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Volumn 50, Issue 26, 2011, Pages 5905-5917

Combined structural and functional investigation of a C-3′′- ketoreductase involved in the biosynthesis of dTDP-l-digitoxose

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ANTITUMOR ANTIBIOTICS; CATALYTIC ROLE; CONFORMATIONAL CHANGE; GLUCOSE 1-PHOSPHATE; HIGH-RESOLUTION STRUCTURES; KETO GROUPS; LYSINE MUTATION; MUTANT PROTEINS; NATURAL PRODUCTS; OXIDOREDUCTASES; SOIL-DWELLING; TERNARY COMPLEX; WILD-TYPE ENZYMES;

EID: 79959782300     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200514b     Document Type: Article
Times cited : (22)

References (35)
  • 1
    • 0031127564 scopus 로고    scopus 로고
    • The role of carbohydrates in biologically active natural products
    • Weymouth-Wilson, A. C. (1997) The role of carbohydrates in biologically active natural products Nat. Prod. Rep. 14, 99-110 (Pubitemid 27191082)
    • (1997) Natural Product Reports , vol.14 , Issue.2 , pp. 99-110
    • Weymouth-Wilson, A.C.1
  • 3
    • 0018942259 scopus 로고
    • Novel antitumor antibiotics, tetrocarcins
    • Tomita, F., Tamaoki, T., Shirahata, K., Kasai, M., Morimoto, M., Ohkubo, S., Mineura, K., and Ishii, S. (1980) Novel antitumor antibiotics, tetrocarcins J. Antibiot. 33, 668-670 (Pubitemid 10016623)
    • (1980) Journal of Antibiotics , vol.33 , Issue.6 , pp. 668-670
    • Tomita, F.1    Tamaoki, T.2    Shirahata, K.3
  • 4
    • 0020451795 scopus 로고
    • 2, F and F-1, new antibiotics. Fermentation, isolation and characterization
    • Tamaoki, T., Kasai, M., Shirahata, K., and Tomita, F. (1982) Tetrocarcins E1, E2, F and F-1, new antibiotics. Fermentation, isolation and characterization J. Antibiot. 35, 979-984 (Pubitemid 13241415)
    • (1982) Journal of Antibiotics , vol.35 , Issue.8 , pp. 979-984
    • Tamaoki, T.1    Kasai, M.2    Shirahata, K.3    Tomita, F.4
  • 6
    • 36749055680 scopus 로고    scopus 로고
    • Elucidation of the kijanimicin gene cluster: Insights into the biosynthesis of spirotetronate antibiotics and nitrosugars
    • DOI 10.1021/ja0744854
    • Zhang, H., White-Phillip, J. A., Melancon, C. E., III, Kwon, H. J., Yu, W. L., and Liu, H. W. (2007) Elucidation of the kijanimicin gene cluster: Insights into the biosynthesis of spirotetronate antibiotics and nitrosugars J. Am. Chem. Soc. 129, 14670-14683 (Pubitemid 350207880)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.47 , pp. 14670-14683
    • Zhang, H.1    White-Phillip, J.A.2    Melancon III, C.E.3    Kwon, H.-J.4    Yu, W.-L.5    Liu, H.-W.6
  • 7
    • 0018561127 scopus 로고
    • The structure of a novel sugar component of polyene macrolide antibiotics: 2,6-dideoxy-l-ribohexopyranose
    • Zielinski, J., Jereczek, E., Sowinski, P., Falkowski, L., Rudowski, A., and Borowski, E. (1979) The structure of a novel sugar component qof polyene macrolide antibiotics: 2,6-Dideoxy- l -ribohexopyranose J. Antibiot. 32, 565-568 (Pubitemid 10067608)
    • (1979) Journal of Antibiotics , vol.32 , Issue.6 , pp. 565-568
    • Zielinski, J.1    Jereczek, E.2    Sowinski, P.3
  • 9
    • 0036224507 scopus 로고    scopus 로고
    • Biosynthesis of the dideoxysugar component of jadomycin B: Genes in the jad cluster of Streptomyces venezuelae ISP5230 for L-digitoxose assembly and transfer to the angucycline aglycone
