Purification and N-terminal amino acid sequence of solanapyrone synthase, a natural Diels-Alderase from Alternaria solani.
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.
Katayama
Kinya
K
School of Veterinary Medicine, Faculty of Veterinary Science, Nippon Veterinary and Life Science University, Musashino-shi, Tokyo 180-8602, Japan. kkatayam@nvlu.ac.jp
Kobayashi
Tomonori
T
Chijimatsu
Masao
M
Ichihara
Akitami
A
Oikawa
Hideaki
H
D000528:Alternaria / Q000201:enzymology*; D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D008025:Ligases / Q000737:chemistry / Q000302:isolation & purification*; D008969:Molecular Sequence Data
D008025:Ligases