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Graham DE , Bock CL , Schalk-Hihi C , Lu ZCJ , Markham GD
Identification of a highly diverged class of S- adenosylmethionine synthetases in the archaea
Journal of Biological Chemistry. 2000 Feb 11;275(6) :4055-4059
AbstractS-Adenosylmethionine is the primary alkylating agent in all known organisms. ATP:L-methionine S-adenosyl-transferase (MAT) catalyzes the only known biosynthetic: route to this central metabolite. Although the amino acid sequence of MAT is strongly conserved among bacteria and eukarya, no homologs have been recognized in the completed genome sequences of any archaea, In this study, MAT has been purified to homogeneity from the archaeon Methanococcus jannaschii, and the gene encoding it has been identified by mass spectrometry. The peptide mass map identifies the gene encoding MAT as MJ1208, a hypothetical open reading frame, The gene was cloned in Escherichia coli, and expressed enzyme has been purified and characterized. This protein has only 22 and 23% sequence identity to the E, coli and human enzymes, respectively, whereas those are 59% identical to each other. The few identical residues include the majority of those constituting the polar active site residues. Each complete archaeal genome sequence contains a homolog of this archaeal-type MAT. Surprisingly, three bacterial genomes encode both the archaeal and eukaryal/bacterial types of MAT. This identification of a second major class of MAT emphasizes the long evolutionary history of the archaeal lineage and the structural diversity found even in crucial metabolic enzymes.
NotesTimes Cited: 5 English Article 283RJ J BIOL CHEM