Physical and Enzymological Interaction of Bacillus subtilis Proteins Required for De Novo Pyridoxal 5′-Phosphate Biosynthesis
AUTOR(ES)
Belitsky, Boris R.
FONTE
American Society for Microbiology
RESUMO
Bacillus subtilis synthesizes pyridoxal 5′-phosphate, the active form of vitamin B6, by a poorly characterized pathway involving the yaaD and yaaE genes. The pdxS (yaaD) mutant was confirmed to be a strict B6 auxotroph, but the pdxT (yaaE) mutant turned out to be a conditional auxotroph depending on the availability of ammonium in the growth medium. The PdxS and PdxT proteins copurified during affinity chromatography and apparently form a complex that has glutaminase activity. PdxS and PdxT appear to encode the synthase and glutaminase subunits, respectively, of a glutamine amidotransferase of as-yet-unknown specificity essential for B6 biosynthesis.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=344226Documentos Relacionados
- Coenzymatic Activity of Pyridoxal 5′-Sulfate and Related Analogues of Pyridoxal 5′-Phosphate
- Characterization of Two Kinases Involved in Thiamine Pyrophosphate and Pyridoxal Phosphate Biosynthesis in Bacillus subtilis: 4-Amino-5-Hydroxymethyl-2-Methylpyrimidine Kinase and Pyridoxal Kinase
- Biochemical characterization of gapB-encoded erythrose 4-phosphate dehydrogenase of Escherichia coli K-12 and its possible role in pyridoxal 5'-phosphate biosynthesis.
- Involvement of the gapA- and epd (gapB)-Encoded Dehydrogenases in Pyridoxal 5′-Phosphate Coenzyme Biosynthesis in Escherichia coli K-12
- Affinity of Cystathionine β-Synthase for Pyridoxal 5′-Phosphate in Cultured Cells: A MECHANISM FOR PYRIDOXINE-RESPONSIVE HOMOCYSTINURIA