    • Wang, L., White, R. L., and Vining, L. C. (2002) Biosynthesis of the dideoxysugar component of jadomycin B: Genes in the jad cluster of Streptomyces venezuelae ISP5230 for l -digitoxose assembly and transfer to the angucycline aglycone Microbiology 148, 1091-1103 (Pubitemid 34436784)
    • (2002) Microbiology , vol.148 , Issue.4 , pp. 1091-1103
    • Wang, L.1    White, R.L.2    Vining, L.C.3
  • 10
    • 57549105096 scopus 로고    scopus 로고
    • Natural-product sugar biosynthesis and enzymatic glycodiversification
    • Thibodeaux, C. J., Melancon, C. E., III, and Liu, H. W. (2008) Natural-product sugar biosynthesis and enzymatic glycodiversification Angew. Chem., Int. Ed. 47, 9814-9859
    • (2008) Angew. Chem., Int. Ed. , vol.47 , pp. 9814-9859
    • Thibodeaux, C.J.1    Liu, H.W.2
  • 12
    • 0030589696 scopus 로고    scopus 로고
    • The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: An osmoprotective periplasmic enzyme containing non-dissociable NADP
    • Kingston, R. L., Scopes, R. K., and Baker, E. N. (1996) The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: An osmoprotective periplasmic enzyme containing non-dissociable NADP Structure 4, 1413-1428 (Pubitemid 27050275)
    • (1996) Structure , vol.4 , Issue.12 , pp. 1413-1428
    • Kingston, R.L.1    Scopes, R.K.2    Baker, E.N.3
  • 13
    • 79952172915 scopus 로고    scopus 로고
    • Biochemical and structural characterization of WlbA from Bordetella pertussis and Chromobacterium violaceum: Enzymes required for the biosynthesis of 2,3-diacetamido-2,3-dideoxy- d -mannuronic Acid
    • Thoden, J. B. and Holden, H. M. (2011) Biochemical and structural characterization of WlbA from Bordetella pertussis and Chromobacterium violaceum: Enzymes required for the biosynthesis of 2,3-diacetamido-2,3-dideoxy- d -mannuronic Acid Biochemistry 50, 1483-1491
    • (2011) Biochemistry , vol.50 , pp. 1483-1491
    • Thoden, J.B.1    Holden, H.M.2
  • 14
    • 33847291392 scopus 로고    scopus 로고
    • Understanding a transcriptional paradigm at the molecular level: The structure of yeast Gal80p
    • DOI 10.1074/jbc.C600285200
    • Thoden, J. B., Sellick, C. A., Reece, R. J., and Holden, H. M. (2007) Understanding a transcriptional paradigm at the molecular level. The structure of yeast Gal80p J. Biol. Chem. 282, 1534-1538 (Pubitemid 47076674)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.3 , pp. 1534-1538
    • Thoden, J.B.1    Sellick, C.A.2    Reece, R.J.3    Holden, H.M.4
  • 15
    • 15744370513 scopus 로고    scopus 로고
    • Molecular structure of human galactokinase: Implications for type II galactosemia
    • DOI 10.1074/jbc.M412916200
    • Thoden, J. B., Timson, D. J., Reece, R. J., and Holden, H. M. (2005) Molecular structure of human galactokinase: Implications for Type II galactosemia J. Biol. Chem. 280, 9662-9670 (Pubitemid 40409664)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.10 , pp. 9662-9670
    • Thoden, J.B.1    Timson, D.J.2    Reece, R.J.3    Holden, H.M.4
  • 16
    • 41849097831 scopus 로고    scopus 로고
    • In vitro characterization of the enzymes involved in TDP-D-forosamine biosynthesis in the spinosyn pathway of Saccharopolyspora spinosa
    • DOI 10.1021/ja0771383
    • Hong, L., Zhao, Z., Melancon, C. E., III, Zhang, H., and Liu, H. W. (2008) In vitro characterization of the enzymes involved in TDP- d -forosamine biosynthesis in the spinosyn pathway of Saccharopolyspora spinosa J. Am. Chem. Soc. 130, 4954-4967 (Pubitemid 351500129)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.14 , pp. 4954-4967
