Abstract
Mutant SM6, of Glp- Mal- phenotype, was isolated from Salmonella typhimurium LT2 after treatment with N-methyl-N′-nitro-N-nitrosoguanidine. The mutant was able to use neither glycerol nor l-α-glycerophosphate, nor maltose as carbon source. Enzyme and transport assays indicated that glycerol kinase and l-α-glycerophosphate permease were present. No activity of the cytochrome linked l-α-glycerophosphate dehydrogenase could be demonstrated. This activity was present in LT2 cells grown in the presence of glycerol. These results were interpreted as a glpD- character in the mutant. The inability to utilize maltose as carbon source was due to lack of the amylomaltase activity. The second enzyme needed for the utilization of maltose, maltodextrine phosphorylase, was present in mutant SM6 at normal levels. The mutant was thus malQ-. By conjugation, both affected loci were located at about minutes 111–112 on the bacterial chromosome. By transduction it was found that there was approximately a 20% linkage between the two affected loci.
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Aceves-Piña, E., Ortega, M.V. & Artís, M. Linkage of the Salmonella typhimurium chromosomal loci encoding for the cytochrome-linked l-α-glycerophosphate dehydrogenase and amylomaltase activities. Arch. Microbiol. 101, 59–70 (1974). https://doi.org/10.1007/BF00455925
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DOI: https://doi.org/10.1007/BF00455925