메뉴 건너뛰기




Volumn 66, Issue 4, 2002, Pages 808-819

Growth-phase dependent expression of the mevalonate pathway in a terpenoid antibiotic-producing streptomyces strain

Author keywords

Mevalonate pathway; Northern blotting; Streptomyces; Terpenoid; Terpentecin

Indexed keywords

ESCHERICHIA COLI; KITASATOSPORA GRISEOLA; STREPTOMYCES;

EID: 0036545358     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.66.808     Document Type: Article
Times cited : (38)

References (51)
  • 4
    • 0028837082 scopus 로고
    • Biochemistry and molecular biology of the isoprenoid biosynthetic pathways in plants
    • Chappell, J., Biochemistry and molecular biology of the isoprenoid biosynthetic pathways in plants. Annu. Rev. Plant Physiol. Plant Mol. Biol., 46, 521-547 (1995).
    • (1995) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.46 , pp. 521-547
    • Chappell, J.1
  • 5
    • 0021765976 scopus 로고
    • Isolation and characterization of yeast mutants blocked in mevalonic acid formation
    • Servouse, M., Mons, N., Baillaargeat, J.-L., and Karst, F., Isolation and characterization of yeast mutants blocked in mevalonic acid formation. Biochem. Biophy. Res. Com., 123, 424-430 (1984).
    • (1984) Biochem. Biophy. Res. Com. , vol.123 , pp. 424-430
    • Servouse, M.1    Mons, N.2    Baillaargeat, J.-L.3    Karst, F.4
  • 6
    • 0032170425 scopus 로고    scopus 로고
    • The deox-yxylulose phosphate pathway of terpenoid biosynthesis in plants and microorganisms
    • Eisenreich, W., Schwarz, M., Catayrade, A., Arigoni, D., Zenk, M. H., and Bacher, A., The deox-yxylulose phosphate pathway of terpenoid biosynthesis in plants and microorganisms. Chem. Biol., 5, R221-R233 (1998).
    • (1998) Chem. Biol. , vol.5 , pp. R221-R233
    • Eisenreich, W.1    Schwarz, M.2    Catayrade, A.3    Arigoni, D.4    Zenk, M.H.5    Bacher, A.6
  • 7
    • 0031464024 scopus 로고    scopus 로고
    • Studies on the biosynthesis of terpenoidal compounds produced by Actinomycetes. 2. Biosynthesis of carquinostatin B via the non-mevalonate pathway in Streptomyces exfoliatus
    • Orihara, N., Furihata, K., and Seto, H., Studies on the biosynthesis of terpenoidal compounds produced by Actinomycetes. 2. Biosynthesis of carquinostatin B via the non-mevalonate pathway in Streptomyces exfoliatus. J. Antibiot., 50, 979-981 (1997).
    • (1997) J. Antibiot. , vol.50 , pp. 979-981
    • Orihara, N.1    Furihata, K.2    Seto, H.3
  • 8
    • 0027368126 scopus 로고
    • Isoprenoid biosynthesis in bacteria: A novel pathway for the early steps leading to isopentenyl diphosphate
    • Rohmer, M., Knani, M., Simonin, P., Sutter, B., and Sahm, H., Isoprenoid biosynthesis in bacteria: a novel pathway for the early steps leading to isopentenyl diphosphate. Biochem. J., 295, 517-524 (1993).
    • (1993) Biochem. J. , vol.295 , pp. 517-524
    • Rohmer, M.1    Knani, M.2    Simonin, P.3    Sutter, B.4    Sahm, H.5
  • 9
    • 0029922877 scopus 로고    scopus 로고
    • Glyceraldehyde 3-phosphate and pyruvate as precursors of isoprenic units in an alternative non-mevalonate pathway for terpenoid biosynthesis
    • Rohmer, M., Seemann, M., Horbach, S., BringerMeyer, S., and Sahm, H., Glyceraldehyde 3-phosphate and pyruvate as precursors of isoprenic units in an alternative non-mevalonate pathway for terpenoid biosynthesis. J. Am. Chem. Soc., 118, 2564-2566 (1996).
