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Gene Review

ldhA  -  fermentative D-lactate dehydrogenase, NAD...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK1377, JW1375, hslF, hslI, htpH
 
 
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Disease relevance of ldhA

 

High impact information on ldhA

  • These results suggest that although binding of D-lactate dehydrogenase is independent of the physical state of the membrane, reconstitution of the D-lactate oxidase activity in membrane vesicles is dependent upon the fatty acid composition of the phospholipid, hence the physical state of the membrane [3].
  • Inactive and temperature-sensitive folding mutants generated by tryptophan substitutions in the membrane-bound d-lactate dehydrogenase of Escherichia coli [4].
  • Most of the expressed D-lactate dehydrogenase from the partially active mutants is also Triton-insoluble; a small fraction, however, is soluble in Triton and can be purified to yield active enzyme [4].
  • Monoclonal antibodies against the membrane-bound, flavin-linked D-lactate dehydrogenase of Escherichia coli: preparation, characterization, and use in immunoaffinity chromatography [5].
  • After the column is washed free of unadsorbed protein, elution at high pH in the presence of guanidine hydrochloride yields a fraction containing highly purified, catalytically active D-lactate dehydrogenase [5].
 

Chemical compound and disease context of ldhA

 

Biological context of ldhA

 

Associations of ldhA with chemical compounds

  • VAL23 is a double mutant unable to produce lactate and formate due to deletions of the ldhA and pflB genes that code for lactate dehydrogenase and pyruvate-formate lyase, respectively [7].
  • The protocol involves chromatography of a Triton X-100 extract of membrane vesicles containing D-lactate dehydrogenase on a column made with the monoclonal antibody coupled to a solid support [5].
  • 19F-Labeled D-lactate dehydrogenases prepared by addition of fluorotryptophans to a tryptophan-requiring strain are able to reconstitute D-lactate dehydrogenase-deficient membrane vesicles [8].
  • A biochemical study of the reconstitution of D-lactate dehydrogenase-deficient membrane vesicles using fluorine-labeled components [8].
  • 19F-Labeled membrane vesicles, prepared by growing a fatty acid auxotroph of a D-lactate dehydrogenase-deficient strain on 8,8-difluoromyristic acid, can be reconstituted for oxidase and transport activities by binding exogenous D-lactate dehydrogenase [8].
 

Analytical, diagnostic and therapeutic context of ldhA

References

  1. Chromosome-Encoded Narrow-Spectrum Ambler Class A {beta}-Lactamase GIL-1 from Citrobacter gillenii. Naas, T., Aubert, D., Ozcan, A., Nordmann, P. Antimicrob. Agents Chemother. (2007) [Pubmed]
  2. Fed-batch two-phase production of alanine by a metabolically engineered Escherichia coli. Smith, G.M., Lee, S.A., Reilly, K.C., Eiteman, M.A., Altman, E. Biotechnol. Lett. (2006) [Pubmed]
  3. Effect of lipids on the reconstitution of D-lactate oxidase in Escherichia coli membrane vesicles. George-Nascimento, C., Wakil, S.J., Short, S.A., Kaback, H.R. J. Biol. Chem. (1976) [Pubmed]
  4. Inactive and temperature-sensitive folding mutants generated by tryptophan substitutions in the membrane-bound d-lactate dehydrogenase of Escherichia coli. Truong, H.T., Pratt, E.A., Rule, G.S., Hsue, P.Y., Ho, C. Biochemistry (1991) [Pubmed]
  5. Monoclonal antibodies against the membrane-bound, flavin-linked D-lactate dehydrogenase of Escherichia coli: preparation, characterization, and use in immunoaffinity chromatography. Santos, E., Tahara, S.M., Kaback, H.R. Biochemistry (1985) [Pubmed]
  6. Characterization of (R)-2-Hydroxyisocaproate Dehydrogenase and a Family III Coenzyme A Transferase Involved in Reduction of L-Leucine to Isocaproate by Clostridium difficile. Kim, J., Darley, D., Selmer, T., Buckel, W. Appl. Environ. Microbiol. (2006) [Pubmed]
  7. Engineering Escherichia coli to improve culture performance and reduce formation of by-products during recombinant protein production under transient intermittent anaerobic conditions. Lara, A.R., Vazquez-Limón, C., Gosset, G., Bolívar, F., López-Munguía, A., Ramírez, O.T. Biotechnol. Bioeng. (2006) [Pubmed]
  8. A biochemical study of the reconstitution of D-lactate dehydrogenase-deficient membrane vesicles using fluorine-labeled components. Pratt, E.A., Jones, J.A., Cottam, P.F., Dowd, S.R., Ho, C. Biochim. Biophys. Acta (1983) [Pubmed]
 
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