Premium
Selection and biochemical studies of pyrimidine‐requiring mutants of Lactobacillus plantarum
Author(s) -
Masson A.,
Kammerer B.,
Hubert J.C.
Publication year - 1994
Publication title -
journal of applied bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.889
H-Index - 156
eISSN - 1365-2672
pISSN - 0021-8847
DOI - 10.1111/j.1365-2672.1994.tb03049.x
Subject(s) - uracil , auxotrophy , pyrimidine metabolism , lactobacillus plantarum , biochemistry , mutant , aspartate carbamoyltransferase , enzyme , orotic acid , pyrimidine , biology , chemistry , bacteria , lactic acid , gene , genetics , purine , dna , allosteric regulation
Mutagenesis and mutant enrichment in Lactobacillus plantarum, a lactic acid bacterium used in silage, sauerkraut and sausage fabrication, were studied. In optimal conditions, auxotrophic mutants were obtained that permitted investigation of the de novo pyrimidine biosynthesis. Uracil‐requiring mutants were characterized for their enzymatic defect, in aspartate transcarbamylase (ATCase), dihydro‐orotase (DHOase), dihydro‐orotate dehydrogenase (DHOdehase), orotidine monophosphate pyrophosphorylase (OMPppase) or in orotidine monophosphate decarboxylase (OMPdecase). The five enzymatic activities are totally repressed by uracil in the growth medium.