The broad-specificity, membrane-bound lactate dehydrogenase of Neisseria gonorrhoeae: ties to aromatic metabolism.
Neisseria gonorrhoeae can convert phenyllactate (PL) to phenylalanine and 4-hydroxyphenyllactate (HPL) to tyrosine. This was demonstrated by nutritional and physiological approaches. The enzymic basis for this unusual ability was shown to be the broad specificity of a particulate, unidirectional, pyridine-nucleotide-independent lactate dehydrogenase. This enzyme, denoted [iLDH], has been implicated in a pathogenic mechanism whereby host-derived lactate is linked to increased gonococcal oxygen consumption and electron transport. A similar role for HPL, a metabolite available in human host tissues, may provide a selective basis to explain evolution of broadened [iLDH] specificity in Neisseria. The interplay between aromatic metabolism and [iLDH] suggests new approaches for manipulating the host-pathogen relationship.
Bhatnagar
R K
RK
Department of Microbiology and Cell Science, University of Florida, Gainesville 32611.
Hendry
A T
AT
Shanmugam
K T
KT
Jensen
R A
RA
D002462:Cell Membrane / Q000201:enzymology; D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D007770:L-Lactate Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism*; D007773:Lactates / Q000378:metabolism; D009344:Neisseria gonorrhoeae / Q000378:metabolism*; D010666:Phenylpropionates / Q000378:metabolism
D007773:Lactates; D010666:Phenylpropionates; C017648:3-phenyllactic acid; C001418:4-hydroxyphenyllactic acid; D007770:L-Lactate Dehydrogenase