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Volumn 71, Issue 4, 2010, Pages 241-249

Evolution of enzymatic activities of testis-specific short-chain dehydrogenase/reductase in drosophila

Author keywords

Drosophila; Drosophila alcohol dehydrogenase; Enzyme evolution; Exon shuffling; Short chain dehydrogenase reductase

Indexed keywords

ALCOHOL DEHYDROGENASE; CHIMERIC PROTEIN; DETERGENT; DROSOPHILA PROTEIN; FATTY ACID SYNTHASE; JINGWEI PROTEIN, DROSOPHILA; OXIDOREDUCTASE; SHORT CHAIN TRANS 2 ENOYL COA REDUCTASE; SHORT CHAIN TRANS-2-ENOYL-COA REDUCTASE;

EID: 77957559994     PISSN: 00222844     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00239-010-9384-5     Document Type: Article
Times cited : (15)

References (41)
  • 1
    • 0017058392 scopus 로고
    • Evolution of enzyme function and the development of catalytic efficiency
    • DOI 10.1021/bi00670a032
    • WJ Albery JR Knowles 1976 Evolution of enzyme function and the development of catalytic efficiency Biochemistry 15 5631 5640 10.1021/bi00670a032 999839 1:CAS:528:DyaE2sXlt1Wrsw%3D%3D (Pubitemid 8004280)
    • (1976) Biochemistry , vol.15 , Issue.25 , pp. 5631-5640
    • Albery, W.J.1    Knowles, J.R.2
  • 2
    • 0030667789 scopus 로고    scopus 로고
    • Understanding enzyme superfamilies. Chemistry as the fundamental determinant in the evolution of new catalytic activities
    • DOI 10.1074/jbc.272.49.30591
    • PC Babbitt JA Gerlt 1997 Understanding enzyme superfamilies. Chemistry as the fundamental determinant in the evolution of new catalytic activities J Biol Chem 272 30591 30594 10.1074/jbc.272.49.30591 9388188 1:CAS:528: DyaK2sXnvFSlsbg%3D (Pubitemid 27527485)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.49 , pp. 30591-30594
    • Babbitt, P.C.1    Gerlt, J.A.2
  • 3
    • 0029651191 scopus 로고
    • A functionally diverse enzyme superfamily that abstracts the alpha protons of carboxylic acids
    • 10.1126/science.7855594 7855594 1:CAS:528:DyaK2MXktVKjsLc%3D
    • PC Babbitt GT Mrachko MS Hasson GW Huisman R Kolter D Ringe GA Petsko GL Kenyon JA Gerlt 1995 A functionally diverse enzyme superfamily that abstracts the alpha protons of carboxylic acids Science 267 1159 1161 10.1126/science. 7855594 7855594 1:CAS:528:DyaK2MXktVKjsLc%3D
    • (1995) Science , vol.267 , pp. 1159-1161
    • Babbitt, P.C.1    Mrachko, G.T.2    Hasson, M.S.3    Huisman, G.W.4    Kolter, R.5    Ringe, D.6    Petsko, G.A.7    Kenyon, G.L.8    Gerlt, J.A.9
  • 4
    • 0032544367 scopus 로고    scopus 로고
    • The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 A resolution
    • DOI 10.1006/jmbi.1998.2015
    • J Benach S Atrian R Gonzalez-Duarte R Ladenstein 1998 The refined crystal structure of Drosophila lebanonensis alcohol dehydrogenase at 1.9 A resolution J Mol Biol 282 383 399 10.1006/jmbi.1998.2015 9735295 1:CAS:528: DyaK1cXmtlClsb0%3D (Pubitemid 28418791)
    • (1998) Journal of Molecular Biology , vol.282 , Issue.2 , pp. 383-399
