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1998 | 45 | 4 |

Tytuł artykułu

Chemical modification of lysine and arginine residues of bovine heart 2-oxoglutarate dehydrogenase: Effect on the enzyme activity and regulation

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Chemical modification of arginine and lysine residues of bovine heart 2-oxoglutarate dehydrogenase with phenylglyoxal and pyridoxal 5'-phosphate inactivated the enzyme, indicating the importance of these residues for the catalysis. Inactivation caused by pyridoxal 5'-phosphate was prevented in the presence of thiamine pyrophosphate and Mg2+ allowing the assumption that lysine residues participate in binding of the cofactor.

Wydawca

-

Rocznik

Tom

45

Numer

4

Opis fizyczny

p.1031-1036,fig.

Twórcy

  • National Academy of Sciences of Belarus, BLK-50, 230009 Grodno, Belarus

Bibliografia

  • 1. Cooney, G.J., Taegtmeyer, H. & Newsholme, E.A. (1981) Tricarboxylic acid cycle flux and enzyme activities in the isolated rat heart. Bio- chem. J. 200, 701-703.
  • 2. Riordan, J.F. (1979) Arginyl residues and an­ion binding sites in proteins. Mol. Celi Bio- chem. 26, 71-92.
  • 3. Gomazkova, V.S., Stafeeva, O.A. & Severin, S.E. (1981) The role of arginine residues in the functioning of cr-ketoglutarate dehydroge­nase from pigeon breast muscle. Biochem. In­ternat 2, 51-57.
  • 4. Ali, M.S., Roche, T.E. & Patel, M.S. (1993) Identification of the essential cysteine residue in the active site of bovine pyruvate dehydro­genase. J. BioL Chem. 268, 22353-22356.
  • 5. Gomazkova, V.S. & Krasovskaja, O.E. (1979) Regulation of a-ketoglutarate dehydrogenase complex from pigeon breast muscle. Bio- khimiya, 44, 1126-1136 (in Russian).
  • 6. Valinger, Z., Engel, P.C. & Metzler, D.E. (1993) Is pyridoxal S'-phosphate an affinity la­bel for phosphate-binding sites in protein: The case of bovine glutamate dehydrogenase. Bio­chem. J. 294, 835-839.
  • 7. Gnatenko, D.V., Kornelyuk, A.L. & Lavrik, O.I. (1991) Chemical modification of lysine residues of tyrosyl-t-RNA synthetase from bo­vine liver by pyridoxal 5'-phosphate. Bio- khimiya 56, 1984-1990 (in Russian).
  • 8. Stafeeva, OA., Gomazkova, V.S. & Severin, S.E. (1983) Essential arginine residues for catalytic and regulatory functions of tt-keto-glutarate dehydrogenase from pigeon breast muscle. Biochem. InternaL 6, 315-321.
  • 9. Stenley, C.J. & Perham, R.N. (1980) Purifica­tion of 2-oxo acid dehydrogenase multienzyme complexes from ox heart by a new method. Biochem. J. 191, 147-154.
  • 10. Severin, S.E. & Gomazkova, V.S. (1971) Puri­fication and resolution of pigeon breast a-ket­oglutarate dehydrogenase complex. Biokhi- miya 36, 1099-1106 (in Russian).
  • 11. Berezin, I.V. & Klyosov, A.A. (1976) The Prac­tical Course of Chemical and Enzyme Kinetics. Moscow University Edition, Moscow (in Rus­sian).
  • 12. Keleti, T. (1986) Basic Enzyme Kinetics. Aka- demiai Kiado, Budapest.
  • 13. MyUyla, R., Giinzler, V., Kivirikko, K.I. & Kaska, D.D. (1992) Modification of vertebrate and algal prolyl 4-hydroxylases and vertebrate lysyl hydroxylase by diethyl pyrocarbonate. Biochem. J. 286, 923-927.
  • 14. Ostrovtsova, S.A. (1996) Inhibition of 2-oxo- glutarate dehydrogenase complex by free fatty acids. Med. Set Res. 24, 625-627.
  • 15.Schellenberger, A. (1996) Problems in the un­derstanding of thiamin-pyrophosphate en­zymes; in Biochemistry and Physiology of Thia­min Diphosphate Enzymes (Bisswanger, H. & Schellenberger, A., eds.) pp. 3-18, A. u. C. In- temann, Wissenschaftlicher Verlag, Prien.
  • 16.Bunik, V.I., Buneeva, O.A. & Gomazkova, V.S. (1990) Change in a-ketoglutarate dehydroge­nase co-operative properties due to dihydroli- poate and NADH. FEBS Lett. 269, 252-254.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

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