메뉴 건너뛰기




Volumn 58, Issue , 2000, Pages 121-148

Steroid dehydrogenase structures, mechanism of action, and disease

Author keywords

[No Author keywords available]

Indexed keywords

3ALPHA(OR 20BETA) HYDROXYSTEROID DEHYDROGENASE; ALDOSTERONE; HYDROCORTISONE; HYDROXYSTEROID DEHYDROGENASE;

EID: 0033628253     PISSN: 00836729     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0083-6729(00)58023-6     Document Type: Review
Times cited : (75)

References (66)
  • 1
    • 0005454789 scopus 로고
    • Paracrine influence of human breast stromal fibroblasts on breast epithelial cells: Secretion of a polypeptide which stimulates reductive 17β-oestradiol dehydrogenase activity
    • E.F. Adams C.J. Newton G.J. Tait H. Braumsberg M.J. Reed V.H.T. James Paracrine influence of human breast stromal fibroblasts on breast epithelial cells: Secretion of a polypeptide which stimulates reductive 17β-oestradiol dehydrogenase activity Int. J. Cancer 42 1988 119 122
    • (1988) Int. J. Cancer , vol.42 , pp. 119-122
    • Adams, E.F.1    Newton, C.J.2    Tait, G.J.3    Braumsberg, H.4    Reed, M.J.5    James, V.H.T.6
  • 4
    • 0030587782 scopus 로고    scopus 로고
    • Crystal structure of the ternary complex of 1,3,8-trihydroxysteroid naphtalene reductase from Magnaporthe grisea with NADPH and an active-site inhibitor
    • A. Andersson D. Jordan G. Schneider Y. Lindqvist Crystal structure of the ternary complex of 1,3,8-trihydroxysteroid naphtalene reductase from Magnaporthe grisea with NADPH and an active-site inhibitor Structure 4 1997 1161 1170
    • (1997) Structure , vol.4 , pp. 1161-1170
    • Andersson, A.1    Jordan, D.2    Schneider, G.3    Lindqvist, Y.4
  • 5
    • 0031573526 scopus 로고    scopus 로고
    • The 1.25Å crystal structure of sepiapterin reductase reveals its binding mode to pterins and brain neurotransmitters
    • G. Auerbach A. Herrmann M. Gütlich M. Fischer U. Jacob A. Bacher R. Huber The 1.25Å crystal structure of sepiapterin reductase reveals its binding mode to pterins and brain neurotransmitters EMBO J. 16 1997 7219 7230
    • (1997) EMBO J. , vol.16 , pp. 7219-7230
    • Auerbach, G.1    Herrmann, A.2    Gütlich, M.3    Fischer, M.4    Jacob, U.5    Bacher, A.6    Huber, R.7
  • 6
    • 0029761692 scopus 로고    scopus 로고
    • Crystal structure of human estrogenic 17β-hydroxysteroid dehydrogenase complexed with 17β-estradiol
    • A. Azzi P.H. Rehse D.W. Zhu R.L. Campbell F. Labrie S.C. Lin Crystal structure of human estrogenic 17β-hydroxysteroid dehydrogenase complexed with 17β-estradiol Nat. Struct. Biol. 8 1996 665 668
    • (1996) Nat. Struct. Biol. , vol.8 , pp. 665-668
    • Azzi, A.1    Rehse, P.H.2    Zhu, D.W.3    Campbell, R.L.4    Labrie, F.5    Lin, S.C.6
  • 8
    • 0026736606 scopus 로고
    • The molecular structure of UDP-galactose 4-epimerase from Escherichia coli determined at 2.5Å resolution
    • A.J. Bauer I. Rayment P.A. Frey H.M. Holden The molecular structure of UDP-galactose 4-epimerase from Escherichia coli determined at 2.5Å resolution Proteins: Struct., Funct., Genet. 12 1992 372 381
    • (1992) Proteins: Struct., Funct., Genet. , vol.12 , pp. 372-381
    • Bauer, A.J.1    Rayment, I.2    Frey, P.A.3    Holden, H.M.4
  • 9
    • 0032544367 scopus 로고    scopus 로고
    • The refined crystal structure of Drosophila levanonensis alcohol dehydrogenase at 1.9 Å resolution