    • Hong, L.1    Zhao, Z.2    Melancon III, C.E.3    Zhang, H.4    Liu, H.-W.5
  • 17
    • 34547095033 scopus 로고    scopus 로고
    • The X-ray structure of dTDP-4-keto-6-deoxy- d -glucose-3,4-ketoisomerase
    • Davis, M. L., Thoden, J. B., and Holden, H. M. (2007) The X-ray structure of dTDP-4-keto-6-deoxy- d -glucose-3,4-ketoisomerase J. Biol. Chem. 282, 19227-19236
    • (2007) J. Biol. Chem. , vol.282 , pp. 19227-19236
    • Davis, M.L.1    Thoden, J.B.2    Holden, H.M.3
  • 24
    • 0028774539 scopus 로고
    • The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides refined at 2.0 Å resolution
    • Rowland, P., Basak, A. K., Gover, S., Levy, H. R., and Adams, M. J. (1994) The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides refined at 2.0 Å resolution Structure 2, 1073-1087
    • (1994) Structure , vol.2 , pp. 1073-1087
    • Rowland, P.1    Basak, A.K.2    Gover, S.3    Levy, H.R.4    Adams, M.J.5
  • 25
    • 0036304792 scopus 로고    scopus 로고
    • Crystal structure of a biliverdin IXα reductase enzyme-cofactor complex
    • DOI 10.1016/S0022-2836(02)00383-2
    • Whitby, F. G., Phillips, J. D., Hill, C. P., McCoubrey, W., and Maines, M. D. (2002) Crystal structure of a biliverdin IXα reductase enzyme-cofactor complex J. Mol. Biol. 319, 1199-1210 (Pubitemid 34729428)
    • (2002) Journal of Molecular Biology , vol.319 , Issue.5 , pp. 1199-1210
    • Whitby, F.G.1    Phillips, J.D.2    Hill, C.P.3    McCoubrey, W.4    Maines, M.D.5
  • 26
    • 33747460737 scopus 로고    scopus 로고
    • Crystal structure of NADP(H)-dependent 1,5-anhydro-D-fructose reductase from Sinorhizobium morelense at 2.2 Å resolution: Construction of a NADH-accepting mutant and its application in rare sugar synthesis
    • DOI 10.1021/bi052589q
    • Dambe, T. R., Kuhn, A. M., Brossette, T., Giffhorn, F., and Scheidig, A. J. (2006) Crystal structure of NADP(H)-dependent 1,5-anhydro- d -fructose reductase from Sinorhizobium morelense at 2.2 Å resolution: Construction of a NADH-accepting mutant and its application in rare sugar synthesis Biochemistry 45, 10030-10042 (Pubitemid 44257397)
    • (2006) Biochemistry , vol.45 , Issue.33 , pp. 10030-10042
    • Dambe, T.R.1    Kuhn, A.M.2    Brossette, T.3    Giffhorn, F.4    Scheidig, A.J.5
  • 27
    • 37448999171 scopus 로고    scopus 로고
    • Structures of dimeric dihydrodiol dehydrogenase apoenzyme and inhibitor complex: Probing the subunit interface with site-directed mutagenesis
    • Carbone, V., Endo, S., Sumii, R., Chung, R. P., Matsunaga, T., Hara, A., and El-Kabbani, O. (2008) Structures of dimeric dihydrodiol dehydrogenase apoenzyme and inhibitor complex: Probing the subunit interface with site-directed mutagenesis Proteins 70, 176-187
    • (2008) Proteins , vol.70 , pp. 176-187
    • Carbone, V.1    Endo, S.2    Sumii, R.3    Chung, R.P.4    Matsunaga, T.5    Hara, A.6    El-Kabbani, O.7
  • 28
    • 77956418190 scopus 로고    scopus 로고
    • Structural and functional studies of WlbA: A dehydrogenase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy- d -mannuronic acid
    • Thoden, J. B. and Holden, H. M. (2010) Structural and functional studies of WlbA: A dehydrogenase involved in the biosynthesis of 2,3-diacetamido-2,3- dideoxy- d -mannuronic acid Biochemistry 49, 7939-7948
