@article{7993168263f04a6895a36bf3b8e0debb,
title = "Characterization and Structural Determination of CmnG-A, the Adenylation Domain That Activates the Nonproteinogenic Amino Acid Capreomycidine in Capreomycin Biosynthesis",
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.",
keywords = "CmnG, adenylation domains, capreomycidine, capreomycin, nonproteinogenic amino acid",
author = "Chen, {I. Hsuan} and Ting Cheng and Wang, {Yung Lin} and Huang, {Szu Jo} and Hsiao, {Yu Hsuan} and Lai, {Yi Ting} and Toh, {Shu Ing} and John Chu and Rudolf, {Jeffrey D.} and Chang, {Chin Yuan}",
note = "Publisher Copyright: {\textcopyright} 2022 Wiley-VCH GmbH.",
year = "2022",
month = dec,
day = "16",
doi = "10.1002/cbic.202200563",
language = "English",
volume = "23",
journal = "ChemBioChem",
issn = "1439-4227",
publisher = "Wiley-VCH Verlag",
number = "24",
}