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Research Article

Irreversible inhibition of aldolase by a phosphorylated α-dicarbonyl compound

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Pages 21-27 | Received 13 Feb 2007, Accepted 08 Mar 2007, Published online: 04 Oct 2008

References

  • Lundblad RL. The modification of arginine. Chemical reagents for protein modification2nd ed. CRC Press. 1991; 173–213
  • Takahashi K. The reaction of phenylglyoxal with arginine residues in proteins. J Biol Chem 1968; 243: 6171–6179
  • Yamasaki RB, Vega A, Feeney RE. Modification of available arginine residues in proteins by p-Hydroxyphenylglyoxal. Anal Biochem 1980; 109: 32–40
  • Borders CL, Jr, Pearson LJ, McLaughlin AE, Gustafson ME, Vasiloff J, An FY, Morgan DJ. 4-Hydroxy-3-nitrophenylglyoxal. A chromophoric reagent for arginyl residues in proteins. Biochim Biophys Acta 1979; 568: 491–495
  • Yankeelov JA, Jr, Mitchell CD, Crawford TH. A simple trimerization of 2,3-butanedione yielding a selective reagent for the modification of arginine in proteins. J Am Chem Soc 1968; 90: 1664–1666
  • Toi K, Bynum E, Norris E, Itano HA. Studies on the chemical modification of arginine. I. The reaction of 1,2-cyclohexanedione with arginine and arginyl residues of proteins. J Biol Chem 1967; 242: 1036–1043
  • Takahashi K. Further studies on the reactions of phenylglyoxal and related reagents with proteins. J Biochem (Tokyo) 1977; 81: 403–414
  • Chaplin MF. The use of ninhydrin as a reagent for the reversible modification of arginine residues in proteins. Biochem J 1976; 155: 457–459
  • Honegger A, Hughes GJ, Wilson KJ. Chemical modification of peptides by hydrazine. Biochem J 1981; 199: 53–59
  • Riordan JF. Functional arginyl residues in carboxypeptidase A. Modification with butanedione. Biochemistry 1973; 12: 3915–3923
  • Patthy L, Smith EL. Reversible modification of arginine residues. Application to sequence studies by restriction of tryptic hydrolysis to lysine residues. J Biol Chem 1975; 250: 557–564
  • Lobb RR, Stokes AM, Hill HA, Riordan JF. A functional arginine residue in rabbit-muscle aldolase. Eur J Biochem 1976; 70: 517–522
  • Patthy L, Varadi A, Thesz J, Kovacs K. Identification of the C-1-phosphate-binding arginine residue of rabbit-muscle aldolase. Isolation of 1,2-cyclohexanedione-labeled peptide by chemisorption chromatography. Eur J Biochem 1979; 99: 309–313
  • Vlahos CJ, Ghalambor MA, Dekker EE. Evidence for an essential arginine residue in the active site of Escherichia coli 2-keto-4-hydroxyglutarate aldolase. Modification with 1,2-cyclohexanedione. J Biol Chem 1985; 260: 5480–5485
  • Ogata H, Takeo K, Kuwahara A, Suzuno R, Fujimoto M, Shimizu J. An exploration of the binding site of aldolase using alkanediol monoglycolate bisphosphoric esters. Biochim Biophys Acta 1983; 742: 384–390
  • Patthy L, Thesz J. Origin of the selectivity of alpha-dicarbonyl reagents for arginyl residues of anion-binding sites. Eur J Biochem 1980; 105: 387–393
  • Lakhdar-Ghazal F, Blonski C, Willson M, Michels P, Perie J. Glycolysis and proteases as targets for the design of new anti-trypanosome drugs. Curr Top Med Chem 2002; 2: 439–456
  • Racker E. Spectrophotometric measurement of hexokinase and phosphohexokinase activity. J Biol Chem 1947; 167: 843–854
  • Marklund S, Marklund G. Involvement of the superoxide anion radical in the autoxidation of pyrogallol and a convenient assay for superoxide dismutase. Eur J Biochem 1974; 47: 469–474
  • Gefflaut T, Blonski C, Perie J. Slow reversible inhibitions of rabbit muscle aldolase with substrate analogues: Synthesis, enzymatic kinetics and UV difference spectroscopy studies. Bioorg Med Chem 1996; 4: 2043–2054
  • Blonski C, Gefflaut T, Perie J. Effects of chirality and substituents at carbon 3 in dihydroxyacetone-phosphate analogues on their binding to rabbit muscle aldolase. Bioorg Med Chem 1995; 3: 1247–1253
  • Hajra AK, Agranoff BW. Acyl dihydroxyacetone phosphate. Characterization of a 32P-labeled lipid from guinea pig liver mitochondria. J Biol Chem 1968; 243: 1617–1622
  • Blom N, Sygusch J. Product binding and role of the C-terminal region in class I D-fructose 1,6-bisphosphate aldolase. Nat Struct Biol 1997; 4: 36–39
  • Polticelli F, Bottaro G, Battistoni A, Carri MT, Djinovic-Carugo K, Bolognesi M, O'Neill P, Rotilio G, Desideri A. Modulation of the catalytic rate of Cu,Zn superoxide dismutase in single and double mutants of conserved positively and negatively charged residues. Biochemistry 1995; 34: 6043–6049

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