Structural basis for glycyl radical formation by pyruvate formate-lyase activating enzyme (Q27652499)

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Jian Yang

2

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Meng Li

3

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William E Broderick

4

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Catherine L Drennan

Proceedings of the National Academy of Sciences of the United States of America

6

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language of work or name

English

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publication date

21 October 2008

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published in

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volume

105

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issue

42

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page(s)

16137-41

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The free radical in pyruvate formate-lyase is located on glycine-734

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Spore photoproduct lyase from Bacillus subtilis spores is a novel iron-sulfur DNA repair enzyme which shares features with proteins such as class III anaerobic ribonucleotide reductases and pyruvate-formate lyases

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Biochemical and genetic characterization of benzylsuccinate synthase from Thauera aromatica: a new glycyl radical enzyme catalysing the first step in anaerobic toluene metabolism.

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Glycyl free radical in pyruvate formate-lyase: synthesis, structure characteristics, and involvement in catalysis.

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21 January 2018

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Pyruvate Formate-Lyase-Activating Enzyme: Strictly Anaerobic Isolation Yields Active Enzyme Containing a [3Fe–4S]+ Cluster

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Routes of flavodoxin and ferredoxin reduction in Escherichia coli. CoA-acylating pyruvate: flavodoxin and NADPH: flavodoxin oxidoreductases participating in the activation of pyruvate formate-lyase

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inferred from PubMed ID database lookup

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A Glycyl Radical Site in the Crystal Structure of a Class III Ribonucleotide Reductase

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