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Published on: November 3, 2018
Isolation and complete sequence of the purL gene encoding FGAM synthase II in Lactobacillus casei
Z M Gu1, D W Martindale, B H Lee
1Department of Microbiology, McGill University, Macdonald Campus, Ste. Anne de Bellevue, Québec, Canada.
Abstract:
The purL gene from Lactobacillus casei, encoding phosphoribosylformylglycinamidine synthase II involved in the de novo synthesis of purines, was cloned and sequenced. The putative purL product of 741 amino acids (M(r) of 79,575) shows 25% and 53% identity to the homologous enzymes from Escherichia coli and Bacillus subtilis, respectively. In addition, partial sequences of two other pur genes (purQ and purF) and a possible third gene (purC) were obtained. All these genes are organized in an operon similar to that of B. subtilis. In contrast, the corresponding genes from E. coli and Salmonella typhimurium are scattered through the genome.
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