    • J. Benach S. Atrian R. Gonzalez-Duarte R. Ladenstein The refined crystal structure of Drosophila levanonensis alcohol dehydrogenase at 1.9 Å resolution J. Mol. Biol. 282 1998 383 399
    • (1998) J. Mol. Biol. , vol.282 , pp. 383-399
    • Benach, J.1    Atrian, S.2    Gonzalez-Duarte, R.3    Ladenstein, R.4
  • 10
    • 0029764218 scopus 로고    scopus 로고
    • Structure of 3α-hydroxysteroid/dihytdrodiol dehydrogenase complexed with NADP+
    • M.J. Bennett B.P. Schlegel J.M. Jex T.M. Penning M. Lewis Structure of 3α-hydroxysteroid/dihytdrodiol dehydrogenase complexed with NADP+ Biochemistry 35 1996 10702 10711
    • (1996) Biochemistry , vol.35 , pp. 10702-10711
    • Bennett, M.J.1    Schlegel, B.P.2    Jex, J.M.3    Penning, T.M.4    Lewis, M.5
  • 12
    • 0002247212 scopus 로고
    • Structure-function relationships among nicotinamide-adenine dinucleotide dependent oxidoreductases
    • J.J. Birktoft L.J. vanaszak Structure-function relationships among nicotinamide-adenine dinucleotide dependent oxidoreductases T. Milkton W. Hearn Peptide and Protein Review Vol. 4 1984 Dekker New York 1 44
    • (1984) , pp. 1-44
    • Birktoft, J.J.1    vanaszak, L.J.2
  • 13
    • 0024333867 scopus 로고
    • The aldoketo reductase superfamily cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases
    • K.M. Bohren B. Bullock B. Wermuth K.H. Gabbay The aldoketo reductase superfamily cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases J. Biol. Chem. 264 1989 9547 9551
    • (1989) J. Biol. Chem. , vol.264 , pp. 9547-9551
    • Bohren, K.M.1    Bullock, B.2    Wermuth, B.3    Gabbay, K.H.4
  • 14
    • 0030586820 scopus 로고    scopus 로고
    • The structure of a complex of human 17β-hydroxysteroid with estradiol and NADP+ identifies two principal targets for the design of inhibitors
    • R. Breton D. Housset C. Mazza J.C. Fontecilla-Camps The structure of a complex of human 17β-hydroxysteroid with estradiol and NADP+ identifies two principal targets for the design of inhibitors Structure 4 1996 905 915
    • (1996) Structure , vol.4 , pp. 905-915
    • Breton, R.1    Housset, D.2    Mazza, C.3    Fontecilla-Camps, J.C.4
  • 17
    • 0028988237 scopus 로고
    • Crystal structure and function of the isoniazid target of mycobacterium tuberculosis
    • A. Dessen A. Quemard J.S. Blanchard W.R. Jacobs Jr. J.C. Sacchettini Crystal structure and function of the isoniazid target of mycobacterium tuberculosis Science 267 1995 1638 1641
    • (1995) Science , vol.267 , pp. 1638-1641
    • Dessen, A.1    Quemard, A.2    Blanchard, J.S.3    Jacobs, W.R.4    Sacchettini, J.C.5
  • 18
    • 0028943455 scopus 로고
    • Molecular cloning of a novel widely expressed human 80 kDA 17β-dehydrogenase (A-specific), a member of the aldo-keto reductase family
    • Y. Deyashiki K. Ohshima M. Nakanishi K. Sato A. Hara Molecular cloning of a novel widely expressed human 80 kDA 17β-dehydrogenase (A-specific), a member of the aldo-keto reductase family J. Biol. Chem. 270 1995 10461 10467
    • (1995) J. Biol. Chem. , vol.270 , pp. 10461-10467
    • Deyashiki, Y.1    Ohshima, K.2    Nakanishi, M.3    Sato, K.4    Hara, A.5
  • 19
    • 0023284318 scopus 로고
    • Estrogenic regulation of growth and polypeptide growth factor secretion in human breast carcinoma
    • R.B. Dickson M.E. Lippman Estrogenic regulation of growth and polypeptide growth factor secretion in human breast carcinoma Endocrinol. Rev. 8 1987 29 43
    • (1987) Endocrinol. Rev. , vol.8 , pp. 29-43
