Physical and enzymological interaction of Bacillus subtilis proteins required for de novo pyridoxal 5′-phosphate biosynthesis

被引：66

作者：

Belitsky, BR ^{[1
]}

机构：

[1] Tufts Univ, Sch Med, Dept Mol Biol & Microbiol, Boston, MA 02111 USA

来源：

JOURNAL OF BACTERIOLOGY | 2004年 / 186卷 / 04期

关键词：

D O I：

10.1128/JB.186.4.1191-1196.2004

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Bacillus subtilis synthesizes pyridoxal 5'-phosphate, the active form of vitamin B-6, by a poorly characterized pathway involving the yaaD and yaaE genes. The pdxS (yaaD) mutant was confirmed to be a strict B-6 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 B-6 biosynthesis.

引用

页码：1191 / 1196

页数：6

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