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 2564-2566
    • Rohmer, M.1    Seemann, M.2    Horbach, S.3    Bringermeyer, S.4    Sahm, H.5
  • 10
    • 0032542140 scopus 로고    scopus 로고
    • Studies on the biosynthesis of terpenoids produced by Ac-tinomycetes. Part 4. Formation of BE-40644 by the mevalonate and nonmevalonate pathways
    • Seto, H., Orihara, N., and Furihata, K., Studies on the biosynthesis of terpenoids produced by Ac-tinomycetes. Part 4. Formation of BE-40644 by the mevalonate and nonmevalonate pathways. Tetrahedron Lett., 39, 9497-9500 (1998).
    • (1998) Tetrahedron Lett. , vol.39 , pp. 9497-9500
    • Seto, H.1    Orihara, N.2    Furihata, K.3
  • 11
    • 0030605182 scopus 로고    scopus 로고
    • Simultaneous operation of the mevalonate and non-mevalonate pathways in the biosynthesis of isopen-tenyl diphosphate in Streptomyces aeriouvifer
    • Seto, H., Watanabe, H., and Furihata, K., Simultaneous operation of the mevalonate and non-mevalonate pathways in the biosynthesis of isopen-tenyl diphosphate in Streptomyces aeriouvifer. Tetrahedron Lett., 37, 7979-7982 (1996).
    • (1996) Tetrahedron Lett. , vol.37 , pp. 7979-7982
    • Seto, H.1    Watanabe, H.2    Furihata, K.3
  • 12
    • 0032478189 scopus 로고    scopus 로고
    • Cloning and characterization of a gene from Escherichia coli encoding a transketolase-like enzyme that catalyzes the synthesis of D-1-deoxyxylulose 5-phosphate, a common precursor for isoprenoid, thiamine, and pyridox-ol biosynthesis
    • Lois, L. M., Campos, N., Rosa Putra, S., Danielsen, K., Rohmer, M., and Boronat, A., Cloning and characterization of a gene from Escherichia coli encoding a transketolase-like enzyme that catalyzes the synthesis of D-1-deoxyxylulose 5-phosphate, a common precursor for isoprenoid, thiamine, and pyridox-ol biosynthesis. Proc. Natl. Acad. Sci. USA, 95, 2105-2110 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2105-2110
    • Lois, L.M.1    Campos, N.2    Rosa Putra, S.3    Danielsen, K.4    Rohmer, M.5    Boronat, A.6
  • 13
    • 0030696041 scopus 로고    scopus 로고
    • Identification of a thiamine-dependent synthase in Escherichia coli required for the formation of the 1-deoxy-D-xylulose 5-phosphate precursor to isoprenoids, thiamine, and pyridoxol
    • Sprenger, G. A., Schorken, U., Wiegert, T., Grolle, S., DeGraaf, A. A., Taylor, S. V., Begley, T. P., Bringer-Meyer, S., and Sahm, H., Identification of a thiamine-dependent synthase in Escherichia coli required for the formation of the 1-deoxy-D-xylulose 5-phosphate precursor to isoprenoids, thiamine, and pyridoxol. Proc. Natl. Acad. Sci. USA, 94, 12857-12862 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12857-12862
    • Sprenger, G.A.1    Schorken, U.2    Wiegert, T.3    Grolle, S.4    Degraaf, A.A.5    Taylor, S.V.6    Begley, T.P.7    Bringer-Meyer, S.8    Sahm, H.9
  • 14
    • 0035180811 scopus 로고    scopus 로고
    • 1-deoxy-D-xylulose 5-phosphate synthase, the gene product of open reading frame (ORF) 2816 and ORF 2895 in Rhodobacter capsulatus
    • Hahn, F. M., Eubanks, L. M., Testa, C. A., Blagg, B. S., Baker, J. A., and Poulter, C. D., 2001. 1-deoxy-D-xylulose 5-phosphate synthase, the gene product of open reading frame (ORF) 2816 and ORF 2895 in Rhodobacter capsulatus. J. Bacteriol., 183, 1-11.
