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Gene Review:

ldhA - D-lactate dehydrogenase

Escherichia coli UTI89

Smith, G.M. et al., Lara, A.R. et al., Kim, J. et al.

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Disease relevance of ldhA

DL: -Alanine was produced from glucose in an Escherichia coli pfl pps poxB ldhA aceEF pTrc99A-alaD strain which lacked pyruvate-formate lyase, phosphoenolpyruvate (PEP) synthase, pyruvate oxidase, lactate dehydogenase, components of the pyruvate dehydogenase complex and over-produced alanine dehydrogenase (ALD) [1].

High impact information on ldhA

Deduced amino acid sequences of ldhA and hadA from the genome of C. difficile showed high identities to d-lactate dehydrogenase and family III CoA transferase, respectively [2].
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 [3].

References

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]
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]
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]

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