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Gene Review:

lpdA - dihydrolipoamide dehydrogenase

Escherichia coli O157:H7 str. EDL933

Rinas, U. et al., Else, A.J. et al., Cicek, G. et al., Argyrou, A. et al., Seckler, R. et al.

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Disease relevance of lpdA

Mycobacterium tuberculosis lipoamide dehydrogenase is encoded by Rv0462 and not by the lpdA or lpdB genes [1].
The T. b. brucei dihydrolipoamide dehydrogenase gene has been expressed in Escherichia coli and the resultant protein purified; its N-terminus is processed in a similar fashion to that in the trypanosome, but with reduced specificity [2].
Antigens of isolated bovine heart mitochondria reacting with antibodies of myocarditis serum on two-dimensional Western blots were identified by MALDI-TOF and NanoESI mass spectrometry as myosin heavy chain beta and as dihydrolipoamide dehydrogenase of the mitochondrial 2-oxoacid dehydrogenase complexes [3].

High impact information on lpdA

On Western blots, antibodies raised against dihydrolipoamide dehydrogenase from the stereorarian trypanosome, Trypanosoma cruzi, cross-react strongly with the dihydrolipoamide dehydrogenase from all three T. brucei species; by this method, the relative molecular masses of their dihydrolipoamide dehydrogenases are indistinguishable [2].
These inclusion bodies additionally contain significant amounts of the heat-shock chaperone DnaK, and putative DnaK substrates such as the elongation factor Tu (ET-Tu) and the metabolic enzymes dihydrolipoamide dehydrogenase (LpdA), tryptophanase (TnaA), and d-tagatose-1,6-bisphosphate aldolase (GatY) [4].
Reassociation to a fully active complex molecule works with equal facility between the pyruvate dehydrogenase component and a dihydrolipoamide transacetylase: dihydrolipoamide dehydrogenase subcomplex from either organism in all possible combinations [5].

References

Mycobacterium tuberculosis lipoamide dehydrogenase is encoded by Rv0462 and not by the lpdA or lpdB genes. Argyrou, A., Blanchard, J.S. Biochemistry (2001) [Pubmed]
Dihydrolipoamide dehydrogenase in the trypanosoma subgenus, trypanozoon. Else, A.J., Clarke, J.F., Willis, A., Jackman, S.A., Hough, D.W., Danson, M.J. Mol. Biochem. Parasitol. (1994) [Pubmed]
Analysis of mitochondrial antigens reveals inner membrane succinate dehydrogenase flavoprotein subunit as autoantigen to antibodies in anti-M7 sera. Cicek, G., Schiltz, E., Hess, D., Staiger, J., Brandsch, R. Clin. Exp. Immunol. (2002) [Pubmed]
Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production in Escherichia coli. Rinas, U., Hoffmann, F., Betiku, E., Estap??, D., Marten, S. J. Biotechnol. (2007) [Pubmed]
Purification and properties of the pyruvate dehydrogenase complex from Salmonella typhimurium and formation of hybrids with the enzyme complex from Escherichia coli. Seckler, R., Binder, R., Bisswanger, H. Biochim. Biophys. Acta (1982) [Pubmed]

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