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Sueda, S. et al.

Sueda, Islam, Kondo,

Protein engineering of pyruvate carboxylase: investigation on the function of acetyl-CoA and the quaternary structure.

Pyruvate carboxylase (PC) from Bacillus thermodenitrificans was engineered in such a way that the polypeptide chain was divided into two, between the biotin carboxylase ( BC) and carboxyl transferase (CT) domains. The two proteins thus formed, PC-(BC) and PC-(CT+BCCP), retained their catalytic activity as assayed by biotin-dependent ATPase and oxamate-dependent oxalacetate decarboxylation, for the former and the latter, respectively. Neither activity was dependent on acetyl-CoA, in sharp contrast to the complete reaction of intact PC. When assessed by gel filtration chromatography, PC-(BC) was found to exist either in dimers or monomers, depending on the protein concentration, while PC-(CT + BCCP) occurred in dimers for the most part. The two proteins do not associate spontaneously or in the presence of acetyl-CoA. Based on these observations, this paper discusses how the tetrameric structure of PC is built up and how acetyl-CoA modulates the protein structure.[1]

References

Protein engineering of pyruvate carboxylase: investigation on the function of acetyl-CoA and the quaternary structure. Sueda, S., Islam, M.N., Kondo, H. Eur. J. Biochem. (2004) [Pubmed]

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