    • Benach, J.1    Atrian, S.2    Gonzalez-Duarte, R.3    Ladenstein, R.4
  • 5
    • 0033523083 scopus 로고    scopus 로고
    • The catalytic reaction and inhibition mechanism of Drosophila alcohol dehydrogenase: Observation of an enzyme-bound NAD-ketone adduct at 1.4 A resolution by X-ray crystallography
    • DOI 10.1006/jmbi.1999.2765
    • J Benach S Atrian R Gonzalez-Duarte R Ladenstein 1999 The catalytic reaction and inhibition mechanism of Drosophila alcohol dehydrogenase: observation of an enzyme-bound NAD-ketone adduct at 1.4 A resolution by X-ray crystallography J Mol Biol 289 335 355 10.1006/jmbi.1999.2765 10366509 1:CAS:528:DyaK1MXjslSltL8%3D (Pubitemid 29278386)
    • (1999) Journal of Molecular Biology , vol.289 , Issue.2 , pp. 335-355
    • Benach, J.1    Atrian, S.2    Gonzalez-Duarte, R.3    Ladenstein, R.4
  • 6
    • 0035969839 scopus 로고    scopus 로고
    • Genesis of Drosophila ADH: The shaping of the enzymatic activity from a SDR ancestor
    • DOI 10.1016/S0009-2797(00)00265-9, PII S0009279700002659
    • J Benach S Atrian R Ladenstein R Gonzalez-Duarte 2001 Genesis of Drosophila ADH: the shaping of the enzymatic activity from a SDR ancestor Chem Biol Interact 130-132 405 415 10.1016/S0009-2797(00)00265-9 11306062 (Pubitemid 32295831)
    • (2001) Chemico-Biological Interactions , vol.130-132 , pp. 405-415
    • Benach, J.1    Atrian, S.2    Ladenstein, R.3    Gonzalez-Duarte, R.4
  • 7
    • 9644266658 scopus 로고    scopus 로고
    • Drosophila alcohol dehydrogenase: Acetate-enzyme interactions and novel insights into the effects of electrostatics on catalysis
    • DOI 10.1016/j.jmb.2004.10.028, PII S0022283604013208
    • J Benach JO Winberg JS Svendsen S Atrian R Gonzalez-Duarte R Ladenstein 2005 Drosophila alcohol dehydrogenase: acetate-enzyme interactions and novel insights into the effects of electrostatics on catalysis J Mol Biol 345 579 598 10.1016/j.jmb.2004.10.028 15581900 1:CAS:528:DC%2BD2cXhtVCnsrrJ (Pubitemid 39575926)
    • (2005) Journal of Molecular Biology , vol.345 , Issue.3 , pp. 579-598
    • Benach, J.1    Winberg, J.-O.2    Svendsen, J.-S.3    Atrian, S.4    Gonzalez-Duarte, R.5    Ladenstein, R.6
  • 8
    • 0033969946 scopus 로고    scopus 로고
    • Solvent accessibility and purifying selection within proteins of Escherichia coli and Salmonella enterica
    • 10677853 1:CAS:528:DC%2BD3cXosFyntg%3D%3D
    • CD Bustamante JP Townsend DL Hartl 2000 Solvent accessibility and purifying selection within proteins of Escherichia coli and Salmonella enterica Mol Biol Evol 17 301 308 10677853 1:CAS:528:DC%2BD3cXosFyntg%3D%3D
    • (2000) Mol Biol Evol , vol.17 , pp. 301-308
    • Bustamante, C.D.1    Townsend, J.P.2    Hartl, D.L.3
  • 9
    • 0025821146 scopus 로고
    • Gene expression, adaptation and evolution in higher organisms. Evidence from studies of Drosophila alcohol dehydrogenases
    • 10.1016/0305-0491(91)90135-Z 1790667 1:STN:280:DyaK387msVaqsg%3D%3D
