Mycobacterial polyketide-associated proteins are acyltransferases: Proof of principle with Mycobacterium tuberculosis PapA5
| Autor: | Christopher D. Lima, Julian A. Ferreras, Kenolisa C. Onwueme, Luis E. N. Quadri, John A. Buglino |
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| Rok vydání: | 2004 |
| Předmět: |
Sequence analysis
Molecular Sequence Data Sequence alignment Polymerase Chain Reaction Mass Spectrometry Substrate Specificity Mycobacterium tuberculosis Polyketide Bacterial Proteins Gene cluster Amino Acid Sequence Peptide sequence DNA Primers Multidisciplinary Base Sequence Sequence Homology Amino Acid biology Genetic Complementation Test Biological Sciences biology.organism_classification Lipids Peptide Fragments Kinetics Biochemistry Acyltransferases Acetyltransferase Mutagenesis Site-Directed Polyketide Synthases Sequence Alignment |
| Zdroj: | Proceedings of the National Academy of Sciences. 101:4608-4613 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.0306928101 |
| Popis: | Mycobacterium tuberculosis ( Mt ) produces complex virulence-enhancing lipids with scaffolds consisting of phthiocerol and phthiodiolone dimycocerosate esters (PDIMs). Sequence analysis suggested that PapA5, a so-called polyketide-associated protein (Pap) encoded in the PDIM synthesis gene cluster, as well as PapA5 homologs found in Mt and other species, are a subfamily of acyltransferases. Studies with recombinant protein confirmed that PapA5 is an acetyltransferase. Deletion analysis in Mt demonstrated that papA5 is required for PDIM synthesis. We propose that PapA5 catalyzes diesterification of phthiocerol and phthiodiolone with mycocerosate. These studies present the functional characterization of a Pap and permit inferences regarding roles of other Paps in the synthesis of complex lipids, including the antibiotic rifamycin. |
| Databáze: | OpenAIRE |
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