An in Vitro Reducing System for the Enzymic Conversion of Cobalamin to Adenosylcobalamin
| Autor: | Jorge C. Escalante-Semerena, Maris V. Fonseca |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Flavodoxin
Stereochemistry Molecular Sequence Data In Vitro Techniques Reductase Biochemistry Mass Spectrometry Bacterial Proteins Escherichia coli medicine Amino Acid Sequence Molecular Biology Chromatography High Pressure Liquid Ferredoxin chemistry.chemical_classification Alkyl and Aryl Transferases Sequence Homology Amino Acid biology Chemistry Biological activity Cell Biology Adenosylcobalamin Amino acid Ferredoxin-NADP Reductase Vitamin B 12 Enzyme Dehydratase biology.protein bacteria Electrophoresis Polyacrylamide Gel Cobamides Oxidation-Reduction medicine.drug |
| Zdroj: | Journal of Biological Chemistry. 276:32101-32108 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m102510200 |
| Popis: | Homogeneous ferredoxin (flavodoxin):NADP(+) reductase and flavodoxin A proteins served as electron donors for the reduction of co(III)rrinoids to co(I)rrinoids in vitro. The resulting co(I)rrinoids served as substrates for the ATP:co(I)rrinoid adenosyltransferase (CobA) enzyme of Salmonella enterica serovar Typhimurium LT2 and were converted to their respective adenosylated derivatives. The reaction products were isolated by reverse phase high performance liquid chromatography, and their identities were confirmed by UV-visible spectroscopy, mass spectrometry, and in vivo biological activity assays. Adenosylcobalamin generated by this system supported the activity of 1,2-propanediol dehydratase as effectively as authentic adenosylcobalamin. This is the first report of a protein system that can be coupled to the adenosyltransferase CobA enzyme for the conversion of co(III)rrinoids to their adenosylated derivatives. |
| Databáze: | OpenAIRE |
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