메뉴 건너뛰기




Volumn 143-144, Issue , 2003, Pages 493-501

Significance of individual amino acid residues for coenzyme and substrate specificity of 17β-hydroxysteroid dehydrogenase from the fungus Cochliobolus lunatus

Author keywords

17 Hydroxysteroid dehydrogenase; Cochliobolus lunatus; Fungi; SDR

Indexed keywords

30ALPHA,20BETA HYDROXYSTEROID DEHYDROGENASE; ALCOHOL DEHYDROGENASE; AMINO ACID; ESTR 4 ENE 3,17 DIONE; NANDROLONE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; RECOMBINANT PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TESTOSTERONE 17BETA DEHYDROGENASE; UNCLASSIFIED DRUG;

EID: 0344642993     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(02)00205-3     Document Type: Conference Paper
Times cited : (19)

References (30)
  • 1
    • 0036183076 scopus 로고    scopus 로고
    • Short-chain dehydrogenase/reductase (SDR) relationships: A large family with eight clusters common to human, animal, and plant genomes
    • Kallberg Y., Oppermann U., Joernvall H., Persson B. Short-chain dehydrogenase/reductase (SDR) relationships: a large family with eight clusters common to human, animal, and plant genomes. Prot. Sci. 11:2002;636-641.
    • (2002) Prot. Sci. , vol.11 , pp. 636-641
    • Kallberg, Y.1    Oppermann, U.2    Joernvall, H.3    Persson, B.4
  • 3
    • 0039699818 scopus 로고    scopus 로고
    • SDR and MDR: Completed genome sequences show these protein families to be large, of old origin and of complex nature
    • Joernvall H., Hoog J.O., Persson B. SDR and MDR: completed genome sequences show these protein families to be large, of old origin and of complex nature. FEBS Lett. 445:1999;254-261.
    • (1999) FEBS Lett. , vol.445 , pp. 254-261
    • Joernvall, H.1    Hoog, J.O.2    Persson, B.3
  • 4
    • 0030925341 scopus 로고    scopus 로고
    • Molecular endocrinology of hydroxysteroid dehydrogenases
    • Penning T.M. Molecular endocrinology of hydroxysteroid dehydrogenases. Endocr. Rev. 18:1997;281-305.
    • (1997) Endocr. Rev. , vol.18 , pp. 281-305
    • Penning, T.M.1
  • 5
    • 0027959548 scopus 로고
    • The short-chain alcohol dehydrogenase superfamily: Variations on a common theme
    • Krozowski Z. The short-chain alcohol dehydrogenase superfamily: variations on a common theme. J. Steroid Biochem. Mol. Biol. 51:1994;125-130.
    • (1994) J. Steroid Biochem. Mol. Biol. , vol.51 , pp. 125-130
    • Krozowski, Z.1
  • 6
    • 0031021249 scopus 로고    scopus 로고
    • Active site directed mutagenesis of 3β/17β-hydroxysteroid dehydrogenase establishes differential effects on short-chain dehydrogenase/reductase reaction
    • Oppermann U.C., Filling C., Berndt K.D., Persson B., Benach J., Ladenstein R., Jornvall H. Active site directed mutagenesis of 3β/17β-hydroxysteroid dehydrogenase establishes differential effects on short-chain dehydrogenase/reductase reaction. Biochemistry. 36:1997;34-40.
    • (1997) Biochemistry , vol.36 , pp. 34-40
    • Oppermann, U.C.1    Filling, C.2    Berndt, K.D.3    Persson, B.4    Benach, J.5    Ladenstein, R.6    Jornvall, H.7
  • 7
    • 0031716024 scopus 로고    scopus 로고
    • Roles of the Ser146, Tyr159, and Lys163 residues in the catalytic action of 7α-hydroxysteroid dehydrogenase from Escherichia coli
    • Tanabe T., Tanaka N., Uchikawa K., Kabashima T., Ito K., Nonaka T., Mitsui Y., Tsuru M., Yoshimoto T. Roles of the Ser146, Tyr159, and Lys163 residues in the catalytic action of 7α-hydroxysteroid dehydrogenase from Escherichia coli. J. Biochem. 124:1998;634-641.
    • (1998) J. Biochem. , vol.124 , pp. 634-641
    • Tanabe, T.1    Tanaka, N.2    Uchikawa, K.3    Kabashima, T.4    Ito, K.5    Nonaka, T.6    Mitsui, Y.7    Tsuru, M.8    Yoshimoto, T.9
  • 10
    • 0032575502 scopus 로고    scopus 로고
    • Characterization of Ke6, a new 17β-hydroxysteroid dehydrogenase, and its expression in gonadal tissues
