Neisseria gonorrhoeaepossesses two nicotinamide adenine dinucleotide-independent lactate dehydrogenases
| Autor: | Gaines C. Martin, Randy S. Fischer, Roy A. Jensen, Premila Rao |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Mutant
Nicotinamide adenine dinucleotide medicine.disease_cause Microbiology Isozyme Substrate Specificity chemistry.chemical_compound Lactate dehydrogenase Genetics medicine Molecular Biology chemistry.chemical_classification L-Lactate Dehydrogenase biology Cell Membrane Chromatography Ion Exchange NAD biology.organism_classification Neisseria gonorrhoeae Culture Media Isoenzymes Enzyme chemistry Biochemistry Mutation Lactates Neisseriaceae Bacteria |
| Zdroj: | FEMS Microbiology Letters. 115:39-44 |
| ISSN: | 1574-6968 0378-1097 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text