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Gene Review

AK1  -  adenylate kinase 1

Bos taurus

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Disease relevance of AK1


High impact information on AK1

  • The effects of phosphorylation by A-kinase on native neurofilaments (NF) composed of three distinct subunits: NF-L, NF-M, and NF-H, however, have not yet been described [3].
  • In this paper, we examined the effects of phosphorylation of NF proteins by A-kinase on both native and reassembled filaments containing all three NF subunits [3].
  • The active catalytic subunit of A-kinase applied intracellularly through the recording pipette failed to alter functional expression of IAC [4].
  • Adrenocorticotropic hormone and cAMP inhibit noninactivating K+ current in adrenocortical cells by an A-kinase-independent mechanism requiring ATP hydrolysis [4].
  • Neurofilament phosphatase (NF-phosphatase) activity, which dephosphorylates NF proteins phosphorylated by cyclic AMP-dependent protein kinase (A-kinase), was detected in NF fractions prepared from bovine spinal cords [5].

Biological context of AK1


Anatomical context of AK1


Associations of AK1 with chemical compounds

  • The chain folds of the adenylate kinase isoenzymes are similar again from a position corresponding to residue 115 of AK1 onwards [14].
  • These effects are very similar to those seen with cyclic AMP-dependent protein kinase (A-kinase) [15].
  • The depsipeptide that lacks a Leu6 amide proton is a good substrate for A-kinase, but the corresponding N-methylated peptide is phosphorylated far less efficiently [16].
  • As part of a search for peptides that have specificity for selected protein kinases, the possibility that adenosine cyclic 3',5'-phosphate dependent protein kinase (A-kinase) recognizes the hydrogen-bonding potential of its peptide substrates was investigated [16].
  • This result and others presented in this paper suggest that although enzyme-substrate hydrogen bonding may play some role in A-kinase catalysis of phosphoryl group transfer, other explanations are necessary to account for the relative reactivities of N alpha-methylated and depsi-containing peptide 1 analogues.(ABSTRACT TRUNCATED AT 250 WORDS)[16]

Enzymatic interactions of AK1

  • HMG 14 phosphorylated by both A-kinase and NII-kinase eluted from double-stranded DNA-columns almost identically (190 mM NaCl) with the unphosphorylated protein [17].

Other interactions of AK1

  • Bovine heart AK2 contains 44 residues more than the homologous isoenzyme AK1 (myokinase) [6].
  • With 30% of all aligned residues being identical, the homology between AK3 and AK1 is well established [18].
  • Prephosphorylation of tau by A-kinase, C-kinase, or CK-2 (but not by CK-1, CaM kinase II or Gr kinase) increased both the rate and extent of a subsequent phosphorylation catalyzed by GSK-3 by several-fold [19].
  • In one step, this technique separates the phosphorylated derivative from A-kinase, ATP, unphosphorylated HMG 14, and a minor phosphorylated by-product which evidence suggests may be the previously reported Ser 6, 24-diphospho-HMG 14 [13].
  • These results suggest that spermine may inhibit TH activity by interacting with the pterin binding site of the enzyme molecule in a manner of negative cooperativity, and that this inhibition is reversed by the conformational change of regulatory domain of TH after phosphorylation by A-kinase [20].

