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Volumn 121, Issue 4, 1997, Pages 696-704

Effects of random mutagenesis in a putative substrate-binding domain of geranylgeranyl diphosphate synthase upon intermediate formation and substrate specificity

Author keywords

Enzyme mechanism; Farnesyl diphosphate; Geranylgeranyl diphosphate synthase; Isoprenoids; Prenyltransferase

Indexed keywords

DIMETHYLALLYLTRANSFERASE; FARNESYL TRANS TRANSFERASE; SYNTHETASE;

EID: 0030940428     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021642     Document Type: Article
Times cited : (13)

References (23)
  • 1
    • 0028088478 scopus 로고
    • Purification and properties of geranylgeranyl-diphosphate synthase from bovine brain
    • Sagami, H., Morita, Y., and Ogura, K. (1994) Purification and properties of geranylgeranyl-diphosphate synthase from bovine brain. J. Biol. Chem. 269, 20561-20566
    • (1994) J. Biol. Chem. , vol.269 , pp. 20561-20566
    • Sagami, H.1    Morita, Y.2    Ogura, K.3
  • 2
    • 0029157321 scopus 로고
    • BTS1 encodes a geranylgeranyl diphosphate synthase in Saccharomyces cerevisae
    • Jiang, Y., Proteau, P., Poulter, C.D., and Ferro-Novick, S. (1995) BTS1 encodes a geranylgeranyl diphosphate synthase in Saccharomyces cerevisae. J. Biol. Chem. 270, 21793-21799
    • (1995) J. Biol. Chem. , vol.270 , pp. 21793-21799
    • Jiang, Y.1    Proteau, P.2    Poulter, C.D.3    Ferro-Novick, S.4
  • 3
    • 0028269724 scopus 로고
    • Isoprunyl diphosphate synthase: Protein scquenvu comparison, a phylogenetic tree, and predictions of secondary structure
    • Chen, A., Kroon, P.A., and Poulter, C.D. (1994) Isoprunyl diphosphate synthase: Protein scquenvu comparison, a phylogenetic tree, and predictions of secondary structure. Protein Sci. 3, 600-607
    • (1994) Protein Sci. , vol.3 , pp. 600-607
    • Chen, A.1    Kroon, P.A.2    Poulter, C.D.3
  • 4
    • 0028283930 scopus 로고
    • Arehacbacterial ether-linked biosynthetic: Gene. Expression cloning, sequencing, and characterization of geranylgeranyl diphosphate synthase
    • Ohnuma, S.-i., Suzuki, M., and Nishino, T. (1994) Arehacbacterial ether-linked biosynthetic: gene. Expression cloning, sequencing, and characterization of geranylgeranyl diphosphate synthase. J. Biol. Chem. 209, 14792-14797
    • (1994) J. Biol. Chem. , vol.209 , pp. 14792-14797
    • Ohnuma, S.-I.1    Suzuki, M.2    Nishino, T.3
  • 5
    • 0027217518 scopus 로고
    • Purification and characterization of famesyl diphosphate/geranylgeranyl diphosphate syn- Thase
    • Chen, A. and Poulter, C.D. (1993) Purification and characterization of famesyl diphosphate/geranylgeranyl diphosphate syn- thase. J. Biol. Chem. 268, 11002-11007
    • (1993) J. Biol. Chem. , vol.268 , pp. 11002-11007
    • Chen, A.1    Poulter, C.D.2
  • 6
    • 0000291597 scopus 로고
    • Purification and characterization of geranylgoranyl diphosphate synthase from Methanobacterium thermoformicicum SF-4
    • Tnchibana, A., Tanaka, T., Taniguchi, M., and Oi, S. (1993) Purification and characterization of geranylgoranyl diphosphate synthase from Methanobacterium thermoformicicum SF-4. Biosci. Biotech. Biochem. 57, 1129-1133
    • (1993) Biosci. Biotech. Biochem. , vol.57 , pp. 1129-1133
    • Tnchibana, A.1    Tanaka, T.2    Taniguchi, M.3    Oi, S.4
  • 7
    • 0027054065 scopus 로고