    • (2010) Biochemistry , vol.49 , pp. 7939-7948
    • Thoden, J.B.1    Holden, H.M.2
  • 29
    • 0034642209 scopus 로고    scopus 로고
    • Delineation of the roles of amino acids involved in the catalytic functions of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase
    • Vought, V., Ciccone, T., Davino, M. H., Fairbairn, L., Lin, Y., Cosgrove, M. S., Adams, M. J., and Levy, H. R. (2000) Delineation of the roles of amino acids involved in the catalytic functions of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase Biochemistry 39, 15012-15021
    • (2000) Biochemistry , vol.39 , pp. 15012-15021
    • Vought, V.1    Ciccone, T.2    Davino, M.H.3    Fairbairn, L.4    Lin, Y.5    Cosgrove, M.S.6    Adams, M.J.7    Levy, H.R.8
  • 30
    • 0014487357 scopus 로고
    • Subunit interactions of glucose-6-phosphate dehydrogenase from human erythrocytes
    • Cohen, P. and Rosemeyer, M. A. (1969) Subunit interactions of glucose-6-phosphate dehydrogenase from human erythrocytes Eur. J. Biochem. 8, 8-15
    • (1969) Eur. J. Biochem. , vol.8 , pp. 8-15
    • Cohen, P.1    Rosemeyer, M.A.2
  • 31
    • 44449160397 scopus 로고    scopus 로고
    • Structural and functional features of dimeric dihydrodiol dehydrogenase
    • Carbone, V., Hara, A., and El-Kabbani, O. (2008) Structural and functional features of dimeric dihydrodiol dehydrogenase Cell. Mol. Life Sci. 65, 1464-1474
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 1464-1474
    • Carbone, V.1    Hara, A.2    El-Kabbani, O.3
  • 32
    • 0035923401 scopus 로고    scopus 로고
    • Crystal structures of the precursor form of glucose-fructose oxidoreductase from zymomonas mobilis and its complexes with bound ligands
    • DOI 10.1021/bi011355d
    • Nurizzo, D., Halbig, D., Sprenger, G. A., and Baker, E. N. (2001) Crystal structures of the precursor form of glucose-fructose oxidoreductase from Zymomonas mobilis and its complexes with bound ligands Biochemistry 40, 13857-13867 (Pubitemid 33078854)
    • (2001) Biochemistry , vol.40 , Issue.46 , pp. 13857-13867
    • Nurizzo, D.1    Halbig, D.2    Sprenger, G.A.3    Baker, E.N.4
  • 33
    • 0041317450 scopus 로고    scopus 로고
    • The three-dimensional structures of the Mycobacterium tuberculosis dihydrodipicolinate reductase-NADH-2,6-PDC and -NADPH-2,6-PDC complexes. Structural and mutagenic analysis of relaxed nucleotide specificity
    • DOI 10.1021/bi030044v
    • Cirilli, M., Zheng, R., Scapin, G., and Blanchard, J. S. (2003) The three-dimensional structures of the Mycobacterium tuberculosis dihydrodipicolinate reductase-NADH-2,6-PDC and -NADPH-2,6-PDC complexes. Structural and mutagenic analysis of relaxed nucleotide specificity Biochemistry 42, 10644-10650 (Pubitemid 37102103)
    • (2003) Biochemistry , vol.42 , Issue.36 , pp. 10644-10650
    • Cirilli, M.1    Zheng, R.2    Scapin, G.3    Blanchard, J.S.4
  • 34
    • 0034687532 scopus 로고    scopus 로고
    • Roles of His-79 and Tyr-180 of d -xylose/dihydrodiol dehydrogenase in catalytic function
    • Asada, Y., Aoki, S., Ishikura, S., Usami, N., and Hara, A. (2000) Roles of His-79 and Tyr-180 of d -xylose/dihydrodiol dehydrogenase in catalytic function Biochem. Biophys. Res. Commun. 278, 333-337
    • (2000) Biochem. Biophys. Res. Commun. , vol.278 , pp. 333-337
    • Asada, Y.1    Aoki, S.2    Ishikura, S.3    Usami, N.4    Hara, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.