. (2005) [Pubmed]
  16. The chaperone activity of trigger factor is distinct from its isomerase activity during co-expression with adenylate kinase in Escherichia coli. Li, Z.Y., Liu, C.P., Zhu, L.Q., Jing, G.Z., Zhou, J.M. FEBS Lett. (2001) [Pubmed]
  17. Biochemical properties of rice adenylate kinase and subcellular location in plant cells. Kawai, M., Uchimiya, H. Plant Mol. Biol. (1995) [Pubmed]
  18. Evidence for in vivo synthesis of thiamin triphosphate by cytosolic adenylate kinase in chicken skeletal muscle. Miyoshi, K., Egi, Y., Shioda, T., Kawasaki, T. J. Biochem. (1990) [Pubmed]
  19. An expanded adenylate kinase gene family in the protozoan parasite Trypanosoma cruzi. Bouvier, L.A., Miranda, M.R., Canepa, G.E., Alves, M.J., Pereira, C.A. Biochim. Biophys. Acta (2006) [Pubmed]
  20. Adenylate kinases from thermosensitive Escherichia coli strains. Haase, G.H., Brune, M., Reinstein, J., Pai, E.F., Pingoud, A., Wittinghofer, A. J. Mol. Biol. (1989) [Pubmed]
  21. Nucleoside diphosphate kinase-like activity in adenylate kinase of Mycobacterium tuberculosis. Meena, L.S., Chopra, P., Bedwal, R.S., Singh, Y. Biotechnol. Appl. Biochem. (2003) [Pubmed]
  22. Site-directed mutagenesis of Pro-17 located in the glycine-rich region of adenylate kinase. Tagaya, M., Yagami, T., Noumi, T., Futai, M., Kishi, F., Nakazawa, A., Fukui, T. J. Biol. Chem. (1989) [Pubmed]
  23. Circular dichroism investigation of Escherichia coli adenylate kinase. Monnot, M., Gilles, A.M., Girons, I.S., Michelson, S., Bârzu, O., Fermandjian, S. J. Biol. Chem. (1987) [Pubmed]
  24. Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new structural family with the P-loop nucleoside triphosphate hydrolase fold. Matte, A., Goldie, H., Sweet, R.M., Delbaere, L.T. J. Mol. Biol. (1996) [Pubmed]
  25. Zinc chelation and structural stability of adenylate kinase from Bacillus subtilis. Perrier, V., Surewicz, W.K., Glaser, P., Martineau, L., Craescu, C.T., Fabian, H., Mantsch, H.H., Bârzu, O., Gilles, A.M. Biochemistry (1994) [Pubmed]
  26. Structural and functional consequences of amino acid substitutions in the second conserved loop of Escherichia coli adenylate kinase. Rose, T., Glaser, P., Surewicz, W.K., Mantsch, H.H., Reinstein, J., Le Blay, K., Gilles, A.M., Bârzu, O. J. Biol. Chem. (1991) [Pubmed]
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