Article
Exploitation of the broad specificity of the membrane-bound isoenzyme of lactate dehydrogenase for direct selection of null mutants in Neisseria gonorrhoeae.
Journal of general microbiology - 1 Jan 1990
Hendry A T, Bhatnagar R K, Shanmugam K T, Jensen R A
Abstract excerpt
Lactic acid is readily utilized as a carbon and energy source by Neisseria gonorrhoeae. The oxidation of lactate is coupled to electron transport via a membrane-bound lactate dehydrogenase (iLDH) which is independent of pyridine nucleotide. The broad substrate specificity of iLDH endows N. gonorrhoeae with the novel ability to convert phenyllactate to L-phenylalanine via phenylpyruvate. N. gonorrhoeae ATCC 27628...
Topics
- Drug Resistance, Microbial
- Isoenzymes
- L-Lactate Dehydrogenase
- Lactates
- Lactic Acid
- Mutation
- Neisseria gonorrhoeae
- Phenylacetates
- Phenylpropionates