Characterization and Structural Determination of CmnG-A, the Adenylation Domain That Activates the Nonproteinogenic Amino Acid Capreomycidine in Capreomycin Biosynthesis

I. Hsuan Chen, Ting Cheng, Yung Lin Wang, Szu Jo Huang, Yu Hsuan Hsiao, Yi Ting Lai, Shu Ing Toh, John Chu, Jeffrey D. Rudolf, Chin Yuan Chang*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

Capreomycidine (Cap) is a nonproteinogenic amino acid and building block of nonribosomal peptide (NRP) natural products. We report the formation and activation of Cap in capreomycin biosynthesis. CmnC and CmnD catalyzed hydroxylation and cyclization, respectively, of l-Arg to form l-Cap. l-Cap is then adenylated by CmnG-A before being incorporated into the nonribosomal peptide. The co-crystal structures of CmnG-A with l-Cap and adenosine nucleotides provide insights into the specificity and engineering opportunities of this unique adenylation domain.

Original languageEnglish
Article numbere202200563
JournalChemBioChem
Volume23
Issue number24
DOIs
StatePublished - 16 Dec 2022

Keywords

  • CmnG
  • adenylation domains
  • capreomycidine
  • capreomycin
  • nonproteinogenic amino acid

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