Activation of the anaerobic ribonucleotide reductase from Escherichia coli by S-adenosylmethionine.
作者： J Harder , R Eliasson , E Pontis , M.D. Ballinger , P Reichard
DOI: 10.1016/S0021-9258(19)74075-7
关键词:
摘要: The anaerobic ribonucleoside triphosphate reductase from Escherichia coli reduces CTP to dCTP in the presence of a second protein, named dA1, and Chelex-treated boiled extract bacteria, RT. reaction requires S-adenosylmethionine, NADPH, dithiothreitol, ATP, Mg2+ K+ ions. It occurs only under conditions. We now show that overall two steps. first is an activation by dA1 RT possibly In step, activated with ATP acting as allosteric effector. During activation, S-adenosylmethionine cleaved reductively methionine + 5'-deoxyadenosine. This step inhibited strongly S-adenosylhomocysteine various chelators. shows considerable similarity pyruvate formate-lyase (Knappe, J., Neugebauer, F. A., Blaschkowski, H. P., Ganzler, M. (1984) Proc. Natl. Acad. Sci. U.S.A. 81, 1332-1335).
sci-hub.st 参考文章(17)
R Eliasson, E Pontis, M Fontecave, C Gerez, J Harder, H Jörnvall, M Krook, P Reichard, Characterization of components of the anaerobic ribonucleotide reductase system from Escherichia coli. Journal of Biological Chemistry. ,vol. 267, pp. 25541- 25547 ,(1992) , 10.1016/S0021-9258(19)74074-5
M Fontecave, R Eliasson, P Reichard, Enzymatic regulation of the radical content of the small subunit of Escherichia coli ribonucleotide reductase involving reduction of its redox centers. Journal of Biological Chemistry. ,vol. 264, pp. 9164- 9170 ,(1989) , 10.1016/S0021-9258(18)60509-5
M L Moss, P A Frey, Activation of lysine 2,3-aminomutase by S-adenosylmethionine. Journal of Biological Chemistry. ,vol. 265, pp. 18112- 18115 ,(1990) , 10.1016/S0021-9258(17)44724-7
R M Petrovich, F J Ruzicka, G H Reed, P A Frey, Metal cofactors of lysine-2,3-aminomutase. Journal of Biological Chemistry. ,vol. 266, pp. 7656- 7660 ,(1991) , 10.1016/S0021-9258(20)89498-8
J Baraniak, M L Moss, P A Frey, Lysine 2,3-aminomutase. Support for a mechanism of hydrogen transfer involving S-adenosylmethionine. Journal of Biological Chemistry. ,vol. 264, pp. 1357- 1360 ,(1989) , 10.1016/S0021-9258(18)94194-3
Robert H. Abeles, William S. Beck, The Mechanism of Action of Cobamide Coenzyme in the Ribonucleotide Reductase Reaction Journal of Biological Chemistry. ,vol. 242, pp. 3589- 3593 ,(1967) , 10.1016/S0021-9258(18)95848-5
Volker UNKRIG, Franz A. NEUGEBAUER, Joachim KNAPPE, The free radical of pyruvate formate-lyase: characterization by EPR spectroscopy and involvement in catalysis as studied with the substrate-analogue hypophosphite FEBS Journal. ,vol. 184, pp. 723- 728 ,(1989) , 10.1111/J.1432-1033.1989.TB15072.X
T.P. Chirpich, V. Zappia, R.N. Costilow, H.A. Barker, Lysine 2,3-aminomutase. Purification and properties of a pyridoxal phosphate and S-adenosylmethionine-activated enzyme. Journal of Biological Chemistry. ,vol. 245, pp. 1778- 1789 ,(1970) , 10.1016/S0021-9258(19)77160-9
H P C Hogenkamp, R K Ghambeer, C Brownson, R L Blakley, E Vitols, Cobamides and Ribonucleotide Reduction VI. ENZYME-CATALYZED HYDROGEN EXCHANGE BETWEEN WATER AND DEOXYADENOSYLCOBALAMIN Journal of Biological Chemistry. ,vol. 243, pp. 799- 808 ,(1968) , 10.1016/S0021-9258(19)81736-2
A. F. Wagner, M. Frey, F. A. Neugebauer, W. Schafer, J. Knappe, The free radical in pyruvate formate-lyase is located on glycine-734. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 89, pp. 996- 1000 ,(1992) , 10.1073/PNAS.89.3.996