Results 211 to 220 of about 196,005 (260)

Ribonucleotide reductase from saccharomyces cerevisiae

Biochemical and Biophysical Research Communications, 1970
Partially purified ribonucleotide reductase from Saccharomyces cerevisiae was unstable in solution; however, enzyme activity could be maintained by quick-freezing and storage at low temperatures. The reduction of CDP was stimulated by ATPMg++, and maximal activity was obtained with E.
E, Vitols, V A, Bauer, E C, Stanbrough
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Ribonucleotide Reductase—a Radical Enzyme

Science, 1983
Ribonucleotide reductases catalyze the enzymatic formation of deoxyribonucleotides, an obligatory step in DNA synthesis. The native form of the enzyme from Escherichia coli or from mammalian sources contains as part of its polypeptide structure a free tyrosyl radical, stabilized by an iron center.
P, Reichard, A, Ehrenberg
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Crystallographic investigations of ribonucleotide reductase

Biochemical Society Transactions, 1993
Introduction Ribonucleotide reductase catalyses the de novo production of deoxyribonucleotides. The enzyme reduces all the four main ribonucleotides to the corresponding deoxyribonucleotides. In higher organisms and in Eschmkhziz coli. this takes place at the diphosphate level I 1 1. Kibonucleotide reductase from E.
P, Nordlund, A, Aberg, U, Uhlin, H, Eklund   +3 more
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Ribonucleotide reductase: regulation, regulation, regulation

Trends in Biochemical Sciences, 1992
Ribonucleotide reductase (RNR) catalyses the rate limiting step in the production of deoxyribonucleotides needed for DNA synthesis. It is composed of two dissimilar subunits, R1, the large subunit containing the allosteric regulatory sites, and R2, the small subunit containing a binuclear iron center and a tyrosyl free radical.
S J, Elledge, Z, Zhou, J B, Allen
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Structural features of ribonucleotide reductase

Proteins: Structure, Function, and Bioinformatics, 1986
AbstractHerpes simplex virus type 1 (HSV‐1) encodes a ribonucleotide reductase which comprises two polypeptides with sizes of 136,000 (RR1) and 38,000 mol. wt. (RR2). We have determined the entire DNA sequence specifying HSV‐1 RR1 and have identified two adjacent open reading frames in varicella‐zoster virus (VZV) which have homology to HSV RR1 and RR2;
I, Nikas, J, McLauchlan, A J, Davison, W R, Taylor, J B, Clements   +4 more
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Drug action on ribonucleotide reductase

Advances in Enzyme Regulation, 1985
Ribonucleotide reductase catalyzes the rate-limiting step in DNA synthesis. It represents a key metabolic site at which specific inhibitors have been directed as potential antitumor agents. Several different classes of ribonucleotide reductase inhibitors have been generated and studied.
J G, Cory, G L, Carter
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Thiyl Radicals in Ribonucleotide Reductases

Science, 1996
The ribonucleoside triphosphate reductase (RTPR) from Lactobacillus leichmannii catalyzes adenosylcobalamin (AdoCbl)-dependent nucleotide reduction, as well as exchange of the 5′ hydrogens of AdoCbl with solvent. A protein-based thiyl radical is proposed as an intermediate in both of these processes. In the presence
S, Licht, G J, Gerfen, J, Stubbe
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Regulation of Ribonucleotide Reductase

1981
Publisher Summary This chapter discusses the regulation of ribonucleotide reductase. Ribonucleotide reductase catalyzes the first unique step of DNA synthesis by converting the four ribonucleotides to the corresponding deoxyribonucleotides. Deoxyribonucleotides are highly specialized metabolites playing only limited roles apart from their function as
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Transcriptional Regulation of Ribonucleotide Reductase

1991
The Swiss 3T3 cell system can be used to explore the molecular mechanism of proliferation. These fibroblasts can be arrested in a quiescent homogeneous Go/G1 state by serum deprivation and then induced to proliferate by a variety of mitogenic growth factors (1). An important endeavour in determining the basis of growth factor action is to elucidate the
D A, Albert, E, Rozengurt
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Ribonucleotide reductases and radical reactions

Cellular and Molecular Life Sciences (CMLS), 1998
Ribonucleotide reductases (RNRs) catalyse the reduction of ribonucleotides to deoxyribonucleotides. They play a pivotal role in the regulation of DNA synthesis and are targets for antiproliferative drugs. Ribonucleotide reductases are unique enzymes in that they all require a protein radical for activity.
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