    • (2001) J. Bacteriol. , vol.183 , pp. 1-11
    • Hahn, F.M.1    Eubanks, L.M.2    Testa, C.A.3    Blagg, B.S.4    Baker, J.A.5    Poulter, C.D.6
  • 15
    • 0034666627 scopus 로고    scopus 로고
    • Tools for discovery of inhibitors of the 1-deoxy-D-xylulose-5-phosphate (DXP) synthase and DXP reductoisomerase: An approach with enzymes from the pathogenic bacterium Pseudomonas aeruginosa
    • Altincicek, B., Hintz, M., Sanderbrand, S., Wiesner, J., Beck, E., and Jomaa, H., Tools for discovery of inhibitors of the 1-deoxy-D-xylulose-5-phosphate (DXP) synthase and DXP reductoisomerase: an approach with enzymes from the pathogenic bacterium Pseudomonas aeruginosa. FEMS Microbiol. Lett., 190, 329-333 (2000).
    • (2000) FEMS Microbiol. Lett. , vol.190 , pp. 329-333
    • Altincicek, B.1    Hintz, M.2    Sanderbrand, S.3    Wiesner, J.4    Beck, E.5    Jomaa, H.6
  • 16
    • 0033985493 scopus 로고    scopus 로고
    • Cloning and characterization of 1-deoxy-D-xylu-lose 5-phosphate synthase from Streptomyces sp. Strain CL190, which uses both the mevalonate and nonmevalonate pathways for isopentenyl diphosphate biosynthesis
    • Kuzuyama, T., Takagi, M., Takahashi, S., and Seto, H., Cloning and characterization of 1-deoxy-D-xylu-lose 5-phosphate synthase from Streptomyces sp. Strain CL190, which uses both the mevalonate and nonmevalonate pathways for isopentenyl diphosphate biosynthesis. J. Bacteriol., 182, 891-897 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 891-897
    • Kuzuyama, T.1    Takagi, M.2    Takahashi, S.3    Seto, H.4
  • 17
    • 0034930422 scopus 로고    scopus 로고
    • Molecular cloning, expression and characterization of the first three genes in the mevalonate-independent isoprenoid pathway in Streptomyces coelicolor
    • Cane, D. E., Chow, C., Lillo, A., and Kang, I., Molecular cloning, expression and characterization of the first three genes in the mevalonate-independent isoprenoid pathway in Streptomyces coelicolor. Bioorganic Medical Chem., 9, 1467-1477 (2001).
    • (2001) Bioorganic Medical Chem. , vol.9 , pp. 1467-1477
    • Cane, D.E.1    Chow, C.2    Lillo, A.3    Kang, I.4
  • 18
    • 0032731682 scopus 로고    scopus 로고
    • A Syn-echococcus leopoliensis SAUG 1402-1 operon harboring the 1-deoxyxylulose 5-phosphate synthase gene and two additional open reading frames is functionally involved in the dimethylallyl diphosphate synthesis
    • Miller, B., Heuser, T., and Zimmer, W., A Syn-echococcus leopoliensis SAUG 1402-1 operon harboring the 1-deoxyxylulose 5-phosphate synthase gene and two additional open reading frames is functionally involved in the dimethylallyl diphosphate synthesis. FEBS Lett., 460, 485-490 (1999).
    • (1999) FEBS Lett. , vol.460 , pp. 485-490
    • Miller, B.1    Heuser, T.2    Zimmer, W.3
  • 19
    • 0035933854 scopus 로고    scopus 로고
    • 1-deoxy-D-xylulose-5-phosphate synthase, a limiting enzyme for plastidic isoprenoid biosynthesis in plants
    • Esteves, J. M., Cantero, A., Reindl, A., Reichler, S., and Leon, P., 1-deoxy-D-xylulose-5-phosphate synthase, a limiting enzyme for plastidic isoprenoid biosynthesis in plants. J. Biol. Chem., 276, 22901-22909 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 22901-22909
    • Esteves, J.M.1    Cantero, A.2    Reindl, A.3    Reichler, S.4    Leon, P.5
  • 20
    • 0343614184 scopus 로고    scopus 로고
    • A family of transketolases that directs isoprenoid biosynthesis via a mevalonate-independent pathway
    • Lange, B. M., Wildrung, M. R., McCaskill, D., and Croteau, R., A family of transketolases that directs isoprenoid biosynthesis via a mevalonate-independent pathway. Proc. Natl. Acad. Sci. USA, 95, 2100-2104 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2100-2104
    • Lange, B.M.1    Wildrung, M.R.2    McCaskill, D.3    Croteau, R.4
  • 21
    • 0032132839 scopus 로고    scopus 로고
    • Dedicated roles of plastid transketolases during the early onset of isoprenoid biogenesis in pepper fruits
    • Bouvier, F., d’Harlingue, A., Suire, C., Backhous, R. A., and Camara, B., Dedicated roles of plastid transketolases during the early onset of isoprenoid biogenesis in pepper fruits. Plant. Physiol., 117, 1423-1431 (1998).
