Characterization of Cfa1, a Monofunctional Acyl Carrier Protein Involved in the Biosynthesis of the Phytotoxin Coronatine
| Autor: | Heather Seidle, Vidhya Rangaswamy, Ronald J. Parry, Carol L. Bender, Robin Couch |
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| Rok vydání: | 2004 |
| Předmět: |
Bacterial Toxins
Molecular Sequence Data Pseudomonas syringae macromolecular substances Biology medicine.disease_cause Microbiology chemistry.chemical_compound Biosynthesis Acyl Carrier Protein Acyl-Carrier Protein S-Malonyltransferase Escherichia coli Fatty Acid Synthase Type II medicine Amino Acids Molecular Biology Escherichia coli Proteins Coronatine Phytotoxin Enzymes and Proteins enzymes and coenzymes (carbohydrates) Acyl carrier protein Indenes Biochemistry chemistry Acyltransferases biology.protein lipids (amino acids peptides and proteins) Fimbriae Proteins |
| Zdroj: | Journal of Bacteriology. 186:2499-2503 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.186.8.2499-2503.2004 |
| Popis: | Cfa1 was overproduced in Escherichia coli and Pseudomonas syringae , and the degree of 4′-phosphopantetheinylation was determined. The malonyl-coenzyme A:acyl carrier protein transacylase (FabD) of P. syringae was overproduced and shown to catalyze malonylation of Cfa1, suggesting that FabD plays a role in coronatine biosynthesis. Highly purified Cfa1 did not exhibit self-malonylation activity. |
| Databáze: | OpenAIRE |
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