    • Fomitcheva J., Baker M.E., Anderson E., Lee G.Y., Aziz N. Characterization of Ke6, a new 17β-hydroxysteroid dehydrogenase, and its expression in gonadal tissues. J. Biol. Chem. 273:1998;22664-22671.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22664-22671
    • Fomitcheva, J.1    Baker, M.E.2    Anderson, E.3    Lee, G.Y.4    Aziz, N.5
  • 12
    • 0033591454 scopus 로고    scopus 로고
    • Human brain short-chain L-3-hydroxyacyl coenzyme A dehydrogenase is a single domain multifunctional enzyme
    • He X.Z., Merz G., Mehta P., Schultz H., Yang S.-Y. Human brain short-chain L-3-hydroxyacyl coenzyme A dehydrogenase is a single domain multifunctional enzyme. J. Biol. Chem. 274:1999;15014-15019.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15014-15019
    • He, X.Z.1    Merz, G.2    Mehta, P.3    Schultz, H.4    Yang, S.-Y.5
  • 14
    • 0030251001 scopus 로고    scopus 로고
    • Purification and characterization of 17β-hydroxysteroid dehydrogenase from the filamentous fungus Cochliobolus lunatus
    • Lanišnik Rižner T., Žakelj-Mavrič M., Plemenitaš A., Zorko M. Purification and characterization of 17β-hydroxysteroid dehydrogenase from the filamentous fungus Cochliobolus lunatus. J. Steroid Biochem. Mol. Biol. 59:1996;205-214.
    • (1996) J. Steroid Biochem. Mol. Biol. , vol.59 , pp. 205-214
    • Lanišnik Rižner, T.1    Žakelj-Mavrič, M.2    Plemenitaš, A.3    Zorko, M.4
  • 15
    • 0039848368 scopus 로고    scopus 로고
    • A novel 17β-hydroxysteroid dehydrogenase in the fungus Cochliobolus lunatus: New insights into the evolution of steroid-hormone signalling
    • Lanišnik Rižner T., Moeller G., Thole H.H., Žakelj-Mavrič M., Adamski J. A novel 17β-hydroxysteroid dehydrogenase in the fungus Cochliobolus lunatus: new insights into the evolution of steroid-hormone signalling. Biochem. J. 337:1999;425-431.
    • (1999) Biochem. J. , vol.337 , pp. 425-431
    • Lanišnik Rižner, T.1    Moeller, G.2    Thole, H.H.3    Žakelj-Mavrič, M.4    Adamski, J.5
  • 16
    • 17044454420 scopus 로고    scopus 로고
    • 17β-Hydroxysteroid dehydrogenase from the fungus Cochliobolus lunatus: Structural and functional aspects
    • Lanišnik Rižner T., Stojan J., Adamski J. 17β-Hydroxysteroid dehydrogenase from the fungus Cochliobolus lunatus: structural and functional aspects. Chem.-Biol. Interact. 130-132:2001;793-803.
    • (2001) Chem.-Biol. Interact. , vol.130-132 , pp. 793-803
    • Lanišnik Rižner, T.1    Stojan, J.2    Adamski, J.3
  • 17
    • 0034670381 scopus 로고    scopus 로고
    • 17β-Hydroxysteroid dehydrogenase from Cochliobolus lunatus: Model structure and substrate specificity
    • Lanišnik Rižner T., Adamski J., Stojan J. 17β-Hydroxysteroid dehydrogenase from Cochliobolus lunatus: model structure and substrate specificity. Arch. Biochem. Biophys. 384:2000;255-262.
    • (2000) Arch. Biochem. Biophys. , vol.384 , pp. 255-262
    • Lanišnik Rižner, T.1    Adamski, J.2    Stojan, J.3
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0036066976 scopus 로고    scopus 로고
    • Progressive loss of PAX9 expression correlates with increasing malignancy of dysplastic and cancerous epithelium of the human oesophagus
    • Gerber J.K., Richter T., Kremmer E., Adamski J., Hofler H., Balling R., Peters H. Progressive loss of PAX9 expression correlates with increasing malignancy of dysplastic and cancerous epithelium of the human oesophagus. J. Pathol. 197:2002;293-297.
    • (2002) J. Pathol. , vol.197 , pp. 293-297
    • Gerber, J.K.1    Richter, T.2    Kremmer, E.3    Adamski, J.4    Hofler, H.5    Balling, R.6    Peters, H.7
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0029683826 scopus 로고    scopus 로고
    • Involvement of two basic residues (Lys17 and Arg39) of mouse lung carbonyl reductase in NADP(H)-binding and fatty acid activation: Site directed mutagenesis and kinetic analysis
