Unification of biosynthetic pathways of a variety of plant polyketides

2015 Fiscal Year Final Research Report

• Project/Area Number: 25242067
• Research Category: Grant-in-Aid for Scientific Research (A)
• Allocation Type: Single-year Grants
• Section: 一般
• Research Field: Biomolecular chemistry
• Research Institution: University of Shizuoka
• Principal Investigator: Noguchi Hiroshi 静岡県立大学, 薬学部, 教授 (60126141)
• Co-Investigator(Kenkyū-buntansha): MORITA HIROYUKI 富山大学, 和漢医薬学総合研究所, 教授 (20416663) ; UMEHARA KAORU 静岡県立大学, 薬学部, 講師 (40185070) ; WATANABE KENJI 静岡県立大学, 薬学部, 教授 (50360938)
• Project Period (FY): 2013-04-01 – 2016-03-31
• Keywords: ポリケタイド / 生合成 / 反応機構 / タンパク質結晶構造解析 / 植物 / 酵素工学

Outline of Final Research Achievements

We showed the possibility that tyrosine 72 and histidine 78 was a catalyst residue of OAC from analysis and a variation introduction experiment of the complex X-rays crystal structure with the Oribe Thor acid which was Oribe Thor acid closure enzyme (OAC) derived from hemp and the product. Furthermore, We clarified what enzyme activity attenuated when bulky substituted the amino acid residue which formed a pentyl-binding pocket full of the hydrophobicity that we found in an active site of OAC for a higher bulky residue. Based on the X-ray crystallographic analysis about these variation enzymes, the capacity of the pentyl-binding pocket decreased by introduction of the variation, and a substrate became hard to be connected, it became clear to attenuate enzyme activity.

Free Research Field

天然物化学