从头合成5'-磷酸吡哆醛所需的枯草芽孢杆菌蛋白质的物理和酶学相互作用。
Physical and enzymological interaction of Bacillus subtilis proteins required for de novo pyridoxal 5'-phosphate biosynthesis.
作者信息
Belitsky Boris R
机构信息
Department of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.
出版信息
J Bacteriol. 2004 Feb;186(4):1191-6. doi: 10.1128/JB.186.4.1191-1196.2004.
Abstract
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.
摘要
枯草芽孢杆菌通过一条涉及yaaD和yaaE基因、特征尚不明确的途径合成维生素B6的活性形式——5'-磷酸吡哆醛。已证实pdxS（yaaD）突变体是严格的B6营养缺陷型，但pdxT（yaaE）突变体却是一种依赖于生长培养基中铵可用性的条件营养缺陷型。PdxS和PdxT蛋白在亲和层析过程中共纯化，并且显然形成了一种具有谷氨酰胺酶活性的复合物。PdxS和PdxT似乎分别编码一种对B6生物合成必不可少的、特异性未知的谷氨酰胺酰胺转移酶的合酶和谷氨酰胺酶亚基。
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