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Journal of Bacteriology, February 2004, p. 1191-1196, Vol. 186, No. 4
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.4.1191-1196.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Physical and Enzymological Interaction of Bacillus subtilis Proteins Required for De Novo Pyridoxal 5'-Phosphate Biosynthesis

Boris R. Belitsky*

Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts 02111

Received 31 July 2003/ Accepted 5 October 2003

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.

* Mailing address: Department of Molecular Biology and Microbiology, Tufts University School of Medicine, 136 Harrison Ave., Boston, MA 02111. Phone: (617) 636-3618. Fax: (617) 636-0337. E-mail: bbelit02{at}granite.tufts.edu.

Journal of Bacteriology, February 2004, p. 1191-1196, Vol. 186, No. 4
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.4.1191-1196.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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