    • (1998) Plant. Physiol. , vol.117 , pp. 1423-1431
    • Bouvier, F.1    D’harlingue, A.2    Suire, C.3    Backhous, R.A.4    Camara, B.5
  • 22
    • 0342505289 scopus 로고    scopus 로고
    • Carotenoid biosynthesis during tomato fruit development: Regulatory role of 1-deoxy-D-xylulose 5-phosphate synthase
    • Lois, L. M., Rodrigues-Concepcion, Gallego M. F., Campos, N., and Boronat, A., Carotenoid biosynthesis during tomato fruit development: regulatory role of 1-deoxy-D-xylulose 5-phosphate synthase. Plant J., 22, 503-513 (2000).
    • (2000) Plant J. , vol.22 , pp. 503-513
    • Lois, L.M.1    Rodrigues-Concepcion, G.M.F.2    Campos, N.3    Boronat, A.4
  • 23
    • 0033843763 scopus 로고    scopus 로고
    • 1-deoxy-D-xylulose 5-phosphate synthase from periwinkle: CDNA identification and induced gene expression in terpenoid indole alkaloid-producing cells
    • Chahed, K., Oudin, A., Guivarc’h, N., Hamdi, D., Chenieux, J. C., Rideau, M., and Clastre, M., 1-deoxy-D-xylulose 5-phosphate synthase from periwinkle: cDNA identification and induced gene expression in terpenoid indole alkaloid-producing cells. Plant Physiol. Biochem., 38, 559-566 (2000).
    • (2000) Plant Physiol. Biochem. , vol.38 , pp. 559-566
    • Chahed, K.1    Oudin, A.2    Guivarc’h, N.3    Hamdi, D.4    Chenieux, J.C.5    Rideau, M.6    Clastre, M.7
  • 24
    • 0034733529 scopus 로고    scopus 로고
    • Characterization of 1-deoxy-D-xylulose 5-phosphate reductoisomerase, an enzyme involved in the biosynthesis of isopentenyl diphosphate, and identification of its catalytic amino acid residues
    • Kuzuyama, T., Takahashi, S., Takagi, M., and Seto, H., Characterization of 1-deoxy-D-xylulose 5-phosphate reductoisomerase, an enzyme involved in the biosynthesis of isopentenyl diphosphate, and identification of its catalytic amino acid residues. J. Biol. Chem., 275, 19928-19932 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 19928-19932
    • Kuzuyama, T.1    Takahashi, S.2    Takagi, M.3    Seto, H.4
  • 25
    • 0032544054 scopus 로고    scopus 로고
    • A 1-deoxy-D-xylulose 5-phosphate reduc-toisomerase catalyzing the formation of 2-C-methyl-D-erythritol 4-phosphate in an alternative non-mevalonate pathway for terpenoid biosynthesis
    • Takahashi, S., Kuzuyama, T., Watanabe, H., and Seto, H., A 1-deoxy-D-xylulose 5-phosphate reduc-toisomerase catalyzing the formation of 2-C-methyl-D-erythritol 4-phosphate in an alternative non-mevalonate pathway for terpenoid biosynthesis. Proc. Natl. Acad. Sci. USA, 95, 9879-9884 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9879-9884
    • Takahashi, S.1    Kuzuyama, T.2    Watanabe, H.3    Seto, H.4
  • 28
    • 0032693034 scopus 로고    scopus 로고
    • Cytidine 5’-triphosphate-dependent biosynthesis of isoprenoids: YgbP protein of Escherichia coli catalyzes the formation of 4-diphosphocytidyl-2-C-methylerythritol
