|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
16
|
|
pubmed:dateCreated |
1996-9-20
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
We report the cloning of lldA, a Neisseria meningitidis gene for L-lactate dehydrogenase (L-LDH). Escherichia coli contains a single L-LDH gene (lldD) in the lld operon (previously lct). E. coli grown in complex media does not have L-LDH activity, but the activity is induced by growth in defined medium with L-lactate as the carbon source. In contrast, meningococci contain at least one L-LDH in addition to the lldA gene product. These enzymes are active in meningococci grown in complex media and are not dependent on growth in L-lactate. The predicted amino acid sequence of lldA is homologous to that of E. coli lldD and of other prokaryotic and eukaryotic flavin mononucleotide-containing enzymes that catalyze the oxidation of L-lactate and other small alpha-hydroxy acids. A mutant with a deletion in lldA was found to have reduced L-LDH activity. However, this mutant was able to grow on L-lactate, indicating that a second L-LDH must exist. Activity of the lldA enzyme was affected by growth conditions, being increased by growth on a defined medium with either L-lactate or pyruvate as the carbon source. For meningococci grown on a complex medium, activity of the lldA enzyme was increased by growth on plates or in well-aerated broth. A second L-lactate-oxidizing activity was seen in bacteria grown in poorly aerated broth. Neisseria gonorrhoeae contains a homolog of lldA. As for meningococci, mutation of the gonococcal lldA reduced L-LDH activity but did not affect growth on L-lactate.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-13877353,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-14047217,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-18473,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-2019756,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-2122175,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-2231712,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-2324094,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-2545623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-2822666,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-2964639,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-3086230,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-3112120,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-3123517,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-3882663,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-3934080,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-4134571,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-415006,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-4632471,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-6295879,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-6997721,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-7476094,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-7542800,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-7758936,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-7964493,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-8125245,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-8360626,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-8407815,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-8407843,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-8485583,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-8522539,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8759842-8722097
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Aug
|
|
pubmed:issn |
0021-9193
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
178
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
4807-13
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:8759842-Aerobiosis,
pubmed-meshheading:8759842-Amino Acid Sequence,
pubmed-meshheading:8759842-Base Sequence,
pubmed-meshheading:8759842-Cloning, Molecular,
pubmed-meshheading:8759842-Consensus Sequence,
pubmed-meshheading:8759842-DNA Primers,
pubmed-meshheading:8759842-Escherichia coli,
pubmed-meshheading:8759842-Gene Expression Regulation, Bacterial,
pubmed-meshheading:8759842-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:8759842-Haemophilus influenzae,
pubmed-meshheading:8759842-Isoenzymes,
pubmed-meshheading:8759842-Kinetics,
pubmed-meshheading:8759842-L-Lactate Dehydrogenase,
pubmed-meshheading:8759842-Molecular Sequence Data,
pubmed-meshheading:8759842-Neisseria meningitidis,
pubmed-meshheading:8759842-Operon,
pubmed-meshheading:8759842-Polymerase Chain Reaction,
pubmed-meshheading:8759842-Restriction Mapping,
pubmed-meshheading:8759842-Sequence Homology, Amino Acid
|
|
pubmed:year |
1996
|
|
pubmed:articleTitle |
Cloning of a Neisseria meningitidis gene for L-lactate dehydrogenase (L-LDH): evidence for a second meningococcal L-LDH with different regulation.
|
|
pubmed:affiliation |
Laboratory of Bacterial Pathogenesis and Immunology, Rockefeller University, New York, New York 10021, USA.
|
|
pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
|
