Fluoride, pyrophosphate, and base release from 2'-deoxy-2'-fluoronucleoside 5'-diphosphates by ribonucleoside-diphosphate reductase.
نویسندگان
چکیده
منابع مشابه
Active site of ribonucleoside diphosphate reductase from Escherichia coli. Inactivation of the enzyme by 2'-substituted ribonucleoside diphosphates.
Ribonucleoside diphosphate reductase is an allosteric enzyme consisting of two nonidentical subunits, proteins B1 and B2. B1 contains dithiols which participate in the oxidation-reduction reactions of electron transport, while B2 contains a free radical essential for activity. Ribonucleoside diphosphates are bound to B1 but not to B2. Addition of 2'-deoxy-2'-chloro ribonucleoside diphosphates t...
متن کاملSelective inhibition of herpes simplex virus ribonucleoside diphosphate reductase by derivatives of 2-acetylpyridine thiosemicarbazone.
The effects of thiosemicarbazone derivatives of 2-acetylpyridine on mammalian and viral ribonucleoside diphosphate reductases were investigated. The enzymes were partially purified from uninfected and herpes simplex virus type-1 (HSV-1)-infected KB cells by sequential salt fractionation with streptomycin sulfate and ammonium sulfate and by affinity chromatography on ATP-agarose. The five thiose...
متن کاملPhysicochemical characterization of ribonucleoside diphosphate reductase from Escherichia coli.
Ribonucleotide reductase from Escherichia coli consists of two nonidentical subunits, proteins Bl and B2. Affinity chromatography resulted in a Bl preparation which appeared homogeneous during polyacrylamide gel electrophoresis and ultracentrifugation. The molecular weight was 160,000 by sedimentation equilibrium centrifugation using a partial specific volume of 0.706 ml per g at 4”. Protein Bl...
متن کاملReaction Mechanism of Ribonucleoside Diphosphate Reductase from Escherichia coli
Ribonucleoside diphosphate reductase consists of two nonidentical subunits, proteins Bl and B2. The enzyme catalyzes the reduction of ribonucleotides to the corresponding deoxyribonucleotides. The electrons required in this reduction are transported from NADPH via a flavoprotein, thioredoxin reductase, to a low molecular weight protein, thioredoxin. The reduced form of thioredoxin acts as hydro...
متن کاملActive Site of Ribonucleoside Diphosphate Reductase from Escherichia coli
Ribonucleoside diphosphate reductase is an allosteric enzyme consisting of two nonidentical subunits, proteins Bl and B2. Bl contains dithiols which participate in the oxidation-reduction reactions of electron transport, while B2 contains a free radical essential for activity. Ribonucleoside diphosphates are bound to Bl but not to B2. Addition of 2’-deoxy-2’-chloro ribonucleoside diphosphates t...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1980
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)70657-7