    • Chain length distribution of the products formed in solanesyl diphosphate synthase reaction
    • Ohnuma, S.-i., Koyama, T., and Ogura, K. (1992) Chain length distribution of the products formed in solanesyl diphosphate synthase reaction. J. Biochem. 112, 743-749
    • (1992) J. Biochem. , vol.112 , pp. 743-749
    • Ohnuma, S.-I.1    Koyama, T.2    Ogura, K.3
  • 8
    • 0025793572 scopus 로고
    • Variable product specificity of microsomal dehydrodolichyl diphosphate synthase from rat liver
    • Matsuoka, S., Sagami, H., Kurisaki, A., and Ogura, K (1991) Variable product specificity of microsomal dehydrodolichyl diphosphate synthase from rat liver. J. Biol. Chem. 266, 3464-3468
    • (1991) J. Biol. Chem. , vol.266 , pp. 3464-3468
    • Matsuoka, S.1    Sagami, H.2    Kurisaki, A.3    Ogura, K.4
  • 12
    • 0020482354 scopus 로고
    • Efficient enzymatic hydrolysis of polyprenyl pyrophosphate
    • Fujii, H., Koyama, T., and Ogura, K. (1982) Efficient enzymatic hydrolysis of polyprenyl pyrophosphate. Biochim. Biophys. Acta 712, 716-718
    • (1982) Biochim. Biophys. Acta , vol.712 , pp. 716-718
    • Fujii, H.1    Koyama, T.2    Ogura, K.3
  • 13
    • 0019886899 scopus 로고
    • Isolation and characterization of a photoaffinity-labeled peptide from the catalytic site of prenyltransferase
    • Krems, D.N., Bruenger, E., and Rilling, H.C. (1981) Isolation and characterization of a photoaffinity-labeled peptide from the catalytic site of prenyltransferase. Biochemistry 20, 3711-3718
    • (1981) Biochemistry , vol.20 , pp. 3711-3718
    • Krems, D.N.1    Bruenger, E.2    Rilling, H.C.3
  • 14
    • 0018787394 scopus 로고
    • Prenyltransferase. Kinetic studies of the 1-4 coupling reaction with avian liver enzyme
    • Laskovics, F.M., Krafcik, J.M., and Poultor, C.P. (1979) Prenyltransferase. Kinetic studies of the 1-4 coupling reaction with avian liver enzyme. J. Biol. Chem. 254, 9458-9463
    • (1979) J. Biol. Chem. , vol.254 , pp. 9458-9463
    • Laskovics, F.M.1    Krafcik, J.M.2    Poultor, C.P.3
  • 15
    • 0019471750 scopus 로고
    • Prenyltransferase: Determination of the binding mechanism und individual kinetic constants for farnesylpyrophosphate synthase by rapid quen and isotope partitioning experiments
    • Laskovics, F.M. and Poulter, C.D. (1981) Prenyltransferase: Determination of the binding mechanism und individual kinetic constants for farnesylpyrophosphate synthase by rapid quen and isotope partitioning experiments. Biochemistry 20, 1889-1901
    • (1981) Biochemistry , vol.20 , pp. 1889-1901
    • Laskovics, F.M.1    Poulter, C.D.2
  • 16
    • 0025752779 scopus 로고
    • Formation of Z,E,E-geranylgeranyl diphosphate by rat liver microsomes
    • Sagami, H., Matsuoka, S., and Ogura, K. (1991) Formation of Z,E,E-geranylgeranyl diphosphate by rat liver microsomes. Biol. Chem. 268, 3458-3463
    • (1991) Biol. Chem. , vol.268 , pp. 3458-3463
    • Sagami, H.1    Matsuoka, S.2    Ogura, K.3
  • 17
    • 0018782967 scopus 로고
    • Photoaffinity labeling of the catalytic site of prenyltransferase
    • Brems, D.N. and Rilling, H.C. (1979) Photoaffinity labeling of the catalytic site of prenyltransferase, Biochemiatry 18, 860-884
    • (1979) Biochemiatry , vol.18 , pp. 860-884
    • Brems, D.N.1    Rilling, H.C.2
  • 18
    • 0028145239 scopus 로고