    • Dickson, R.B.1    Lippman, M.E.2
  • 20
    • 0024828582 scopus 로고
    • The structure and receptor binding of steroid hormones
    • W.L. Duax J.F. Griffin The structure and receptor binding of steroid hormones B. Testa Advances in Drug Research 1989 Academic Press New York 115 138
    • (1989) , pp. 115-138
    • Duax, W.L.1    Griffin, J.F.2
  • 22
    • 0025820642 scopus 로고
    • Localization of 17β-hydroxysteroid dehydrogenase throughout gestation in human placenta
    • E. Dupont F. Labrie V. Luu-Thé G. Pelletier Localization of 17β-hydroxysteroid dehydrogenase throughout gestation in human placenta J. Histochem. Cytochem. 39 1991 1403 1407
    • (1991) J. Histochem. Cytochem. , vol.39 , pp. 1403-1407
    • Dupont, E.1    Labrie, F.2    Luu-Thé, V.3    Pelletier, G.4
  • 23
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • R.M. Evans The steroid and thyroid hormone receptor superfamily Science 240 1988 889 895
    • (1988) Science , vol.240 , pp. 889-895
    • Evans, R.M.1
  • 24
    • 0027609916 scopus 로고
    • SETOR: Hardware lighted three-dimensional solid model representation of macromolecules
    • S.V. Evans SETOR: Hardware lighted three-dimensional solid model representation of macromolecules J. Mol. Graphics 11 1993 134 138
    • (1993) J. Mol. Graphics , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 27
    • 0028023426 scopus 로고
    • Expression of 17β-hydroxysteroid dehydrogenase in human granulosa cells: Correlation with follicular size, cytochrome P450 aromatase activity and oestradiol production
    • S.A. Ghersevich M.H. Poutanen H.K. Marttikainen K. Vihko Expression of 17β-hydroxysteroid dehydrogenase in human granulosa cells: Correlation with follicular size, cytochrome P450 aromatase activity and oestradiol production J. Endocrinol. 143 1994 139 150
    • (1994) J. Endocrinol. , vol.143 , pp. 139-150
    • Ghersevich, S.A.1    Poutanen, M.H.2    Marttikainen, H.K.3    Vihko, K.4
  • 28
    • 0026732993 scopus 로고
    • Inhibition of Streptomyces hydrogenans 3α,20β-hydroxysteroid dehydrogenase by licorice-derived compounds and crystallization of an enzyme-cofactor-inhibitor complex
    • D. Ghosh M. Erman W. Pangborn W.L. Duax M.E. Baker Inhibition of Streptomyces hydrogenans 3α,20β-hydroxysteroid dehydrogenase by licorice-derived compounds and crystallization of an enzyme-cofactor-inhibitor complex J. Steroid Biochem. Mol. Biol. 42 1992 849 853
    • (1992) J. Steroid Biochem. Mol. Biol. , vol.42 , pp. 849-853
    • Ghosh, D.1    Erman, M.2    Pangborn, W.3    Duax, W.L.4    Baker, M.E.5
  • 29
    • 0028773893 scopus 로고
    • The refined three-dimensional structure of 3α,20β-hydroxysteroid dehydrogenase and possible roles of the residues conserved in “short-chain” dehydrogenases
    • D. Ghosh Z. Wawrzak C.M. Weeks W.L. Duax M. Erman The refined three-dimensional structure of 3α,20β-hydroxysteroid dehydrogenase and possible roles of the residues conserved in “short-chain” dehydrogenases Structure 2 1994 629 640
    • (1994) Structure , vol.2 , pp. 629-640
    • Ghosh, D.1    Wawrzak, Z.2    Weeks, C.M.3    Duax, W.L.4    Erman, M.5
  • 30
    • 0028179243 scopus 로고
    • Mechanism of Inhibition of 3α,20β-hydroxysteroid dehydrogenase by a licorice-derived steroidal inhibitor
    • D. Ghosh M. Erman Z. Wawrzak W.L. Duax W. Pangborn Mechanism of Inhibition of 3α,20β-hydroxysteroid dehydrogenase by a licorice-derived steroidal inhibitor Structure 2 1994 973 980
