Results 241 to 250 of about 48,825 (277)

Reduction of Ribonucleotides

Annual Review of Biochemistry, 1979
PERSPECTIVES AND SUMMARY 1 33 RIBONUCLEOTIDE REDUCTASE FROM ES CHERICHIA COLI 136 Structural Aspects 136 Reaction Mechanism ....... .. ..... ......... ..... ... ...... ... ... ... ....... .. ..... .. ... ..... ... . 138 Allosteric Control 1 39 Hydrogen Transport System 140 RIBONUCLEOTIDE REDUCING SYSTEMS INDUCED BY BACTERIOPHAGES .... . . .
Lars Thelander, Peter Reichard
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Ribonucleotide Reductases

Annual Review of Biochemistry, 2006
Ribonucleotide reductases (RNRs) transform RNA building blocks to DNA building blocks by catalyzing the substitution of the 2′OH-group of a ribonucleotide with a hydrogen by a mechanism involving protein radicals. Three classes of RNRs employ different mechanisms for the generation of the protein radical. Recent structural studies of members from each
Pär, Nordlund, Peter, Reichard
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Carbocyclic glycinamide ribonucleotide is a substrate for glycinamide ribonucleotide transformylase

Archives of Biochemistry and Biophysics, 1988
The carbocyclic analog of glycinamide ribonucleotide has been synthesized from the racemic parent trihydroxy cyclopentyl amine (B.L. Kam and N.J. Oppenheimer (1981) J. Org. Chem. 46, 3268-3272). This analog was accepted as a substrate (Km = 18 microM, Vmax = 0.23 mM/min) by mammalian glycinamide ribonucleotide transformylase (EC 2.1.2.2) with an ...
Martyn F. Price, Carol A. Caperelli
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The reduction of ribonucleotides catalyzed by the enzyme ribonucleotide reductase

Theoretical Chemistry Accounts: Theory, Computation, and Modeling (Theoretica Chimica Acta), 2002
This work is devoted to the study of the radical catalytic pathway for the ribonucleotide reduction process assisted by ribonucleotide reductase. The present study is directed toward the investigation of one of the most controversial steps in the reduction pathway – the elimination of the 2′ hydroxyl group from the ribonucleotide.
Maria J. Ramos, Leif A. Eriksson, Pedro A. Fernandes   +2 more
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Thionucleotides as Inhibitors of Ribonucleotide Reductase [PDF]

Nucleosides, Nucleotides and Nucleic Acids, 2003
AbstractFor Abstract see ChemInform Abstract in Full Text.
Jean-Luc Décout, M. Lepoivre, B. Roy, Stéphane Chambert   +3 more
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Isolation of a multifunctional protein with aminoimidazole ribonucleotide synthetase, glycinamide ribonucleotide synthetase and glycinamide ribonucleotide transformylase activities: characterization of the aminoimidazole ribonucleotide synthetase

Biochemistry, 1986
5-Aminoimidazole ribonucleotide (AIR) synthetase, glycinamide ribonucleotide (GAR) synthetase, and GAR transformylase activities from chicken liver exist on a single polypeptide of Mr 110,000 [Daubner, C. S., Schrimsher, J. L., Schendel, F. J., Young, M., Henikoff, S., Patterson, D., Stubbe, J., & Benkovic, S. J.
J. Stubbe, J. L. Schrimsher, Frederick J. Schendel, Frederick J. Schendel   +3 more
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Ribonucleotide activation by enzyme ribonucleotide reductase: Understanding the role of the enzyme

Journal of Computational Chemistry, 2004
AbstractThis article focuses on the first step of the catalytic mechanism for the reduction of ribonucleotides catalyzed by the enzyme Ribonucleotide Reductase (RNR). This corresponds to the activation of the substrate. In this work a large model of the active site region involving 130 atoms was used instead of the minimal gas phase models used in ...
Maria J. Ramos, Pedro A. Fernandes, Leif A. Eriksson, Nuno M. F. S. A. Cerqueira   +3 more
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Affinity labeling of ribonucleotide reductase by the 2′,3′-dialdehyde derivatives of ribonucleotides

Archives of Biochemistry and Biophysics, 1983
Ribonucleotide reductase from Corynebacterium nephridii is rapidly inactivated by the 2',3'-dialdehyde derivatives of CDP (dial-CDP) and ADP (dial-ADP). The analog of CDP causes the progressive inactivation of ribonucleotide reductase activity with Ki of 0.26 mM and a maximum inactivation rate of 0.092 min-1 at saturating concentrations of dial-CDP ...
Harry P. C. Hogenkamp, Pei Kuo Tsai
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