Identification of coenzyme M biosynthetic phosphosulfolactate synthase: a new family of sulfonate-biosynthesizing enzymes.
Authors Graham David E; Xu Huimin; White Robert H;
JournalJ Biol Chem
PubMed ID11830598
'The hyperthermophilic euryarchaeon Methanococcus jannaschii uses coenzyme M (2-mercaptoethanesulfonic acid) as the terminal methyl carrier in methanogenesis. We describe an enzyme from that organism, (2R)-phospho-3-sulfolactate synthase (ComA), that catalyzes the first step in coenzyme M biosynthesis. ComA catalyzed the stereospecific Michael addition of sulfite to phosphoenolpyruvate over a broad range ... More
Identification of amino acid residues critical for biological activity in human interleukin-18.
Authors Kim Soo-Hyun; Azam Tania; Novick Daniela; Yoon Do-Young; Reznikov Leonid L; Bufler Philip; Rubinstein Menachem; Dinarello Charles A;
JournalJ Biol Chem
PubMed ID11790772
Interleukin-18 (IL-18) is a pro-inflammatory cytokine, and IL-18-binding protein (IL-18BP) is a naturally occurring protein that binds IL-18 and neutralizes its biological activities. Computer modeling of human IL-18 identified two charged residues, Glu-42 and Lys-89, which interact with oppositely charged amino acid residues buried in a large hydrophobic pocket of ... More