Generation of the Glycyl Radical of the Anaerobic Escherichia coli Ribonucleotide Reductase Requires a Specific Activating Enzyme
| Autor: | Peter Reichard, Britt-Marie Sjöberg, Rolf Eliasson, Girbe Buist, Jessica Andersson, Elisabet Pontis, Xueyin Sun |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
DNA
Bacterial 7-Dehydrocholesterol reductase Ribonucleotide Free Radicals Molecular Sequence Data Glycine Biology Reductase medicine.disease_cause Biochemistry Enzyme activator Ribonucleotide Reductases Escherichia coli medicine Amino Acid Sequence Anaerobiosis Molecular Biology chemistry.chemical_classification Base Sequence Sequence Homology Amino Acid Cell Biology Enzyme Activation Open reading frame Ribonucleotide reductase Enzyme chemistry |
| Zdroj: | Journal of Biological Chemistry. 270:2443-2446 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.270.6.2443 |
| Popis: | The anaerobic ribonucleotide reductase from Escherichia coli contains a glycyl radical as part of its polypeptide structure. The radical is generated by an enzyme system present in E. coli. The reductase is coded for by the nrdD gene located at 96 min. Immediately downstream, we now find an open reading frame with the potential to code for a 17.5-kDa protein with sequence homology to a protein required for the generation of the glycyl radical of pyruvate formate lyase. The protein corresponding to this open reading frame is required for the generation of the glycyl radical of the anaerobic reductase and binds tightly to the reductase. The "activase" contains iron, required for activity. The general requirements for generation of a glycyl radical are identical for the reductase and pyruvate formate lyase. For the reductase, the requirement of an iron-containing activase suggests the possibility that the iron-sulfur cluster of the enzyme is not involved in radical generation but may participate directly in the reduction of the ribonucleotide. |
| Databáze: | OpenAIRE |
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