    • (1994) Structure , vol.2 , pp. 973-980
    • Ghosh, D.1    Erman, M.2    Wawrzak, Z.3    Duax, W.L.4    Pangborn, W.5
  • 33
    • 0015530351 scopus 로고
    • Polypeptide conformation of cytoplasmic malate dehydrogenase from an electron density map at 3.0Å resolution
    • E. Hill D. Tsernoglau L. Webb L.J. vanaszak Polypeptide conformation of cytoplasmic malate dehydrogenase from an electron density map at 3.0Å resolution J. Mol. Biol. 72 1972 577 589
    • (1972) J. Mol. Biol. , vol.72 , pp. 577-589
    • Hill, E.1    Tsernoglau, D.2    Webb, L.3    vanaszak, L.J.4
  • 34
    • 0028274855 scopus 로고
    • Three-dimensional structures of rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase: A member of the aldo-keto reductase superfamily
    • S.S. Hoog J.E. Pawlowski P.M. Alzari T.M. Penning M. Lewis Three-dimensional structures of rat liver 3α-hydroxysteroid/dihydrodiol dehydrogenase: A member of the aldo-keto reductase superfamily Proc. Natl. Acad. Sci. U.S 91 1994 2517 2521
    • (1994) , pp. 2517-2521
    • Hoog, S.S.1    Pawlowski, J.E.2    Alzari, P.M.3    Penning, T.M.4    Lewis, M.5
  • 35
    • 0018254898 scopus 로고
    • Nuclear mechanism of estrogen action. Effects of estradiol and anti-estrogens on estrogen receptors and nuclear receptor processing
    • K.B. Horwitz W.L. McGuire Nuclear mechanism of estrogen action. Effects of estradiol and anti-estrogens on estrogen receptors and nuclear receptor processing J. Biol. Chem. 253 1987 8185 8191
    • (1987) J. Biol. Chem. , vol.253 , pp. 8185-8191
    • Horwitz, K.B.1    McGuire, W.L.2
  • 36
    • 0022887575 scopus 로고
    • The role of tissue steroids in regulating aromatase and oestradiol 17β-hydroxysteroid dehydrogenase activities in breast and endometrial cancer
    • V.H.T. James J.M. McNeil P.A. Beranek R.C. vonney M.J. Reed The role of tissue steroids in regulating aromatase and oestradiol 17β-hydroxysteroid dehydrogenase activities in breast and endometrial cancer J. Steroid Biochem. 25 1986 787 790
    • (1986) J. Steroid Biochem. , vol.25 , pp. 787-790
    • James, V.H.T.1    McNeil, J.M.2    Beranek, P.A.3    vonney, R.C.4    Reed, M.J.5
  • 37
    • 0025151257 scopus 로고
    • Regulation of estrogen concentrations in human breast tissues
    • V.H.T. James M.J. Reed N.G. Coldham Regulation of estrogen concentrations in human breast tissues Ann. N.Y. Acad. Sci. 595 1990 227 235
    • (1990) Ann. N.Y. Acad. Sci. , vol.595 , pp. 227-235
    • James, V.H.T.1    Reed, M.J.2    Coldham, N.G.3
  • 40
    • 0026737624 scopus 로고
    • Subunit identity of the dimeric 17β-hydroxysteroid dehydrogenase from human placenta
    • S.X. Lin F. Yang J.Z. Jin R. Breton D.W. Zhu V. Luu-Thé F. Labrie Subunit identity of the dimeric 17β-hydroxysteroid dehydrogenase from human placenta J. Biol. Chem. 267 1992 16182 16187
    • (1992) J. Biol. Chem. , vol.267 , pp. 16182-16187
    • Lin, S.X.1    Yang, F.2    Jin, J.Z.3    Breton, R.4    Zhu, D.W.5    Luu-Thé, V.6    Labrie, F.7
  • 41
    • 0024361957 scopus 로고
    • Characterization of cDNAs for human estradiol 17β-dehydrogenase and assignment of the gene to chromosome 17: Evidence of two mRNA species with distinct 5′ termini in human placenta
    • V. Luu-Thé Y. Lachance C. Labrie G. Leblanc J.L. Thomas R.C. Strickler F. Labrie Characterization of cDNAs for human estradiol 17β-dehydrogenase and assignment of the gene to chromosome 17: Evidence of two mRNA species with distinct 5′ termini in human placenta Mol. Endocrinol. 3 1989 1301 1309
