Interconversion of product specificity of typeI eubacterial farnesyl diphosphate synthase and geranylgeranyl diphosphate synthase by one amino acid substitution
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- Kawasaki Takashi
- Biotechnology Research Center, Toyama Prefectural University
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- Hamano Yoshimitsu
- Biotechnology Research Center, Toyama Prefectural University
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- Kuzuyama Tomohisa
- Institute of Molecular and Cellular Biosciences, The University of Tokyo
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- Itoh Nobuya
- Biotechnology Research Center, Toyama Prefectural University
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- Seto Haruo
- Faculty of Applied Bio-science, Tokyo University of Agriculture
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- Dairi Tohru
- Biotechnology Research Center, Toyama Prefectural University
書誌事項
- タイトル別名
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- Interconversion of the Product Specificity of Type I Eubacterial Farnesyl Diphosphate Synthase and Geranylgeranyl Diphosphate Synthase through One Amino Acid Substitution
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抄録
Prenyltransferases catalyze the sequential condensation of isopentenyl diphosphate into prenyl diphosphates with specific chain lengths. Pioneering studies demonstrated that the product specificities of type I prenyltransferases were mainly determined by the amino acid residues at the 4th and 5th positions before the first aspartate-rich motif (FARM) of the prenyltransferases. We previously cloned a type I geranylgeranyl diphosphate synthase (GGDPSase) gene from Streptomyces griseolosporeus MF730-N6 [Hamano, Y., Dairi, T., Yamamoto, M., Kawasaki, T., Kaneda, K., Kuzuyama, T., Itoh, N., and Seto, H. (2001) Biosci. Biotechnol. Biochem. 65, 1627-1635]. In this study, a prenyltransferase gene was cloned from Streptomyces argenteolus A-2 and was confirmed to encode a type I farnesyl diphosphate synthase (FDPSase). Interestingly, the amino acid residues at the 4th and 5th positions before the FARM were the same in these two enzymes. To identify the amino acid that determines the product chain length, mutated enzymes, GGDPSase (L-50S), FDPSase (S-50L), GGDPSase (V-8A), FDPSase (A-8V), GGDPSase (A+57L), and FDPSase (L+58A), in which the amino acid residue at the -50th, -8th, and +57th (58th) position before or after the FARM was substituted with the corresponding amino acid of the other enzyme, were constructed. The GGDPSase (A+57L) and FDPSase (L+58A) produced farnesyl diphosphate and geranylgeranyl diphosphate, respectively. On the other hand, the other mutated enzymes produced prenyl diphosphates with the same chain lengths as the wild type enzymes did. These results showed that the amino acid residue at the 57th (58th) position after the FARM also played an important role in determination of the product specificity.
収録刊行物
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- The Journal of Biochemistry
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The Journal of Biochemistry 133 (1), 83-91, 2003
社団法人 日本生化学会
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詳細情報 詳細情報について
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- CRID
- 1390282679908857984
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- NII論文ID
- 10012052284
- 130003534488
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- NII書誌ID
- AA00694073
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- COI
- 1:CAS:528:DC%2BD3sXitlOku7Y%3D
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- ISSN
- 17562651
- 0021924X
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- NDL書誌ID
- 6430806
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- PubMed
- 12761202
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- 使用不可