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大肠杆菌的2-酮-3-脱氧葡萄糖酸6-磷酸醛缩酶突变体

2-keto-3-deoxygluconate 6-phosphate aldolase mutants of Escherichia coli.

作者信息

Fradkin J E, Fraenkel D G

出版信息

J Bacteriol. 1971 Dec;108(3):1277-83. doi: 10.1128/jb.108.3.1277-1283.1971.

Abstract

A new mutation in Escherichia coli, giving inability to grow on gluconic, glucuronic, or galacturonic acids, has been identified as complete deficiency of 2-keto-3-deoxygluconate 6-phosphate (KDGP) aldolase activity. The genetic map position of the locus, eda, is about 35 min. The inability to grow on the uronic acids was expected, because the aldolase is on the sole known pathway of their metabolism. However, inability to grow on gluconate was less expected, because the hexose monophosphate shunt might be used, as happens in mutants blocked in the previous step, edd, of the Entner-Doudoroff pathway. The likely explanation of gluconate negativity is inhibition by accumulated KDGP, because gluconate is inhibitory to growth on other substances, and one type of gluconate revertant is eda(-), edd(-). KDGP is probably the inducer of KDGP aldolase.

摘要

已鉴定出大肠杆菌中的一种新突变,该突变导致其无法在葡萄糖酸、葡萄糖醛酸或半乳糖醛酸上生长,这是由于2-酮-3-脱氧葡萄糖酸6-磷酸(KDGP)醛缩酶活性完全缺乏所致。该基因座eda的遗传图谱位置约为35分钟。无法在糖醛酸上生长是可以预料的,因为醛缩酶位于其唯一已知的代谢途径上。然而,无法在葡萄糖酸上生长则较难预料,因为可能会利用磷酸己糖支路,就像在Entner-Doudoroff途径中前一步骤edd受阻的突变体那样。葡萄糖酸阴性的可能解释是积累的KDGP产生抑制作用,因为葡萄糖酸对在其他物质上的生长具有抑制作用,并且一种葡萄糖酸回复突变体是eda(-)、edd(-)。KDGP可能是KDGP醛缩酶的诱导物。

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