在大肠杆菌K-12中分离出一种pdxJ点突变，该突变绕过了磷酸吡哆醛辅酶生物合成中对PdxH氧化酶的需求。
Isolation of a pdxJ point mutation that bypasses the requirement for the PdxH oxidase in pyridoxal 5' -phosphate coenzyme biosynthesis in Escherichia coli K-12.
作者信息
Man T K, Zhao G, Winkler M E
机构信息
Department of Microbiology and Molecular Genetics, University of Texas Houston Medical School 77030-1501, USA.
出版信息
J Bacteriol. 1996 Apr;178(8):2445-9. doi: 10.1128/jb.178.8.2445-2449.1996.
Abstract
We isolated 26 suppressor mutations that allowed growth of a delta pdxH::omega null mutant in the absence of pyridoxal. Each suppressor mapped to pdxJ, and the eight suppressors sequenced contained the same glycine-to-serine change in the PdxJ polypeptide. This bypass suppression suggests that PdxJ may participate in formation of the pyridine ring of pyridoxine 5'-phosphate.
摘要
我们分离出了26个抑制突变，这些突变使得ΔpdxH::omega缺失突变体在没有吡哆醛的情况下能够生长。每个抑制突变都定位到pdxJ，并且测序的8个抑制突变在PdxJ多肽中包含相同的甘氨酸到丝氨酸的变化。这种旁路抑制表明PdxJ可能参与磷酸吡哆醛吡啶环的形成。
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