Effect of mutagenesis at the region upstream from the G(Q/E) motif of three types of geranylgeranyl diphosphate synthase on product chain-length

Effect of mutagenesis at the region upstream from the G(Q/E) motif of three types of geranylgeranyl diphosphate synthase on product chain-length

- Noike Motoyoshi NOIKE Motoyoshi
- Department of Biochemistry and Engineering, Graduate School of Engineering, Tohoku University
- Katagiri Takashi KATAGIRI Takashi
- Department of Biochemistry and Engineering, Graduate School of Engineering, Tohoku University
- Nakayama Toru [他] NAKAYAMA Toru
- Department of Biochemistry and Engineering, Graduate School of Engineering, Tohoku University
- NISHINO Tokuzo
- Department of Biochemistry and Engineering, Graduate School of Engineering, Tohoku University
- HEMMI Hisashi
- Department of Biochemistry and Engineering, Graduate School of Engineering, Tohoku University

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Author(s)

- Noike Motoyoshi NOIKE Motoyoshi
- Department of Biochemistry and Engineering, Graduate School of Engineering, Tohoku University
- Katagiri Takashi KATAGIRI Takashi
- Department of Biochemistry and Engineering, Graduate School of Engineering, Tohoku University
- Nakayama Toru [他] NAKAYAMA Toru
- Department of Biochemistry and Engineering, Graduate School of Engineering, Tohoku University
- NISHINO Tokuzo
- Department of Biochemistry and Engineering, Graduate School of Engineering, Tohoku University
- HEMMI Hisashi
- Department of Biochemistry and Engineering, Graduate School of Engineering, Tohoku University

Abstract

(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.

Journal

Journal of bioscience and bioengineering

Journal of bioscience and bioengineering 107(3), 235-239, 2009-03-25

The Society for Biotechnology, Japan

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Effect of mutagenesis at the region upstream from the G(Q/E) motif of three types of geranylgeranyl diphosphate synthase on product chain-length

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