    • GK Chambers 1991 Gene expression, adaptation and evolution in higher organisms. Evidence from studies of Drosophila alcohol dehydrogenases Comp Biochem Physiol B 99 723 730 10.1016/0305-0491(91)90135-Z 1790667 1:STN:280:DyaK387msVaqsg%3D%3D
    • (1991) Comp Biochem Physiol B , vol.99 , pp. 723-730
    • Chambers, G.K.1
  • 10
    • 0025166586 scopus 로고
    • Site-directed mutagenesis of glycine-14 and two "critical" cysteinyl residues in Drosophila alcohol dehydrogenase
    • 10.1021/bi00457a003 2108721 1:CAS:528:DyaK3cXnt1yktA%3D%3D
    • Z Chen L Lu M Shirley WR Lee SH Chang 1990 Site-directed mutagenesis of glycine-14 and two "critical" cysteinyl residues in Drosophila alcohol dehydrogenase Biochemistry 29 1112 1118 10.1021/bi00457a003 2108721 1:CAS:528:DyaK3cXnt1yktA%3D%3D
    • (1990) Biochemistry , vol.29 , pp. 1112-1118
    • Chen, Z.1    Lu, L.2    Shirley, M.3    Lee, W.R.4    Chang, S.H.5
  • 11
    • 0029039935 scopus 로고
    • Amino acids important in enzyme activity and dimer stability for Drosophila alcohol dehydrogenase
    • 7772022 1:CAS:528:DyaK2MXmtFeku7k%3D
    • SW Chenevert NG Fossett SH Chang I Tsigelny ME Baker WR Lee 1995 Amino acids important in enzyme activity and dimer stability for Drosophila alcohol dehydrogenase Biochem J 308 Pt 2 419 423 7772022 1:CAS:528:DyaK2MXmtFeku7k%3D
    • (1995) Biochem J , vol.308 , Issue.PART 2 , pp. 419-423
    • Chenevert, S.W.1    Fossett, N.G.2    Chang, S.H.3    Tsigelny, I.4    Baker, M.E.5    Lee, W.R.6
  • 12
    • 0036856289 scopus 로고    scopus 로고
    • The pattern of amino acid replacements in alpha/beta-barrels
    • 12411594 1:CAS:528:DC%2BD38XovFOntLg%3D
    • AM Dean C Neuhauser E Grenier GB Golding 2002 The pattern of amino acid replacements in alpha/beta-barrels Mol Biol Evol 19 1846 1864 12411594 1:CAS:528:DC%2BD38XovFOntLg%3D
    • (2002) Mol Biol Evol , vol.19 , pp. 1846-1864
    • Dean, A.M.1    Neuhauser, C.2    Grenier, E.3    Golding, G.B.4
  • 13
    • 0031966661 scopus 로고    scopus 로고
    • The structural basis of molecular adaptation
    • 9549087 1:CAS:528:DyaK1cXitlKiurs%3D
    • GB Golding AM Dean 1998 The structural basis of molecular adaptation Mol Biol Evol 15 355 369 9549087 1:CAS:528:DyaK1cXitlKiurs%3D
    • (1998) Mol Biol Evol , vol.15 , pp. 355-369
    • Golding, G.B.1    Dean, A.M.2
  • 14
    • 0024669738 scopus 로고
    • The metabolism of ethanol-derived acetaldehyde by alcohol dehydrogenase (EC 1.1.1.1) and aldehyde dehydrogenase (EC 1.2.1.3) in Drosophila melanogaster larvae
    • 2499314 1:CAS:528:DyaL1MXitV2lsrY%3D
    • PW Heinstra BW Geer D Seykens M Langevin 1989 The metabolism of ethanol-derived acetaldehyde by alcohol dehydrogenase (EC 1.1.1.1) and aldehyde dehydrogenase (EC 1.2.1.3) in Drosophila melanogaster larvae Biochem J 259 791 797 2499314 1:CAS:528:DyaL1MXitV2lsrY%3D
    • (1989) Biochem J , vol.259 , pp. 791-797
    • Heinstra, P.W.1    Geer, B.W.2    Seykens, D.3    Langevin, M.4
  • 15
    • 0029151128 scopus 로고
