Hydrogen donor specificity of cobamide-dependent ribonucleotide reductase and allosteric regulation of substrate specificity.

نویسندگان

  • W S Beck
  • M Goulian
  • A Larsson
  • P Reichard
چکیده

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Regulation of Cobamide-dependent Ribonucleotide Reductase by Allosteric Effecters and Divalent Cations*

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Factors regulating the rate behavior and substrate specificity of purified cobamide-dependent ribonucleotide reductase of Lacfobacillus leichmannii have been examined in detail. Reduction of each of the four common ribonucleoside triphosphates (@dine triphosphate, uridine triphosphate, adenosine triphosphate, and guanosine triphosphate) is maximally stimulated by a different deoxyribonucleoside...

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Molecular basis for allosteric specificity regulation in class Ia ribonucleotide reductase from Escherichia coli

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The mechanism of action of cobamide coenzyme in the ribonucleotide reductase reaction.

When highly purified cobamide-dependent ribonucleotide reductase from Lacfobacillus leichmannii is incubated with synthetically prepared 5,6-dimethylbenzimidazolylcobamide 5’-deoxyadenosyl coenzyme containing tritium attached to carbon atom 5’ of the deoxyadenosyl moiety (DBCC-5’-3H), tritium is transferred from DBCC-5’-3H to Hz0 in a reaction requiring substrate, enzyme, and dithiol reductant....

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Ribonucleotide reductases: the evolution of allosteric regulation.

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عنوان ژورنال:
  • The Journal of biological chemistry

دوره 241 9  شماره 

صفحات  -

تاریخ انتشار 1966