    • (1989) Mol. Endocrinol. , vol.3 , pp. 1301-1309
    • Luu-Thé, V.1    Lachance, Y.2    Labrie, C.3    Leblanc, G.4    Thomas, J.L.5    Strickler, R.C.6    Labrie, F.7
  • 42
    • 0026333956 scopus 로고
    • Immunohistochemical localization of 17β-hydroxysteroid dehydrogenase in the human endometrium during the menstrual cycle
    • O. Mäentausta R. Sormunen V. Isomaa V.P. Lehto P. Jouppila R. Vihko Immunohistochemical localization of 17β-hydroxysteroid dehydrogenase in the human endometrium during the menstrual cycle Lab. Invest. 65 1991 582 587
    • (1991) Lab. Invest. , vol.65 , pp. 582-587
    • Mäentausta, O.1    Sormunen, R.2    Isomaa, V.3    Lehto, V.P.4    Jouppila, P.5    Vihko, R.6
  • 43
    • 0026781142 scopus 로고
    • Immunohistochemical study of the human 17β-hydroxysteroid dehydrogenase and steroid receptors in endometrial adenocarcinoma
    • O. Mäentausta K. Boman V. Isomaa U. Stendahl T. Backstrom R. Vihko Immunohistochemical study of the human 17β-hydroxysteroid dehydrogenase and steroid receptors in endometrial adenocarcinoma Cancer (Philadelphia) 70 1992 1551 1555
    • (1992) Cancer (Philadelphia) , vol.70 , pp. 1551-1555
    • Mäentausta, O.1    Boman, K.2    Isomaa, V.3    Stendahl, U.4    Backstrom, T.5    Vihko, R.6
  • 44
    • 0032478702 scopus 로고    scopus 로고
    • Unusual charge stabilization of NADP+ in 17β-hydroxysteroid dehydrogenase
    • C. Mazza R. Breton D. Housset J.C. Fontacilla-Camps Unusual charge stabilization of NADP+ in 17β-hydroxysteroid dehydrogenase J. Biol. Chem. 273 1998 8145 8152
    • (1998) J. Biol. Chem. , vol.273 , pp. 8145-8152
    • Mazza, C.1    Breton, R.2    Housset, D.3    Fontacilla-Camps, J.C.4
  • 46
    • 0002990491 scopus 로고
    • A genetic defect in cortisol metabolism as the basis for the syndrome of apparent mineralocorticoid excess
    • M.I. New S.E. Oberfield R. Carey F. Greig S. Ulick L.S. Levind A genetic defect in cortisol metabolism as the basis for the syndrome of apparent mineralocorticoid excess Proc. Serono Sympo. 50 1982 85 101
    • (1982) , pp. 85-101
    • New, M.I.1    Oberfield, S.E.2    Carey, R.3    Greig, F.4    Ulick, S.5    Levind, L.S.6
  • 47
    • 0023691704 scopus 로고
    • Complete amino acid sequence of human placental 17β-hydroxysteroid dehydrogenase deduced from cDNA
    • H. Peltoketo V. Isomaa O.I. Mäentausta R.K. Vihko Complete amino acid sequence of human placental 17β-hydroxysteroid dehydrogenase deduced from cDNA FEBS Lett. 239 1988 73 77
    • (1988) FEBS Lett. , vol.239 , pp. 73-77
    • Peltoketo, H.1    Isomaa, V.2    Mäentausta, O.I.3    Vihko, R.K.4
  • 49
    • 0026557238 scopus 로고
    • Immunological analysis of 17β-hydroxysteroid dehydrogenase in benign and malignant human breast tissue
    • M.H. Poutanen V. Isomaa V.P. Lehto R.K. Vihko Immunological analysis of 17β-hydroxysteroid dehydrogenase in benign and malignant human breast tissue Int. J. Cancer 50 1992 386 390
    • (1992) Int. J. Cancer , vol.50 , pp. 386-390
    • Poutanen, M.H.1    Isomaa, V.2    Lehto, V.P.3    Vihko, R.K.4
  • 50
    • 0027138652 scopus 로고
    • Differential estrogen substrate specificity for transiently expressed human placental 17β-hydroxysteroid dehydrogenase and an endogenous enzymne expressed in cultured COS-m6 cells