    • Aldehyde dehydrogenase activity of Drosophila melanogaster alcohol dehydrogenase: Burst kinetics at high pH and aldehyde dismutase activity at physiological pH
    • 10.1021/bi00038a025 7547972 1:CAS:528:DyaK2MXnvVGnu7o%3D
    • GT Henehan SH Chang NJ Oppenheimer 1995 Aldehyde dehydrogenase activity of Drosophila melanogaster alcohol dehydrogenase: burst kinetics at high pH and aldehyde dismutase activity at physiological pH Biochemistry 34 12294 12301 10.1021/bi00038a025 7547972 1:CAS:528:DyaK2MXnvVGnu7o%3D
    • (1995) Biochemistry , vol.34 , pp. 12294-12301
    • Henehan, G.T.1    Chang, S.H.2    Oppenheimer, N.J.3
  • 16
    • 0001260894 scopus 로고
    • On the Evolution of Biochemical Syntheses
    • 10.1073/pnas.31.6.153 16578152 1:CAS:528:DyaH2MXjt1amsg%3D%3D
    • NH Horowitz 1945 On the Evolution of Biochemical Syntheses Proc Natl Acad Sci USA 31 153 157 10.1073/pnas.31.6.153 16578152 1:CAS:528: DyaH2MXjt1amsg%3D%3D
    • (1945) Proc Natl Acad Sci USA , vol.31 , pp. 153-157
    • Horowitz, N.H.1
  • 19
    • 0019554189 scopus 로고
    • Determination of some biochemical and structural features of alcohol dehydrogenases from Drosophila simulans and Drosophila virilis. Comparison of their properties with the Drosophila melanogaster Adhs enzyme
    • 6796069 1:CAS:528:DyaL3MXktlOrtr8%3D
    • E Juan R Gonzalez-Duarte 1981 Determination of some biochemical and structural features of alcohol dehydrogenases from Drosophila simulans and Drosophila virilis. Comparison of their properties with the Drosophila melanogaster Adhs enzyme Biochem J 195 61 69 6796069 1:CAS:528: DyaL3MXktlOrtr8%3D
    • (1981) Biochem J , vol.195 , pp. 61-69
    • Juan, E.1    Gonzalez-Duarte, R.2
  • 20
    • 57749177443 scopus 로고    scopus 로고
    • RNA-based gene duplication: Mechanistic and evolutionary insights
    • 10.1038/nrg2487 19030023 1:CAS:528:DC%2BD1cXhsFWis7bJ
    • H Kaessmann N Vinckenbosch M Long 2009 RNA-based gene duplication: mechanistic and evolutionary insights Nat Rev Genet 10 19 31 10.1038/nrg2487 19030023 1:CAS:528:DC%2BD1cXhsFWis7bJ
    • (2009) Nat Rev Genet , vol.10 , pp. 19-31
    • Kaessmann, H.1    Vinckenbosch, N.2    Long, M.3
  • 21
    • 58149114702 scopus 로고    scopus 로고
    • Medium- and short-chain dehydrogenase/reductase gene and protein families: Structure-function relationships in short-chain alcohol dehydrogenases
    • 10.1007/s00018-008-8590-4 19011748 1:CAS:528:DC%2BD1cXhsFCgs7nK
    • R Ladenstein JO Winberg J Benach 2008 Medium- and short-chain dehydrogenase/reductase gene and protein families: Structure-function relationships in short-chain alcohol dehydrogenases Cell Mol Life Sci 65 3918 3935 10.1007/s00018-008-8590-4 19011748 1:CAS:528:DC%2BD1cXhsFCgs7nK
    • (2008) Cell Mol Life Sci , vol.65 , pp. 3918-3935
    • Ladenstein, R.1    Winberg, J.O.2    Benach, J.3
  • 22
    • 0027905006 scopus 로고
    • Natural selection and the origin of jingwei, a chimeric processed functional gene in Drosophila
    • 10.1126/science.7682012 7682012 1:CAS:528:DyaK3sXit1OnsrY%3D
