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  • Title: Exploitation of the broad specificity of the membrane-bound isoenzyme of lactate dehydrogenase for direct selection of null mutants in Neisseria gonorrhoeae.
    Author: Hendry AT, Bhatnagar RK, Shanmugam KT, Jensen RA.
    Journal: J Gen Microbiol; 1990 Jan; 136(1):45-50. PubMed ID: 2112587.
    Abstract:
    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 typifies a class of clinical isolate whose growth is inhibited by phenylpyruvate (or L-phenylalanine). Exploiting resistance to growth inhibition by phenyllactate as a strategy of positive selection, mutant derivatives of strain ATCC 27628 lacking iLDH activity were readily obtained. These mutants are incapable of oxidizing phenyllactate, and lack the parent-strain ability to reduce c-type cytochromes in the presence of lactate, phenyllactate or 4-hydroxyphenyllactate. They retain, however, a cytoplasmic NAD(+)-linked lactate dehydrogenase (nLDH). Since the mutants retained the ability to grow on lactate as a sole source of carbon, nLDH presumably can function in an opposite-to-normal physiological direction in the absence of iLDH. This would explain the failure to isolate iLDH-deficient mutants by selection for inability to grow on lactate.
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