Analytical, diagnostic and therapeutic context of AK1


  1. Gamma-butyrobetaine hydroxylase: stereochemical course of the hydroxylation reaction. Englard, S., Blanchard, J.S., Midelfort, C.F. Biochemistry (1985) [Pubmed]
  2. Activation of type I cyclic AMP-dependent protein kinases is impaired by a point mutation in cyclic AMP binding sites. Kuno, T., Shuntoh, H., Takeda, T., Ito, A., Sakaue, M., Hirai, M., Ando, H., Tanaka, C. Eur. J. Pharmacol. (1989) [Pubmed]
  3. Phosphorylation of native and reassembled neurofilaments composed of NF-L, NF-M, and NF-H by the catalytic subunit of cAMP-dependent protein kinase. Hisanaga, S., Matsuoka, Y., Nishizawa, K., Saito, T., Inagaki, M., Hirokawa, N. Mol. Biol. Cell (1994) [Pubmed]
  4. Adrenocorticotropic hormone and cAMP inhibit noninactivating K+ current in adrenocortical cells by an A-kinase-independent mechanism requiring ATP hydrolysis. Enyeart, J.J., Mlinar, B., Enyeart, J.A. J. Gen. Physiol. (1996) [Pubmed]
  5. Neurofilament-associated protein phosphatase 2A: its possible role in preserving neurofilaments in filamentous states. Saito, T., Shima, H., Osawa, Y., Nagao, M., Hemmings, B.A., Kishimoto, T., Hisanaga, S. Biochemistry (1995) [Pubmed]
  6. Mitochondrial adenylate kinase (AK2) from bovine heart. The complete primary structure. Frank, R., Trosin, M., Tomasselli, A.G., Noda, L., Krauth-Siegel, R.L., Schirmer, R.H. Eur. J. Biochem. (1986) [Pubmed]
  7. Biochemical characterization of galloyl pedunculagin (ellagitannin) as a selective inhibitor of the beta-regulatory subunit of A-kinase in vitro. Kosuge, S., Maekawa, T., Saito, C., Tanaka, T., Kouno, I., Ohtsuki, K. J. Biochem. (2001) [Pubmed]
  8. The biological significance of glycyrrhizin- and glycyrrhetinic acid derivative-induced selective phosphorylation of histones H2A and H2B by A-kinase in vitro. Shamsa, F., Iwasa, T., Saito, H., Nagata, N., Ohtsuki, K. Tohoku J. Exp. Med. (1994) [Pubmed]
  9. Evaluation of kemptide, a synthetic serine-containing heptapeptide, as a phosphate acceptor for the estimation of cyclic AMP-dependent protein kinase activity in respiratory tissues. Giembycz, M.A., Diamond, J. Biochem. Pharmacol. (1990) [Pubmed]
  10. PKA-induced stimulation of ROMK1 channel activity is governed by both tethering and non-tethering domains of an A kinase anchor protein. Ali, S., Wei, Y., Lerea, K.M., Becker, L., Rubin, C.S., Wang, W. Cell. Physiol. Biochem. (2001) [Pubmed]
  11. The alpha 1-subunit of skeletal muscle L-type Ca channels is the key target for regulation by A-kinase and protein phosphatase-1C. Zhao, X.L., Gutierrez, L.M., Chang, C.F., Hosey, M.M. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  12. The cyclic nucleotide-dependent phosphorylation of aortic smooth muscle membrane proteins. Parks, T.P., Nairn, A.C., Greengard, P., Jamieson, J.D. Arch. Biochem. Biophys. (1987) [Pubmed]
  13. A one-step preparative method for separating SER 6-phosphorylated HMG 14 from unphosphorylated HMG 14 and in vitro phosphorylation reaction components. Bofinger, D.P., Fucile, N.W., Spaulding, S.W. Anal. Biochem. (1988) [Pubmed]
  14. Mitochondrial adenylate kinase (AK2) from bovine heart. Homology with the cytosolic isoenzyme in the catalytic region. Frank, R., Trosin, M., Tomasselli, A.G., Schulz, G.E., Schirmer, R.H. Eur. J. Biochem. (1984) [Pubmed]
  15. Cyclic GMP-dependent protein kinase phosphorylates phospholamban in isolated sarcoplasmic reticulum from cardiac and smooth muscle. Raeymaekers, L., Hofmann, F., Casteels, R. Biochem. J. (1988) [Pubmed]
  16. Role of enzyme-peptide substrate backbone hydrogen bonding in determining protein kinase substrate specificities. Thomas, N.E., Bramson, H.N., Miller, W.T., Kaiser, E.T. Biochemistry (1987) [Pubmed]
  17. Binding of high-mobility-group proteins HMG 14 and HMG 17 to DNA and histone H1 as influenced by phosphorylation. Palvimo, J., Mäenpää, P.H. Biochim. Biophys. Acta (1988) [Pubmed]
  18. The amino acid sequence of GTP:AMP phosphotransferase from beef-heart mitochondria. Extensive homology with cytosolic adenylate kinase. Wieland, B., Tomasselli, A.G., Noda, L.H., Frank, R., Schulz, G.E. Eur. J. Biochem. (1984) [Pubmed]
  19. Modulation of GSK-3-catalyzed phosphorylation of microtubule-associated protein tau by non-proline-dependent protein kinases. Singh, T.J., Zaidi, T., Grundke-Iqbal, I., Iqbal, K. FEBS Lett. (1995) [Pubmed]
  20. Effect of spermine on tyrosine hydroxylase activity before and after phosphorylation by cyclic AMP-dependent protein kinase. Kiuchi, K., Kiuchi, K., Togari, A., Nagatsu, T. Biochem. Biophys. Res. Commun. (1987) [Pubmed]
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