Phylogenetic analysis of condensation domains in the nonribosomal peptide synthetases
| Autor: | Kenji Washio, Shigenori Kanaya, Masaaki Morikawa, Kazufumi Takano, Niran Roongsawang, Siew Ping Lim |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
chemistry.chemical_classification
Phylogenetic tree Protein Conformation Lineage (evolution) Molecular Sequence Data Peptide Biology Gram-Positive Bacteria Microbiology Combinatorial chemistry Substrate Specificity Amino acid Condensation domain chemistry Nonribosomal peptide Gram-Negative Bacteria Peptide Biosynthesis Nucleic Acid-Independent Genetics Peptide bond Amino Acid Sequence Peptide Synthases Peptides Molecular Biology Peptide sequence Phylogeny |
| Zdroj: | FEMS Microbiology Letters. 252:143-151 |
| ISSN: | 1574-6968 0378-1097 |
| DOI: | 10.1016/j.femsle.2005.08.041 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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