Divergent evolution of a Rossmann fold and identification of its oldest surviving ancestor. (12th June 2009)

• Record Type: Journal Article
• Authors: Duax, William L.; Huether, Robert; Pletnev, Vladimir; Umland, Timothy C.; , Charles M. Weeks
• Is Part Of: International journal of bioinformatics research and applications. Volume 5:Number 3(2009)
• Page Start: 280
• Page End: 294
• Publication Date: 2009-06-12
• Subjects: molecular evolution -- multiple open reading frames -- substrate prediction -- MORF -- beta-ketoacyl -- acyl carrier proteins -- reductase -- short chain oxidoreductase enzymes -- sdr -- tetramer assembly -- cofactor identification -- bioinformatics -- divergent evolution -- Rossmann fold -- fatty acid synthesis -- bacteria -- aromatic residue stacking -- oligomeric assembly; Bioinformatics -- Periodicals; 570.285
• Languages: English
• ISSNs: 1744-5485

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.