Divergent evolution of a Rossmann fold and identification of its oldest surviving ancestor
by William L. Duax, Robert Huether, Vladimir Pletnev, Timothy C. Umland, Charles M. Weeks
International Journal of Bioinformatics Research and Applications (IJBRA), Vol. 5, No. 3, 2009

Abstract: β-ketoacyl (acyl carrier protein) reductase (β-k-ACPR) enzymes are essential to fatty acid synthesis in bacteria. The analyses revealed the most primitive member of the β-k-ACPRs family was a NADP reductase where NADP was recognised by a Thr residue in the β2α3 turn. Aromatic residue stacking at the dimer interface and a previously undetected conserved sequence at the C-terminus, stabilise the oligomeric assembly of these proteins. Our analysis indicates that the primordial members of the β-k-ACPR family probably arose in the α-proteobacteria and are characterised by the presence of multiple open reading frames and an extreme codon and amino acid bias.

Online publication date: Thu, 11-Jun-2009

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