    • Nakanishi M., Kakumoto M., Matsuura K., Deyashiki Y., Tanaka N., Nonaka T., Mitsui Y., Hara A. Involvement of two basic residues (Lys17 and Arg39) of mouse lung carbonyl reductase in NADP(H)-binding and fatty acid activation: site directed mutagenesis and kinetic analysis. J. Biochem. 120:1996;257-263.
    • (1996) J. Biochem. , vol.120 , pp. 257-263
    • Nakanishi, M.1    Kakumoto, M.2    Matsuura, K.3    Deyashiki, Y.4    Tanaka, N.5    Nonaka, T.6    Mitsui, Y.7    Hara, A.8
  • 24
    • 0029643855 scopus 로고
    • Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 Å resolution: The structure origin of the coenzyme specificity in the short-chain dehydrogenase/reductase family
    • Tanaka N., Nonaka T., Nakanishi M., Deyashiki Y., Hara A., Mitsui Y. Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 Å resolution: the structure origin of the coenzyme specificity in the short-chain dehydrogenase/reductase family. Structure. 4:1995;33-45.
    • (1995) Structure , vol.4 , pp. 33-45
    • Tanaka, N.1    Nonaka, T.2    Nakanishi, M.3    Deyashiki, Y.4    Hara, A.5    Mitsui, Y.6
  • 25
    • 0030587782 scopus 로고    scopus 로고
    • Crystal structure of the ternary complex of 1,3,8-trihydroxy-naphthalene reductase from Magnaporthe grisea with NADPH and an active-site inhibitor
    • Andersson S., Jordan D., Schneider G., Lundqvist Y. Crystal structure of the ternary complex of 1,3,8-trihydroxy-naphthalene reductase from Magnaporthe grisea with NADPH and an active-site inhibitor. Structure. 4:1996;1161-1170.
    • (1996) Structure , vol.4 , pp. 1161-1170
    • Andersson, S.1    Jordan, D.2    Schneider, G.3    Lundqvist, Y.4
  • 26
    • 0030000879 scopus 로고    scopus 로고
    • Crystal structures of the binary and ternary complexes of 7α-hydroxysteroid dehydrogenases from Escherichia coli
    • Tanaka N., Nonaka T., Tanabe T., Yoshimoto T., Tsuru D., Mitsui Y. Crystal structures of the binary and ternary complexes of 7α-hydroxysteroid dehydrogenases from Escherichia coli. Biochemistry. 35:1996;7715-7730.
    • (1996) Biochemistry , vol.35 , pp. 7715-7730
    • Tanaka, N.1    Nonaka, T.2    Tanabe, T.3    Yoshimoto, T.4    Tsuru, D.5    Mitsui, Y.6
  • 28
    • 0032544367 scopus 로고    scopus 로고
    • The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 Å resolution
    • Benach J., Atrian S., Gonzales-Duarte R., Ladenstein R. The refined crystal structure of Drosophila lebanonensis 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    Gonzales-Duarte, R.3    Ladenstein, R.4
  • 29
    • 0034749467 scopus 로고    scopus 로고
    • Critical residues for the specificity of cofactors and substrates in human estrogenic 17β-hydroxysteroid dehydrogenase 1: Variants designed from the three-dimensional structure of the enzyme
    • Huang Y.-W., Pineau I., Chang H.-J., Azzi A., Bellemare V., Laberge S., Lin S.-X. Critical residues for the specificity of cofactors and substrates in human estrogenic 17β-hydroxysteroid dehydrogenase 1: variants designed from the three-dimensional structure of the enzyme. Mol. Endocrinol. 15:2001;2010-2020.
    • (2001) Mol. Endocrinol. , vol.15 , pp. 2010-2020
    • Huang, Y.-W.1    Pineau, I.2    Chang, H.-J.3    Azzi, A.4    Bellemare, V.5    Laberge, S.6    Lin, S.-X.7
  • 30
    • 0030786399 scopus 로고    scopus 로고
    • Origin of substrate specificity of human and rat 17β-hydroxysteroid dehydrogenase type 1, using chimeric enzymes and site-directed substitutions
    • Puranen T., Poutanen M., Ghosh D., Vihko R., Vihko P. Origin of substrate specificity of human and rat 17β-hydroxysteroid dehydrogenase type 1, using chimeric enzymes and site-directed substitutions. Endocrinology. 138:1997;3532-3539.
    • (1997) Endocrinology , vol.138 , pp. 3532-3539
    • Puranen, T.1    Poutanen, M.2    Ghosh, D.3    Vihko, R.4    Vihko, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.