Ajith V. Kamath

TL;DR: A new class of glutathione transferases has been discovered by analysis of the expressed sequence tag data base and sequence alignment, named Omega, which exhibit an unusual N-terminal extension that abuts the C terminus to form a novel structural unit.

TL;DR: Physiological studies of the cloned determinant, which has been named mefA for macrolide efflux, provide evidence for its mechanism of action in host bacteria, with results consistent with a hypothesis that the gene encodes a novel antiporter function which pumps erythromycin out of the cell.

TL;DR: Several proteins expressed in Escherichia coli with the N-terminus Gly-Ser-Ser-[His]6- consisted partly (up to 20%) of material with 178 Da of excess mass, sometimes accompanied by a smaller fraction with an excess 258 Da, which suggested that the +258-Da modification was addition of a 6-phosphogluconoyl group.

TL;DR: The Omega class of cytosolic glutathione transferases was initially recognized by bioinformatic analysis of human sequence databases, and orthologous sequences were subsequently discovered in mouse, rat, pig, Caenorhabditis elegans, Schistosoma mansoni, and Drosophila melanogaster.

TL;DR: The structure of the inhibitor complex provides a framework for developing more potent inhibitors of hSDH and an inhibitor that is competitive with fructose.