    • Rohdich, F., Wungsintaweekul, J., Fellermeier, M., Sagner, S., Herz, S., Kis, K., Eisenreich, W., Bacher, A., and Zenk, M. H., Cytidine 5’-triphosphate-dependent biosynthesis of isoprenoids: YgbP protein of Escherichia coli catalyzes the formation of 4-diphosphocytidyl-2-C-methylerythritol. Proc. Natl. Acad. Sci. USA, 95, 11758-11763 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11758-11763
    • Rohdich, F.1    Wungsintaweekul, J.2    Fellermeier, M.3    Sagner, S.4    Herz, S.5    Kis, K.6    Eisenreich, W.7    Bacher, A.8    Zenk, M.H.9
  • 29
    • 0034728128 scopus 로고    scopus 로고
    • Formation of 4-(Cytidine 5’-diphospho)-2-C-methyl-D-erythritol from 2-C-methyl-D-erythritol 4-phosphate by 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, a new enzyme in the nonmevalonate pathway
    • Kuzuyama, T., Takagi, M., Kaneda, K., Dairi, T., and Seto, H., Formation of 4-(cytidine 5’-diphospho)-2-C-methyl-D-erythritol from 2-C-methyl-D-erythritol 4-phosphate by 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, a new enzyme in the nonmevalonate pathway. Tetrahedron Lett., 41, 703-706 (2000).
    • (2000) Tetrahedron Lett. , vol.41 , pp. 703-706
    • Kuzuyama, T.1    Takagi, M.2    Kaneda, K.3    Dairi, T.4    Seto, H.5
  • 30
    • 0034655829 scopus 로고    scopus 로고
    • Studies on the non-mevalonate pathway: Conversion of 4-(cytidine 5? -diphospho)-2-C-methyl-D-erythritol to its 2-phospho derivative by 4-(cytidine 5? -diphospho)-2-C-methyl-D-erythritol kinase
    • Kuzuyama, T., Takagi, M., Kaneda, K., Watanabe, H., Dairi, T., and Seto, H., Studies on the non-mevalonate pathway: conversion of 4-(cytidine 5? -diphospho)-2-C-methyl-D-erythritol to its 2-phospho derivative by 4-(cytidine 5? -diphospho)-2-C-methyl-D-erythritol kinase. Tetrahedron Lett., 41, 2925-2928 (2000).
    • (2000) Tetrahedron Lett. , vol.41 , pp. 2925-2928
    • Kuzuyama, T.1    Takagi, M.2    Kaneda, K.3    Watanabe, H.4    Dairi, T.5    Seto, H.6
  • 31
    • 0034728844 scopus 로고    scopus 로고
    • Studies on the non-mevalonate pathway: Formation of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate from 2-phospho-4-(cytidine 5? -diphospho)-2-C-methyl-D-erythritol
    • Kuzuyama, T., Takagi, M., Kaneda, K., Watanabe, H., Dairi, T., and Seto, H., Studies on the non-mevalonate pathway: Formation of 2-C-methyl-D-erythritol 2,4-cyclodiphosphate from 2-phospho-4-(cytidine 5? -diphospho)-2-C-methyl-D-erythritol. Tetrahedron Lett., 41, 3395-3398 (2000).
    • (2000) Tetrahedron Lett. , vol.41 , pp. 3395-3398
    • Kuzuyama, T.1    Takagi, M.2    Kaneda, K.3    Watanabe, H.4    Dairi, T.5    Seto, H.6
  • 32
    • 0034810693 scopus 로고    scopus 로고
    • Eubacterial Diterpene Cyclase Genes Essential for Production of Isoprenoid Antibiotic-terpentecin
    • Dairi, T., Hamano, Y., Kuzuyama, T., Itoh, N., Furihata, K., and Seto, H., Eubacterial Diterpene Cyclase Genes Essential for Production of Isoprenoid Antibiotic-terpentecin. J. Bacteriol., 183, 6085-6094 (2001).