    • M.H. Poutanen M. Miettinen R.K. Vihko Differential estrogen substrate specificity for transiently expressed human placental 17β-hydroxysteroid dehydrogenase and an endogenous enzymne expressed in cultured COS-m6 cells Endocrinology (Baltimore) 133 1993 2639 2644
    • (1993) Endocrinology (Baltimore) , vol.133 , pp. 2639-2644
    • Poutanen, M.H.1    Miettinen, M.2    Vihko, R.K.3
  • 51
    • 0029621925 scopus 로고
    • Role of 17β-hydroxysteroid dehydrogenase type 1 in endocrine and intracrine estradiol biosynthesis
    • M. Poutanen V. Isomaa H. Peltoketo R.K. Vihko Role of 17β-hydroxysteroid dehydrogenase type 1 in endocrine and intracrine estradiol biosynthesis Steroid Biochem. Mol. Biol. 55 1995 525 532
    • (1995) Steroid Biochem. Mol. Biol. , vol.55 , pp. 525-532
    • Poutanen, M.1    Isomaa, V.2    Peltoketo, H.3    Vihko, R.K.4
  • 52
    • 0027959919 scopus 로고
    • Site-directed mutagenesis of the putative active site of human 17β-hydroxysteroid dehydrogenase type 1
    • T.J. Puranen M.H. Poutanen H.W. Peltoketo P.T. Vihko R.K. Vihko Site-directed mutagenesis of the putative active site of human 17β-hydroxysteroid dehydrogenase type 1 Biochem. J. 304 1994 289 293
    • (1994) Biochem. J. , vol.304 , pp. 289-293
    • Puranen, T.J.1    Poutanen, M.H.2    Peltoketo, H.W.3    Vihko, P.T.4    Vihko, R.K.5
  • 53
    • 0031027687 scopus 로고    scopus 로고
    • Characterization of structural and functional properties of human 17β-hydroxysteroid dehydrogenase type 1 using recombinant enzymes and site directed mutagenesis
    • T.J. Puranen M.H. Poutanen D. Ghosh P.T. Vihko R.K. Vihko Characterization of structural and functional properties of human 17β-hydroxysteroid dehydrogenase type 1 using recombinant enzymes and site directed mutagenesis Mol. Endocrinol. 11 1997 77 86
    • (1997) Mol. Endocrinol. , vol.11 , pp. 77-86
    • Puranen, T.J.1    Poutanen, M.H.2    Ghosh, D.3    Vihko, P.T.4    Vihko, R.K.5
  • 54
    • 0030786399 scopus 로고    scopus 로고
    • Origin of substrate specificity of human and rat 17β-hydroxysteroid dehydroigenase type 1, using chimeric enzymes and site directed mutagenesis
    • T.J. Puranen M.H. Poutanen D. Ghosh P.T. Vihko R.K. Vihko Origin of substrate specificity of human and rat 17β-hydroxysteroid dehydroigenase type 1, using chimeric enzymes and site directed mutagenesis Endocrinology (Baltimore) 138 1997 3532 3539
    • (1997) Endocrinology (Baltimore) , vol.138 , pp. 3532-3539
    • Puranen, T.J.1    Poutanen, M.H.2    Ghosh, D.3    Vihko, P.T.4    Vihko, R.K.5
  • 55
    • 0029645410 scopus 로고
    • Common themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase
    • J.B. Rafferty J.W. Simon C. Baldock P.J. Artymiuk P.J. Baker A.R. Stuije A.R. Slabas D.W. Rice Common themes in redox chemistry emerge from the X-ray structure of oilseed rape ( Brassica napus ) enoyl acyl carrier protein reductase Structure 3 1995 927 938
    • (1995) Structure , vol.3 , pp. 927-938
    • Rafferty, J.B.1    Simon, J.W.2    Baldock, C.3    Artymiuk, P.J.4    Baker, P.J.5    Stuije, A.R.6    Slabas, A.R.7    Rice, D.W.8
  • 56
    • 0028246997 scopus 로고
    • The active site architecture of a short chain dehydrogenase defined by site-directed mutagenesis and structure-modeling
    • L. Ribos-de-Pouplona L.A. Fothergall-Gilmore The active site architecture of a short chain dehydrogenase defined by site-directed mutagenesis and structure-modeling Biochemistry 33 1994 7047 7055
