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J. Bacteriol., Aug 1996, 4807-4813, Vol 178, No. 16
Copyright © 1996, American Society for Microbiology

Cloning of a Neisseria meningitidis gene for L-lactate dehydrogenase (L- LDH): evidence for a second meningococcal L-LDH with different regulation

AL Erwin and EC Gotschlich
Laboratory of Bacterial Pathogenesis and Immunology, Rockefeller University, New York, New York 10021, USA.

We report the cloning of lldA, a Neisseria meningitidis gene for L- lactate dehydrogenase (L-LDH). Escherichia coli contains a single L-LDH gene (lldD) in the lld operon (previously lct). E. coli grown in complex media does not have L-LDH activity, but the activity is induced by growth in defined medium with L-lactate as the carbon source. In contrast, meningococci contain at least one L-LDH in addition to the lldA gene product. These enzymes are active in meningococci grown in complex media and are not dependent on growth in L-lactate. The predicted amino acid sequence of lldA is homologous to that of E. coli lldD and of other prokaryotic and eukaryotic flavin mononucleotide- containing enzymes that catalyze the oxidation of L-lactate and other small alpha-hydroxy acids. A mutant with a deletion in lldA was found to have reduced L-LDH activity. However, this mutant was able to grow on L-lactate, indicating that a second L-LDH must exist. Activity of the lldA enzyme was affected by growth conditions, being increased by growth on a defined medium with either L-lactate or pyruvate as the carbon source. For meningococci grown on a complex medium, activity of the lldA enzyme was increased by growth on plates or in well-aerated broth. A second L-lactate-oxidizing activity was seen in bacteria grown in poorly aerated broth. Neisseria gonorrhoeae contains a homolog of lldA. As for meningococci, mutation of the gonococcal lldA reduced L- LDH activity but did not affect growth on L-lactate.

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