    • (2001) J. Bacteriol. , vol.183 , pp. 6085-6094
    • Dairi, T.1    Hamano, Y.2    Kuzuyama, T.3    Itoh, N.4    Furihata, K.5    Seto, H.6
  • 33
    • 0033965047 scopus 로고    scopus 로고
    • Cloning of the gene encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase from terpenoid antibiotics-producing Strep-tomyces strains
    • Dairi, T., Motohira, Y., Kuzuyama, T., Takahashi, S., Itoh, N., and Seto, H., Cloning of the gene encoding 3-hydroxy-3-methylglutaryl coenzyme A reductase from terpenoid antibiotics-producing Strep-tomyces strains. Mol. Gen. Genet., 262, 957-964 (2000).
    • (2000) Mol. Gen. Genet. , vol.262 , pp. 957-964
    • Dairi, T.1    Motohira, Y.2    Kuzuyama, T.3    Takahashi, S.4    Itoh, N.5    Seto, H.6
  • 34
    • 0035408665 scopus 로고    scopus 로고
    • Cloning of a gene cluster encoding enzymes responsible for the mevalonate pathway from a terpenoid-antibiotic-producing Streptomyces strain
    • Hamano, Y., Dairi, T., Yamamoto, M., Kawasaki, T., Kaneda, K., Kuzuyama, T., Itoh, N., and Seto, H., Cloning of a gene cluster encoding enzymes responsible for the mevalonate pathway from a terpenoid-antibiotic-producing Streptomyces strain. Biosci. Biotechnol. Biochem., 65, 1627-1635 (2001).
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 1627-1635
    • Hamano, Y.1    Dairi, T.2    Yamamoto, M.3    Kawasaki, T.4    Kaneda, K.5    Kuzuyama, T.6    Itoh, N.7    Seto, H.8
  • 35
    • 0000188835 scopus 로고    scopus 로고
    • Chemical and enzymatic synthesis of 1-deoxy-D-xylulose-5-phosphate
    • Taylor, S. V., Vu, L. D., and Begley, T. P., Chemical and enzymatic synthesis of 1-deoxy-D-xylulose-5-phosphate. J. Org. Chem., 63, 275-2377 (1998).
    • (1998) J. Org. Chem. , vol.63 , pp. 275-2377
    • Taylor, S.V.1    Vu, L.D.2    Begley, T.P.3
  • 39
    • 0026727261 scopus 로고
    • Organization and nature of fortimicin A (As-tromicin) biosynthetic genes studied using a cosmid library of Micromonospora olivasterospora DNA
    • Dairi, T., Ohta, T., Hashimoto, E., and Hasegawa, M., Organization and nature of fortimicin A (as-tromicin) biosynthetic genes studied using a cosmid library of Micromonospora olivasterospora DNA. Mol. Gen. Genet., 236, 39-48 (1992).
    • (1992) Mol. Gen. Genet. , vol.236 , pp. 39-48
    • Dairi, T.1    Ohta, T.2    Hashimoto, E.3    Hasegawa, M.4
  • 41
    • 0020390362 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase from yeast
    • Byers, L. D., Glyceraldehyde-3-phosphate dehydrogenase from yeast. Methods Enzymol., 89, 326-335 (1982).
    • (1982) Methods Enzymol. , vol.89 , pp. 326-335
    • Byers, L.D.1
  • 42
    • 0029310651 scopus 로고
    • Cloning and nucleotide sequence of the gene responsible for chlorination of tetracycline
    • Dairi, T., Nakano, T., Aisaka, K., Katsumata, R., and Hasegawa, M., Cloning and nucleotide sequence of the gene responsible for chlorination of tetracycline. Biosci. Biotechnol. Biochem., 59, 1099-1106 (1995).
