Oxidation of D-lactate and L-lactate by Neisseria meningitidis: purification and cloning of meningococcal D-lactate dehydrogenase.
Neisseria meningitidis was found to contain at least two lactate-oxidizing enzymes. One of these was purified 460-fold from spheroplast membranes and found to be specific primarily for D-lactate, with low-affinity activity for L-lactate. The gene for this enzyme (dld) was cloned, and a dld mutant was constructed by insertional inactivation of the gene. The mutant was unable to grow on D-lactate but retained the ability to grow on L-lactate, providing evidence for a second lactate-oxidizing enzyme with specificity for L-lactate. High-affinity L-lactate-oxidizing activity was detected in intact bacteria of both the dld+ and dld mutant strains. This L-lactate-oxidizing activity was also seen in sonicated bacteria but was reduced substantially on detergent solubilization or on preparation of spheroplast membranes.
Erwin
A L
AL
Laboratory of Bacterial Pathogenesis and Immunology, Rockefeller University, New York, New York 10021.
Gotschlich
E C
EC
D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000201:enzymology; D003001:Cloning, Molecular; D004269:DNA, Bacterial / Q000235:genetics; D005798:Genes, Bacterial; D006863:Hydrogen-Ion Concentration; D007770:L-Lactate Dehydrogenase / Q000235:genetics* / Q000378:metabolism; D007773:Lactates / Q000378:metabolism*; D008969:Molecular Sequence Data; D009345:Neisseria meningitidis / Q000201:enzymology*; D010084:Oxidation-Reduction; D016415:Sequence Alignment
D004269:DNA, Bacterial; D007773:Lactates; D007770:L-Lactate Dehydrogenase