Condensation (C) domains in the nonribosomal peptide synthetases are capable of catalyzing peptide bond formation between two consecutively bound various amino acids. C-domains coincide in frequency with the number of peptide bonds in the product peptide. In this study, a phylogenetic approach was used to investigate structural diversity of bacterial C-domains. Phylogenetic trees show that the C-domains are clustered into three functional groups according to the types of substrate donor molecules. They are L-peptidyl donors, D-peptidyl donors, and N-acyl donors. The fact that C-domain structure is not subject to optical configuration of amino acid acceptor molecules supports an idea that the conversion from L to D-form of incorporating amino acid acceptor occurs during or after peptide bond formation. L-peptidyl donors and D-peptidyl donors are suggested to separate before separating the lineage of Gram-positive and Gram-negative bacteria in the evolution process. © 2005 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.
Roongsawang, N., Siew, P. L., Washio, K., Takano, K., Kanaya, S., & Morikawa, M. (2005). Phylogenetic analysis of condensation domains in the nonribosomal peptide synthetases. FEMS Microbiology Letters, 252(1), 143–151. https://doi.org/10.1016/j.femsle.2005.08.041