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Volumn 297, Issue 5, 2002, Pages 1096-1101

Change of product specificity of hexaprenyl diphosphate synthase from sulfolobus solfataricus by introducing mimetic mutations

Author keywords

Archaeal enzyme; Chain length determination; Evolution; Hexaprenyl diphosphate synthase; Isoprenoid; Mimetic mutation; Mutagenesis; Prenyl diphosphate synthase; Prenyltransferase; Terpenoid

Indexed keywords

BACTERIAL ENZYME; GERANYLTRANSFERASE; HEXAPRENYLPYROPHOSPHATE SYNTHETASE; UNCLASSIFIED DRUG;

EID: 0036400595     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(02)02348-3     Document Type: Article
Times cited : (6)

References (19)
  • 1
    • 11544324496 scopus 로고    scopus 로고
    • Enzymatic aspects of isoprenoid chain elongation
    • K. Ogura, T. Koyama, Enzymatic aspects of isoprenoid chain elongation, Chem. Rev. 98 (1998) 1263-1276.
    • (1998) Chem. Rev. , vol.98 , pp. 1263-1276
    • Ogura, K.1    Koyama, T.2
  • 2
    • 0033202922 scopus 로고    scopus 로고
    • Molecular analysis of prenyl chain elongating enzymes
    • T. Koyama, Molecular analysis of prenyl chain elongating enzymes, Biosci. Biotechnol. Biochem. 63 (1999) 1671-1676.
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 1671-1676
    • Koyama, T.1
  • 3
    • 0027503220 scopus 로고
    • Thermostable farnesyl diphosphate synthase of Bacillus stearothermophilus: Molecular cloning, sequence determination, overproduction, and purification
    • T. Koyama, S. Obata, M. Osabe, A. Takeshita, K. Yokoyama, M. Uchida, T. Nishino, K. Ogura, Thermostable farnesyl diphosphate synthase of Bacillus stearothermophilus: molecular cloning, sequence determination, overproduction, and purification, J. Biochem. 113 (1993) 355-363.
    • (1993) J. Biochem. , vol.113 , pp. 355-363
    • Koyama, T.1    Obata, S.2    Osabe, M.3    Takeshita, A.4    Yokoyama, K.5    Uchida, M.6    Nishino, T.7    Ogura, K.8
  • 4
    • 0028269724 scopus 로고
    • Isoprenyl diphosphate synthases: Protein sequence comparisons, a phylogenetic tree, and predictions of secondary structure
    • A. Chen, P.A. Kroon, C.D. Poulter, Isoprenyl diphosphate synthases: protein sequence comparisons, a phylogenetic tree, and predictions of secondary structure, Protein Sci. 3 (1994) 600-607.
    • (1994) Protein Sci. , vol.3 , pp. 600-607
    • Chen, A.1    Kroon, P.A.2    Poulter, C.D.3
  • 5
    • 0028145239 scopus 로고
    • Crystal structure of recombinant farnesyl diphosphate synthase at 2.6-Å resolution
    • L.C. Tarshis, M. Yan, C.D. Poulter, J.C. Sacchettini, Crystal structure of recombinant farnesyl diphosphate synthase at 2.6-Å resolution, Biochemistry 33 (1994) 10871-10877.
    • (1994) Biochemistry , vol.33 , pp. 10871-10877
    • Tarshis, L.C.1    Yan, M.2    Poulter, C.D.3    Sacchettini, J.C.4
  • 6
    • 0029880618 scopus 로고    scopus 로고
    • Conversion from farnesyl diphosphate synthase to geranylgeranyl diphosphate synthase by random chemical mutagenesis
    • S.-i. Ohnuma, T. Nakazawa, H. Hemmi, A.M. Hallberg, T. Koyama, K. Ogura, T. Nishino, Conversion from farnesyl diphosphate synthase to geranylgeranyl diphosphate synthase by random chemical mutagenesis, J. Biol. Chem. 271 (1996) 10087-10095.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10087-10095
    • Ohnuma, S.-I.1    Nakazawa, T.2    Hemmi, H.3    Hallberg, A.M.4    Koyama, T.5    Ogura, K.6    Nishino, T.7
  • 7
    • 0029804201 scopus 로고    scopus 로고
    • A role of the amino acid residue located on the fifth position before the first aspartate-rich motif of farnesyl diphosphate synthase on determination of the final product
    • S.-i. Ohnuma, K. Narita, T. Nakazawa, C. Ishida, Y. Takeuchi, C. Ohto, T. Nishino, A role of the amino acid residue located on the fifth position before the first aspartate-rich motif of farnesyl diphosphate synthase on determination of the final product, J. Biol. Chem. 271 (1996) 30748-30754.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30748-30754
    • Ohnuma, S.-I.1    Narita, K.2    Nakazawa, T.3    Ishida, C.4    Takeuchi, Y.5    Ohto, C.6    Nishino, T.7
  • 8
    • 0029785708 scopus 로고    scopus 로고
    • Conversion of product specificity of archaebacterial geranylgeranyl-diphosphate synthase. Identification of essential amino acid residues for chain length determination of prenyl-transferase reaction
    • S.-i. Ohnuma, K. Hirooka, H. Hemmi, C. Ishida, C. Ohto, T. Nishino, Conversion of product specificity of archaebacterial geranylgeranyl-diphosphate synthase. Identification of essential amino acid residues for chain length determination of prenyl-transferase reaction, J. Biol. Chem. 271 (1996) 18831-18837.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18831-18837
    • Ohnuma, S.-I.1    Hirooka, K.2    Hemmi, H.3    Ishida, C.4    Ohto, C.5    Nishino, T.6
  • 9
    • 0031040182 scopus 로고    scopus 로고
