Effect of mutagenesis at the region upstream from the G(Q/E) motif of three types of geranylgeranyl diphosphate synthase on product chain-length(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

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概要

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• (All-E) geranylgeranyl diphosphate synthases have been classified into three types based on the characteristic sequences around the first aspartate rich motif, which is highly conserved among the enzymes. In type I geranylgeranyl diphosphate synthases, which consist of archaeal enzymes, a bulky amino acid residue at the 5th position upstream from the motif plays a main role in the product determination, by blocking further elongation of prenyl chain as the bottom of the reaction cavity. On the other hand, type III geranylgeranyl diphosphate synthases, which consist of the enzymes from eukaryotes except for plants, use a bulky amino acid residue at the 2nd position upstream from the conserved G(Q/E) motif for product chain-length determination. Thus we introduced mutations into the region upstream from the G(Q/E) motif of geranylgeranyl diphosphate synthases of the three different types to confirm the importance of the region for the product chain-length determination. The results of the mutational analyses indicated that not only the 2nd but also the 3rd position upstream from the G(Q/E) motif is involved in the product chain-length determination mechanism in types I and III geranylgeranyl diphosphate synthases, while the amino acid substitution in this region did not affect the chain-length of the products of type II geranylgeranyl diphosphate synthase, which consist of the enzymes from bacteria and plants. The region upstream from the G(Q/E) motif possibly contributes to the product determination in the wide range of geranylgeranyl diphosphate synthases, as well as that around the first aspartate rich motif.

• 社団法人日本生物工学会の論文

著者

• 西野 友年

  神戸大理

• Nishino Tokuzo

  Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University

• Nakayama Toru

  Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University

• Nishino T

  Department Of Biomolecular Engineering Graduate School Of Engineering Tohoku University

• KATAGIRI Takashi

  Department of Medicine, Division of Cardiology, Shown University School of Medicine

• Nishino Tokuzo

  Dep. Of Biochemistry And Engineering Graduate School Of Engineering Tohoku Univ. Aoba-yama Sendai Mi

• Hemmi H

  Tohoku Univ. Miyagi Jpn

• Hemmi Hisashi

  Department Of Biomolecular Engineering Graduate School Of Engineering Tohoku University

• Hemmi Hisashi

  Department Of Biochemistry And Engineering Tohoku University

• Hemmi Hisashi

  Dep. Of Biochemistry And Engineering Graduate School Of Engineering Tohoku Univ. Aoba-yama Sendai Mi

• Noike Motoyoshi

  Department of Biochemistry and Engineering, Graduate School of Engineering, Tohoku University

• Nakayama Toru

  Department Of Biomolecular Engineering Graduate School Of Engineering Tohoku University

• Katagiri Takashi

  Department Of Applied Chemistry Faculty Of Engineering Osaka University

• Hamada Hiroaki

  Department Of Life Science Faculty Of Science Okayama University Of Science

• Nishino Tokuzo

  Department Of Biochemistry And Engineering Faculty Of Engineering Tohoku University

• Katagiri Takashi

  Department Of Biochemistry And Engineering Graduate School Of Engineering Tohoku University

• Hemmi Hisashi

  Department Of Applied Molecular Biosciences Graduate School Of Bioagricultural Sciences Nagoya Unive

• Noike Motoyoshi

  Inst. Of Multidisciplinary Res. For Advanced Materials Tohoku Univ. Sendai 980-8577 Jpn

• NAKAYAMA Toru

  Department of Applied Microbial Technology, The Kumamoto Institute of Technology:(Present office)Institute for Fundamental Research, Suntory Ltd.

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