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 1099-1106
    • Dairi, T.1    Nakano, T.2    Aisaka, K.3    Katsumata, R.4    Hasegawa, M.5
  • 43
    • 0026727261 scopus 로고
    • Organization and nature of fortimicin A (As-tromicin) biosynthetic genes studied using a cosmid library of Micromonospora olivasterospora DNA
    • Dairi, T., Ohta, T., Hashimoto, E., and Hasegawa, M., Organization and nature of fortimicin A (as-tromicin) biosynthetic genes studied using a cosmid library of Micromonospora olivasterospora DNA. Mol. Gen. Genet., 236, 39-48 (1992).
    • (1992) Mol. Gen. Genet. , vol.236 , pp. 39-48
    • Dairi, T.1    Ohta, T.2    Hashimoto, E.3    Hasegawa, M.4
  • 45
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson, W. R. and Lipman, D. J., Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA, 85, 2444-2448 (1988).
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 47
    • 0026098884 scopus 로고
    • Biosynthesis of the thia-zole moiety of thiamine (Vitamin B1) in higher plant chloroplast
    • 1) in higher plant chloroplast. Proc. Natl. Acad. Sci. USA, 88, 2042-2045 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2042-2045
    • Julliard, J.1    Douce, R.2
  • 48
    • 0029871048 scopus 로고    scopus 로고
    • Pentalenolactone-insensitive glyceralde-hyde-3-phosphate dehydrogenase from Streptomyces arenae is closely related to GAPDH from thermostable eubacteria and plant chloroplasts
    • Fröhlich, K. U., Kannwischer, R., Rudiger, M., and Mecke, D., Pentalenolactone-insensitive glyceralde-hyde-3-phosphate dehydrogenase from Streptomyces arenae is closely related to GAPDH from thermostable eubacteria and plant chloroplasts. Arch. Microbiol., 165, 179-186 (1996).
    • (1996) Arch. Microbiol. , vol.165 , pp. 179-186
    • Fröhlich, K.U.1    Kannwischer, R.2    Rudiger, M.3    Mecke, D.4
  • 49
    • 0024367906 scopus 로고
    • Substitution of a pentalenolactone-sensi-tive glyceraldehyde-3-phosphate dehydrogenase by a genetically distinct resistant isoform accompanies pentalenolactone production in
    • Frohlich, K. U., Wiedmann, M., Lottspeich, F., and Mecke, D., Substitution of a pentalenolactone-sensi-tive glyceraldehyde-3-phosphate dehydrogenase by a genetically distinct resistant isoform accompanies pentalenolactone production in Streptomyces arenae. J. Bacteriol., 171, 6696-6702 (1989).
    • (1989) Streptomyces Arenae. J. Bacteriol. , vol.171 , pp. 6696-6702
    • Frohlich, K.U.1    Wiedmann, M.2    Lottspeich, F.3    Mecke, D.4
  • 50
    • 0028867858 scopus 로고
    • Cloning, sequencing and expression in Escherichia coli of Streptomyces aureofaciens gene encoding glyceraldehyde-3-phosphate dehydrogenase
    • Kormanec, J., Lempelova, A., Farkasovsky, M., and Homerova, D., Cloning, sequencing and expression in Escherichia coli of Streptomyces aureofaciens gene encoding glyceraldehyde-3-phosphate dehydrogenase. Gene, 165, 77-80 (1995).
    • (1995) Gene , vol.165 , pp. 77-80
    • Kormanec, J.1    Lempelova, A.2    Farkasovsky, M.3    Homerova, D.4
  • 51
    • 0030660130 scopus 로고    scopus 로고
    • Expression of the Streptomyces aureofaciens glyceraldehyde-3-phosphate dehydrogenase gene (Gap) is developmentally regulated and induced by glucose
    • Kormanec, J., Lempel’ova, A., Novakova, R., Rezuchova, B., and Homerova, D., Expression of the Streptomyces aureofaciens glyceraldehyde-3-phosphate dehydrogenase gene (gap) is developmentally regulated and induced by glucose. Microbiol., 143, 3555-3561 (1997).
    • (1997) Microbiol. , vol.143 , pp. 3555-3561
    • Kormanec, J.1    Lempel’ova, A.2    Novakova, R.3    Rezuchova, B.4    Homerova, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.