title: The broad-specificity, membrane-bound lactate dehydrogenase of Neisseria gonorrhoeae: ties to aromatic metabolism.
abstract: 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.
authors.affiliation: Department of Microbiology and Cell Science, University of Florida, Gainesville 32611.
authors.forename: R K
authors.initials: RK
authors.lastname: Bhatnagar
authors.forename: A T
authors.initials: AT
authors.lastname: Hendry
authors.forename: K T
authors.initials: KT
authors.lastname: Shanmugam
authors.forename: R A
authors.initials: RA
authors.lastname: Jensen
mesh_terms: 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
chemical_list: D007773:Lactates; D010666:Phenylpropionates; C017648:3-phenyllactic acid; C001418:4-hydroxyphenyllactic acid; D007770:L-Lactate Dehydrogenase