Jennifer L. Seffernick

TL;DR: The data strongly suggest that the 9 amino acid differences between melamine deaminase and AtzA represent a short evolutionary pathway connecting enzymes catalyzing physiologically relevant deamination and dehalogenation reactions, respectively.

TL;DR: It is shown that five geographically distinct atrazine-degrading bacteria contain genes homologous to atzA, -B, and -C, which indicates that globally distributed atrazines are highly conserved in diverse genera of bacteria.

TL;DR: The results of analyses using the SFLD are presented in correcting misannotations, guiding protein engineering experiments, and elucidating the function of recently solved enzyme structures from the structural genomics initiative.

TL;DR: Two highly homologous triazine hydrolases are shuffled and an exploration of the substrate specificities of the resulting enzymes are conducted to acquire a better understanding of the possible distributions of novel functions in sequence space.

TL;DR: The present study more fully defined the OleABCD protein families within the thiolase, α/β-hydrolase, AMP-dependent ligase/synthase, and short-chain dehydrogenase superfamilies, respectively, and proposed that OleA catalyzes a nondecarboxylative thiolytic condensation of fatty acyl chains to generate a β-ketoacyl intermediate that can decar boxylate spontaneously to generate ketones.