    • (1994) Biochemistry , vol.33 , pp. 7047-7055
    • Ribos-de-Pouplona, L.1    Fothergall-Gilmore, L.A.2
  • 57
    • 0032472224 scopus 로고    scopus 로고
    • Modification of the NADH of the isoniazid target (INHA) from Mycobacterium tuberculosis
    • D.A. Rozwarski G.A. Grant D.H.R. Barton W.R. Jacobs Jr. J.C. Sacchettini Modification of the NADH of the isoniazid target (INHA) from Mycobacterium tuberculosis Science 279 1998 98 102
    • (1998) Science , vol.279 , pp. 98-102
    • Rozwarski, D.A.1    Grant, G.A.2    Barton, D.H.R.3    Jacobs, W.R.4    Sacchettini, J.C.5
  • 58
    • 0033514308 scopus 로고    scopus 로고
    • Structure of the ternary complex of human 17β-hydroxysteroid dehydrogenase type 1 with 3-hydroxyestra-1,3,5,7-tetraen-17-one (equilin) and NADP+
    • M.W. Sawicki M. Erman T.J. Puranen V. Pirkko D. Ghosh Structure of the ternary complex of human 17β-hydroxysteroid dehydrogenase type 1 with 3-hydroxyestra-1,3,5,7-tetraen-17-one (equilin) and NADP+ Proc. Natl. Acad. Sci. U.S.A. 96 1999 840 845
    • (1999) , pp. 840-845
    • Sawicki, M.W.1    Erman, M.2    Puranen, T.J.3    Pirkko, V.4    Ghosh, D.5
  • 60
    • 0025019734 scopus 로고
    • Redesign of the coenzyme specificity of a dehydrogenase by protein engineering
    • N.S. Scrutton A. Berry R.N. Perham Redesign of the coenzyme specificity of a dehydrogenase by protein engineering Nature (London) 343 1990 38 43
    • (1990) Nature (London) , vol.343 , pp. 38-43
    • Scrutton, N.S.1    Berry, A.2    Perham, R.N.3
  • 61
    • 0019316280 scopus 로고
    • Bifunctional enzyme activity at the same active site: Study of 3α,20β-hydroxysteroid dehydrogenase with 17-(bromoacetoxy)steroids
    • F. Sweet B.R. Samant Bifunctional enzyme activity at the same active site: Study of 3α,20β-hydroxysteroid dehydrogenase with 17-(bromoacetoxy)steroids Biochemistry 19 1980 978 986
    • (1980) Biochemistry , vol.19 , pp. 978-986
    • Sweet, F.1    Samant, B.R.2
  • 62
    • 0029643855 scopus 로고    scopus 로고
    • Crystal structure of the ternary complex of mouse lung carvonyl reductase at 1.8Å resolution: The structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family
    • N. Tanaka T. Nonaka M. Nakanishi Y. Deyashiki A. Hara Y. Mitsui Crystal structure of the ternary complex of mouse lung carvonyl reductase at 1.8Å resolution: The structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family Structure 4 1996 33 45
    • (1996) Structure , vol.4 , pp. 33-45
    • Tanaka, N.1    Nonaka, T.2    Nakanishi, M.3    Deyashiki, Y.4    Hara, A.5    Mitsui, Y.6
  • 63
    • 0030000879 scopus 로고    scopus 로고
    • Crystal structures of the binary and ternary complexes of 7α-hydroxysteroid dehydrogenase from E. coli
    • N. Tanaka T. Nonaka T. Tanabe T. Yashimoto D. Tsuru Y. Mitsui Crystal structures of the binary and ternary complexes of 7α-hydroxysteroid dehydrogenase from E. coli Biochemistry 35 1996 7715 7730
    • (1996) Biochemistry , vol.35 , pp. 7715-7730
    • Tanaka, N.1    Nonaka, T.2    Tanabe, T.3    Yashimoto, T.4    Tsuru, D.5    Mitsui, Y.6
  • 65
  • 66
    • 0011350036 scopus 로고
    • Structure of glyceraldehyde-3-phosphate dehydrogenase
    • H.C. Watson L.J. vanaszak Structure of glyceraldehyde-3-phosphate dehydrogenase Nature (London) 204 1964 918 920
    • (1964) Nature (London) , vol.204 , pp. 918-920
    • Watson, H.C.1    vanaszak, L.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.