    • M Long CH Langley 1993 Natural selection and the origin of jingwei, a chimeric processed functional gene in Drosophila Science 260 91 95 10.1126/science.7682012 7682012 1:CAS:528:DyaK3sXit1OnsrY%3D
    • (1993) Science , vol.260 , pp. 91-95
    • Long, M.1    Langley, C.H.2
  • 23
    • 0032852328 scopus 로고    scopus 로고
    • Origin of new genes and source for N-terminal domain of the chimerical gene, jingwei, in Drosophila
    • DOI 10.1016/S0378-1119(99)00229-2, PII S0378111999002292
    • M Long W Wang J Zhang 1999 Origin of new genes and source for N-terminal domain of the chimerical gene, jingwei, in Drosophila Gene 238 135 141 10.1016/S0378-1119(99)00229-2 10570991 1:CAS:528:DyaK1MXntFKnurc%3D (Pubitemid 29437409)
    • (1999) Gene , vol.238 , Issue.1 , pp. 135-141
    • Long, M.1    Wang, W.2    Zhang, J.3
  • 24
    • 27144538817 scopus 로고    scopus 로고
    • Evolution: The biochemical architecture of an ancient adaptive landscape
    • DOI 10.1126/science.1115649
    • M Lunzer SP Miller R Felsheim AM Dean 2005 The biochemical architecture of an ancient adaptive landscape Science 310 499 501 10.1126/science.1115649 16239478 1:CAS:528:DC%2BD2MXhtFahtrvM (Pubitemid 41507965)
    • (2005) Science , vol.310 , Issue.5747 , pp. 499-501
    • Lunzer, M.1    Miller, S.P.2    Felsheim, R.3    Dean, A.M.4
  • 26
    • 0033593453 scopus 로고    scopus 로고
    • Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues
    • DOI 10.1074/jbc.274.4.2344
    • S Oue A Okamoto T Yano H Kagamiyama 1999 Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues J Biol Chem 274 2344 2349 10.1074/jbc.274.4.2344 9891001 1:CAS:528:DyaK1MXovVGktw%3D%3D (Pubitemid 29061393)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.4 , pp. 2344-2349
    • Oue, S.1    Okamoto, A.2    Yano, T.3    Kagamiyama, H.4
  • 27
    • 0025420076 scopus 로고
    • Measuring and increasing protein stability
    • 10.1016/0167-7799(90)90146-O 1367432 1:CAS:528:DyaK3cXltFWks7k%3D
    • CN Pace 1990 Measuring and increasing protein stability Trends Biotechnol 8 93 98 10.1016/0167-7799(90)90146-O 1367432 1:CAS:528:DyaK3cXltFWks7k%3D
    • (1990) Trends Biotechnol , vol.8 , pp. 93-98
    • Pace, C.N.1
  • 28
    • 0030729481 scopus 로고    scopus 로고
    • Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold
    • DOI 10.1074/jbc.272.48.29987
    • JJ Perona CS Craik 1997 Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold J Biol Chem 272 29987 29990 10.1074/jbc.272.48.29987 9374470 1:CAS:528:DyaK2sXnslGhtrk%3D (Pubitemid 27512189)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.48 , pp. 29987-29990
    • Perona, J.J.1    Craik, C.S.2
  • 30
    • 1342310509 scopus 로고    scopus 로고
    • Directed evolution relieves product inhibition and confers in vivo function to a rationally designed tyrosine aminotransferase
    • DOI 10.1110/ps.03117204
