title: Purification and N-terminal amino acid sequence of solanapyrone synthase, a natural Diels-Alderase from Alternaria solani.
abstract: The first natural Diels-Alderase, solanapyrone synthase, was purified 1,630-fold from a crude extract. The 41-kDa protein on SDS-polyacrylamide gel electrophoresis was identified as truncated solanapyrone synthase, and its N-terminal amino acid sequence was found to be QETQNLNNFLESNAINP.
authors.affiliation: School of Veterinary Medicine, Faculty of Veterinary Science, Nippon Veterinary and Life Science University, Musashino-shi, Tokyo 180-8602, Japan. kkatayam@nvlu.ac.jp
authors.forename: Kinya
authors.initials: K
authors.lastname: Katayama
authors.forename: Tomonori
authors.initials: T
authors.lastname: Kobayashi
authors.forename: Masao
authors.initials: M
authors.lastname: Chijimatsu
authors.forename: Akitami
authors.initials: A
authors.lastname: Ichihara
authors.forename: Hideaki
authors.initials: H
authors.lastname: Oikawa
mesh_terms: D000528:Alternaria / Q000201:enzymology*; D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D008025:Ligases / Q000737:chemistry / Q000302:isolation & purification*; D008969:Molecular Sequence Data
chemical_list: D008025:Ligases