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Generation of the glycyl radical of the anaerobic Escherichia coli ribonucleotide reductase requires a specific activating enzyme.

Authors
  • Sun, X
  • Eliasson, R
  • Pontis, E
  • Andersson, J
  • Buist, G
  • Sjöberg, B M
  • Reichard, P
Type
Published Article
Journal
The Journal of biological chemistry
Publication Date
Feb 10, 1995
Volume
270
Issue
6
Pages
2443–2446
Identifiers
PMID: 7852304
Source
Medline
License
Unknown

Abstract

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.

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