ArticleFEBS letters2025
In vivo evidence for glycyl radical insertion into a catalytically inactive variant of pyruvate formate-lyase.
Article in FEBS letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The dimeric glycyl radical enzyme pyruvate formate-lyase (PflB; formate acetyltransferase 1) cleaves pyruvate with hypothetical half-site reactivity to formate and acetyl-CoA. The radical introduced onto residue G734 of PflB is transiently transferred to C419 of an adjacent cysteine pair (C418/C419) during catalysis, but it is unclear whether glycyl radical formation is dependent on C419 in vivo. We show here that a deficiency in formate production of an Escherichia coli strain synthesizing a PflB
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