The building blocks of enzymatic and functional structures in living organisms are proteins created by linking amino acids into peptides (sub units of proteins). The mechanisms for creating peptides in proteins and some coenzymes are the clues that White and colleagues are following. "Enzymes that mechanistically do the same thing are included into a family, and we believe that there is an ancestral enzyme for this family," says David Graham, who was an NSF postdoctoral fellow in microbial biology at Virginia Tech.
In their attempt to reconstruct biochemical history, White's group has discovered two enzymes in Methanococcus jannaschii that may predate the cell's use of ribosome to build proteins. Their research will be reported in the Proceedings of the National Academy of Science (PNAS) by Hong Li, a post doc at Virginia Tech; Huimin Xu, a Virginia Tech technician, Graham, now at the University of Texas at Austin, and White, professor of biochemistry. The article (#3391), "Glutathione synthetase homologs encode a-L-glutamate ligases for methanogenic coenzyme F420 and tetrahydrosarcinapterin biosyntheses," will be published in the PNAS online Early Edition during the week of Monday, Aug. 4 Friday, Aug. 8, 2003.
"We found two enzymes, MptN and CofF, which are descendants of the ATP-grasp superfamily," says White.
The ATP superfamily is a group of enzymes that use ATP -- the nucleotide energy source for the cell. "ATP-grasp" refers to a shared nucleotide-binding method. Every self-sustaining, living organism ha
Contact: Dr. Robert H. White