Neisseria gonorrhoeae possesses two nicotinamide adenine dinucleotide-independent lactate dehydrogenases.
An important metabolic capability of Neisseria gonorrhoeae is the utilization of host-derived lactate. Two isoenzymes of the membrane-associated, pyridine dinucleotide-independent type of lactate dehydrogenase (iLDH) participate in lactate assimilation, but exhibit distinctive properties. Isoenzyme iLDH-I utilized lactate exclusively as substrate, exhibiting a preference for the D-isomer. In contrast, isoenzyme iLDH-II exhibited broad substrate specificity (lactate, phenyllactate, and 4-hydroxyphenyllactate), but was stereospecific for the L-isomers. These results explain the difficulty in isolating mutants unable to utilize lactate.
Fischer
R S
RS
Department of Microbiology and Cell Science, University of Florida, Gainesville 32611.
Martin
G C
GC
Rao
P
P
Jensen
R A
RA
D002462:Cell Membrane / Q000201:enzymology; D002852:Chromatography, Ion Exchange; D003470:Culture Media; D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D007773:Lactates / Q000378:metabolism; D009154:Mutation; D009243:NAD / Q000378:metabolism; D009344:Neisseria gonorrhoeae / Q000201:enzymology* / Q000472:pathogenicity; D013379:Substrate Specificity
D003470:Culture Media; D007527:Isoenzymes; D007773:Lactates; D009243:NAD; D007770:L-Lactate Dehydrogenase