    • Conversion from archaeal geranylgeranyl diphosphate synthase to farnesyl diphosphate synthase. Two amino acids before the first aspartate-rich motif solely determine eukaryotic farnesyl diphosphate synthase activity
    • S.-i. Ohnuma, K. Hirooka, C. Ohto, T. Nishino, Conversion from archaeal geranylgeranyl diphosphate synthase to farnesyl diphosphate synthase. Two amino acids before the first aspartate-rich motif solely determine eukaryotic farnesyl diphosphate synthase activity, J. Biol. Chem. 272 (1997) 5192-5198.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5192-5198
    • Ohnuma, S.-I.1    Hirooka, K.2    Ohto, C.3    Nishino, T.4
  • 10
    • 0032500606 scopus 로고    scopus 로고
    • A pathway where polyprenyl diphosphate elongates in prenyltransferase. Insight into a common mechanism of chain length determination of prenyltransferases
    • S.-i. Ohnuma, K. Hirooka, N. Tsuruoka, M. Yano, C. Ohto, H. Nakane, T. Nishino, A pathway where polyprenyl diphosphate elongates in prenyltransferase. Insight into a common mechanism of chain length determination of prenyltransferases, J. Biol. Chem. 273 (1998) 26705-26713.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26705-26713
    • Ohnuma, S.-I.1    Hirooka, K.2    Tsuruoka, N.3    Yano, M.4    Ohto, C.5    Nakane, T.6    Nishino, T.7
  • 12
    • 0032844334 scopus 로고    scopus 로고
    • Protein design of geranyl diphosphate synthase. Structural features that define the product specificities of prenyltransferases
    • K. Narita, S. Ohnuma, T. Nishino, Protein design of geranyl diphosphate synthase. Structural features that define the product specificities of prenyltransferases, J. Biochem. 126 (1999) 566-571.
    • (1999) J. Biochem. , vol.126 , pp. 566-571
    • Narita, K.1    Ohnuma, S.2    Nishino, T.3
  • 13
    • 0036170930 scopus 로고    scopus 로고
    • Novel medium-chain prenyl diphosphate synthase from the thermoacidophilic archaeon Sulfolobus solfataricus
    • H. Hemmi, S. Ikejiri, S. Yamashita, T. Nishino, Novel medium-chain prenyl diphosphate synthase from the thermoacidophilic archaeon Sulfolobus solfataricus, J. Bacteriol. 184 (2002) 615-620.
    • (2002) J. Bacteriol. , vol.184 , pp. 615-620
    • Hemmi, H.1    Ikejiri, S.2    Yamashita, S.3    Nishino, T.4
  • 15
    • 0020482354 scopus 로고
    • Efficient enzymatic hydrolysis of polyprenyl pyrophosphates
    • H. Fujii, T. Koyama, K. Ogura, Efficient enzymatic hydrolysis of polyprenyl pyrophosphates, Biochim. Biophys. Acta 712 (1982) 716-718.
    • (1982) Biochim. Biophys. Acta , vol.712 , pp. 716-718
    • Fujii, H.1    Koyama, T.2    Ogura, K.3
  • 16
    • 0033942062 scopus 로고    scopus 로고
    • Mechanism of product chain length determination for heptaprenyl diphosphate synthase from Bacillus stearothermophilus
    • K. Hirooka, S. Ohnuma, A. Koike-Takeshita, T. Koyama, T. Nishino, Mechanism of product chain length determination for heptaprenyl diphosphate synthase from Bacillus stearothermophilus, Eur. J. Biochem. 267 (2000) 4520-4528.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4520-4528
    • Hirooka, K.1    Ohnuma, S.2    Koike-Takeshita, A.3    Koyama, T.4    Nishino, T.5
  • 17
    • 0032127476 scopus 로고    scopus 로고
    • Molecular cloning and mutational analysis of the ddsA gene encoding decaprenyl diphosphate synthase from Gluconobacter suboxydans
    • K. Okada, T. Kainou, K. Tanaka, T. Nakagawa, H. Matsuda, M. Kawamukai, Molecular cloning and mutational analysis of the ddsA gene encoding decaprenyl diphosphate synthase from Gluconobacter suboxydans, Eur. J. Biochem. 255 (1998) 52-59.
    • (1998) Eur. J. Biochem. , vol.255 , pp. 52-59
    • Okada, K.1    Kainou, T.2    Tanaka, K.3    Nakagawa, T.4    Matsuda, H.5    Kawamukai, M.6
  • 18
    • 0033539554 scopus 로고    scopus 로고
    • Geranyl diphosphate synthase: Cloning, expression, and characterization of this prenyl-transferase as a heterodimer
    • C.C. Burke, M.R. Wildung, R. Croteau, Geranyl diphosphate synthase: cloning, expression, and characterization of this prenyl-transferase as a heterodimer, Proc. Natl. Acad. Sci. USA 96 (1999) 13062-13067.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13062-13067
    • Burke, C.C.1    Wildung, M.R.2    Croteau, R.3
  • 19
    • 0036479223 scopus 로고    scopus 로고
    • Interaction with the small subunit of geranyl diphosphate synthase modifies the chain length specificity of geranylgeranyl diphosphate synthase to produce eranyl diphosphate
    • C. Burke, R. Croteau, Interaction with the small subunit of geranyl diphosphate synthase modifies the chain length specificity of geranylgeranyl diphosphate synthase to produce eranyl diphosphate, J. Biol. Chem. 277 (2002) 3141-3149.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3141-3149
    • Burke, C.1    Croteau, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.