title: (R)-mevalonate 3-phosphate is an intermediate of the mevalonate pathway in Thermoplasma acidophilum.
abstract: The lack of a few conserved enzymes in the classical mevalonate pathway and the widespread existence of isopentenyl phosphate kinase suggest the presence of a partly modified mevalonate pathway in most archaea and in some bacteria. In the pathway, (R)-mevalonate 5-phosphate is thought to be metabolized to isopentenyl diphosphate via isopentenyl phosphate. The long anticipated enzyme that catalyzes the reaction from (R)-mevalonate 5-phosphate to isopentenyl phosphate was recently identified in a Cloroflexi bacterium, Roseiflexus castenholzii, and in a halophilic archaeon, Haloferax volcanii. However, our trial to convert the intermediates of the classical and modified mevalonate pathways into isopentenyl diphosphate using cell-free extract from a thermophilic archaeon Thermoplasma acidophilum implied that the branch point intermediate of these known pathways, i.e. (R)-mevalonate 5-phosphate, is unlikely to be the precursor of isoprenoid. Through the process of characterizing the recombinant homologs of mevalonate pathway-related enzymes from the archaeon, a distant homolog of diphosphomevalonate decarboxylase was found to catalyze the phosphorylation of (R)-mevalonate to yield (R)-mevalonate 3-phosphate. The product could be converted into isopentenyl phosphate, probably through (R)-mevalonate 3,5-bisphosphate, by the action of unidentified T. acidophilum enzymes fractionated by anion-exchange chromatography. These findings demonstrate the presence of a third alternative "Thermoplasma-type" mevalonate pathway, which involves (R)-mevalonate 3-phosphotransferase and probably both (R)-mevalonate 3-phosphate 5-phosphotransferase and (R)-mevalonate 3,5-bisphosphate decarboxylase, in addition to isopentenyl phosphate kinase.
authors.affiliation: From the Department of Applied Molecular Bioscience, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, Aichi 464-8601 and.
authors.forename: Yasuhiro
authors.initials: Y
authors.lastname: Azami
authors.affiliation: From the Department of Applied Molecular Bioscience, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, Aichi 464-8601 and.
authors.forename: Ai
authors.initials: A
authors.lastname: Hattori
authors.affiliation: From the Department of Applied Molecular Bioscience, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, Aichi 464-8601 and.
authors.forename: Hiroto
authors.initials: H
authors.lastname: Nishimura
authors.affiliation: the Institute of Agriculture, Tokyo University of Agriculture and Technology, Saiwaicho 3-5-8, Fuchu, Tokyo 183-8509, Japan.
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Kawaide
authors.affiliation: From the Department of Applied Molecular Bioscience, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, Aichi 464-8601 and.
authors.forename: Tohru
authors.initials: T
authors.lastname: Yoshimura
authors.affiliation: From the Department of Applied Molecular Bioscience, Graduate School of Bioagricultural Sciences, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, Aichi 464-8601 and hhemmi@agr.nagoya-u.ac.jp.
authors.forename: Hisashi
authors.initials: H
authors.lastname: Hemmi
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D019843:Archaeal Proteins / Q000235:genetics / Q000378:metabolism; D001483:Base Sequence; D002474:Cell-Free System; D002852:Chromatography, Ion Exchange; D002855:Chromatography, Thin Layer; D017931:DNA Primers; D008798:Mevalonic Acid / Q000031:analogs & derivatives* / Q000378:metabolism*; D010802:Phylogeny; D013822:Thermoplasma / Q000378:metabolism*
chemical_list: D019843:Archaeal Proteins; D017931:DNA Primers; C045038:phosphomevalonic acid; D000255:Adenosine Triphosphate; D008798:Mevalonic Acid
keywords: Archaea; Biosynthesis; Enzyme; Isoprenoid; Metabolism
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