    • Crystal structure of recombinant farnesyl diphosphate synthase at 2.6 A resolution
    • Tarshis, L.C., Van, M., Poulter, C.D., and Sacchettini, J.C. (1994) Crystal structure of recombinant farnesyl diphosphate synthase at 2.6 A resolution. Biochemistry 33, 10871-10877
    • (1994) Biochemistry , vol.33 , pp. 10871-10877
    • Tarshis, L.C.1    Van, M.2    Poulter, C.D.3    Sacchettini, J.C.4
  • 19
    • 0025367745 scopus 로고
    • Isolation and properties of yeast mutants affected in farnesyl diphosphute synthase
    • Chambon, C., Ladeveze, V., Oulmouden, A., Servouse, M., and Karst, K. (1990) Isolation and properties of yeast mutants affected in farnesyl diphosphute synthase. Curr. Genet. 18, 41-46
    • (1990) Curr. Genet. , vol.18 , pp. 41-46
    • Chambon, C.1    Ladeveze, V.2    Oulmouden, A.3    Servouse, M.4    Karst, K.5
  • 20
    • 0025871657 scopus 로고
    • Sterol pathway is yeast. Identification and properties of mutant strains defective in mevalonate diphosphate docurboxylasc and farnesyl diphosphate synthetase
    • Chambon, C., Ludevozc, V., Servouse, M., Blanohard, L., Juvelot, C., Vladescu, B., and Karst, K. (1991) Sterol pathway is yeast. Identification and properties of mutant strains defective in mevalonate diphosphate docurboxylasc and farnesyl diphosphate synthetase. Lipids 26, 633-636
    • (1991) Lipids , vol.26 , pp. 633-636
    • Chambon, C.1    Ludevozc, V.2    Servouse, M.3    Blanohard, L.4    Juvelot, C.5    Vladescu, B.6    Karst, K.7
  • 21
    • 15144351108 scopus 로고
    • Characterization of a lysineto-glutamic acid mutation in a conservative secquence of farnesyl diphosphate synthase from Saechurumyes cerevisiae
    • Blanchard, L. and Karst, K. (1993) Characterization of a lysineto-glutamic acid mutation in a conservative secquence of farnesyl diphosphate synthase from Saechurumyes cerevisiae. Gene 128, 180-180
    • (1993) Gene , vol.128 , pp. 180-180
    • Blanchard, L.1    Karst, K.2
  • 22
    • 0029880618 scopus 로고    scopus 로고
    • Conversion from farnesyl diphosphate synthase to geranylgeranyl diphosphate synthase by random chemical mutauenesis
    • Ohnuma, S.-i., Nakanawa, T., Hemmi, H., Hallberg, A.-M., Koyama, T., Ogyura, K., and Nishino, T. (1996) Conversion from farnesyl diphosphate synthase to geranylgeranyl diphosphate synthase by random chemical mutauenesis. J. Biol. Chem. 271, 10087-10095
    • (1996) J. Biol. Chem. , vol.271 , pp. 10087-10095
    • Ohnuma, S.-I.1    Nakanawa, T.2    Hemmi, H.3    Hallberg, A.-M.4    Koyama, T.5    Ogyura, K.6    Nishino, T.7
  • 23
    • 0029785708 scopus 로고    scopus 로고
    • Conversion of product specificity of archacbacto rial geranylgeranyl-diphosphate synthase. Identification of essential amino acid residues for chain lenph determination of prenyltransferase reaction
    • Ohnuma, S.-i., Hirooka, K., Hemmi, H., Ishida, C., Ohio, C., and Nishinu, T. (1996) Conversion of product specificity of archacbacto rial geranylgeranyl-diphosphate synthase. Identification of essential amino acid residues for chain lenph determination of prenyltransferase reaction. J. Biol. Chem. 271, 18831-18837
    • (1996) J. Biol. Chem. , vol.271 , pp. 18831-18837
    • Ohnuma, S.-I.1    Hirooka, K.2    Hemmi, H.3    Ishida, C.4    Ohio, C.5    Nishinu, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.