In vivo evidence for glycyl radical insertion into a catalytically inactive variant of pyruvate formate-lyase.

• Tác giả: Michelle Kammel, R Gary Sawers, A F Volker Wagner
• Ngôn ngữ: eng
• Ký hiệu phân loại: 352.49 Budgets for specific international organizations and specific jurisdictions
• Thông tin xuất bản: England : FEBS letters , 2025
• Bộ sưu tập: NCBI
• ID: 747813

Tóm tắt

 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