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枯草芽孢杆菌的嘧啶生物合成途径。

Pyrimidine biosynthetic pathway of Baccillus subtilis.

作者信息

Potvin B W, Kelleher R J, Gooder H

出版信息

J Bacteriol. 1975 Aug;123(2):604-15. doi: 10.1128/jb.123.2.604-615.1975.

Abstract

Biochemical and genetic data were obtained from a series of 51 Pyr- strains of Bacillus subtilis. The observed enzymatic deficiencies allowed the mutants to be placed into 12 clases, some of which represent defects in more than one of the six known pyrimidine biosynthetic enzymes. Mapping analysis by transformation has shown that all the Pyr- mutations are located in a single small area of the B. subtilis genome. A correlation of the biochemical defects and the genetic data has been made. Those mutations conferring similar enzymatic deficiencies were found to be contiguous on the B. subtilis map. Regulatory aspects of the pyrimidine pathway have also been investigated and are compared to previously reported results from other organisms. Evidence is presented which bears upon the possible physical association of the first three enzymes and the association of at least some of the enzymes of this pathway with particulate elements of the cell. A model for the organization of the enzymes is presented with dihydroorotate dehydrogenase as the central enzyme in a proposed aggregate.

摘要

从一系列51株枯草芽孢杆菌的Pyr-菌株中获取了生化和遗传数据。观察到的酶缺陷使这些突变体可被分为12类,其中一些代表六种已知嘧啶生物合成酶中不止一种的缺陷。通过转化进行的图谱分析表明,所有Pyr-突变都位于枯草芽孢杆菌基因组的一个小区域内。已对生化缺陷和遗传数据进行了关联。发现在枯草芽孢杆菌图谱上,那些导致相似酶缺陷的突变是相邻的。还对嘧啶途径的调控方面进行了研究,并与其他生物体先前报道的结果进行了比较。提供了证据,证明前三种酶可能存在物理关联,以及该途径的至少一些酶与细胞颗粒成分的关联。提出了一个酶组织模型,以二氢乳清酸脱氢酶作为拟议聚集体中的核心酶。

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