    • SC Rothman M Voorhies JF Kirsch 2004 Directed evolution relieves product inhibition and confers in vivo function to a rationally designed tyrosine aminotransferase Protein Sci 13 763 772 10.1110/ps.03117204 14767072 1:CAS:528:DC%2BD2cXhvVCmtbg%3D (Pubitemid 38252573)
    • (2004) Protein Science , vol.13 , Issue.3 , pp. 763-772
    • Rothman, S.C.1    Voorhies, M.2    Kirsch, J.F.3
  • 32
    • 0033850591 scopus 로고    scopus 로고
    • The origin of the Jingwei gene and the complex modular structure of its parental gene, yellow emperor, in Drosophila melanogaster
    • 10958846 1:CAS:528:DC%2BD3cXmtFyrtrw%3D
    • W Wang J Zhang C Alvarez A Llopart M Long 2000 The origin of the Jingwei gene and the complex modular structure of its parental gene, yellow emperor, in Drosophila melanogaster Mol Biol Evol 17 1294 1301 10958846 1:CAS:528: DC%2BD3cXmtFyrtrw%3D
    • (2000) Mol Biol Evol , vol.17 , pp. 1294-1301
    • Wang, W.1    Zhang, J.2    Alvarez, C.3    Llopart, A.4    Long, M.5
  • 33
    • 33645666942 scopus 로고    scopus 로고
    • Darwinian evolution can follow only very few mutational paths to fitter proteins
    • 10.1126/science.1123539 16601193 1:CAS:528:DC%2BD28XjtFalsLs%3D
    • DM Weinreich NF Delaney MA Depristo DL Hartl 2006 Darwinian evolution can follow only very few mutational paths to fitter proteins Science 312 111 114 10.1126/science.1123539 16601193 1:CAS:528:DC%2BD28XjtFalsLs%3D
    • (2006) Science , vol.312 , pp. 111-114
    • Weinreich, D.M.1    Delaney, N.F.2    Depristo, M.A.3    Hartl, D.L.4
  • 34
    • 0023992870 scopus 로고
    • Drosophila melanogaster alcohol dehydrogenase. Biochemical properties of the NAD+-plus-acetone-induced isoenzyme conversion
    • 3134011 1:CAS:528:DyaL1cXhs1equ7c%3D
    • JO Winberg JS McKinley-McKee 1988 Drosophila melanogaster alcohol dehydrogenase. Biochemical properties of the NAD+-plus-acetone-induced isoenzyme conversion Biochem J 251 223 227 3134011 1:CAS:528:DyaL1cXhs1equ7c%3D
    • (1988) Biochem J , vol.251 , pp. 223-227
    • Winberg, J.O.1    McKinley-Mckee, J.S.2
  • 35
    • 0026803724 scopus 로고
    • Kinetic interpretations of active site topologies and residue exchanges in Drosophila alcohol dehydrogenases
    • 10.1016/0020-711X(92)90245-V 1733784 1:CAS:528:DyaK38XlsVSqtA%3D%3D
    • JO Winberg JS McKinley-McKee 1992 Kinetic interpretations of active site topologies and residue exchanges in Drosophila alcohol dehydrogenases Int J Biochem 24 169 181 10.1016/0020-711X(92)90245-V 1733784 1:CAS:528: DyaK38XlsVSqtA%3D%3D
    • (1992) Int J Biochem , vol.24 , pp. 169-181
    • Winberg, J.O.1    McKinley-Mckee, J.S.2
  • 36
    • 0032007556 scopus 로고    scopus 로고
    • Drosophila melanogaster alcohol dehydrogenase: Mechanism of aldehyde oxidation and dismutation
    • 9445383 1:CAS:528:DyaK1cXht1arsrk%3D
    • JO Winberg JS McKinley-McKee 1998 Drosophila melanogaster alcohol dehydrogenase: mechanism of aldehyde oxidation and dismutation Biochem J 329 Pt 3 561 570 9445383 1:CAS:528:DyaK1cXht1arsrk%3D
    • (1998) Biochem J , vol.329 , Issue.PART 3 , pp. 561-570
    • Winberg, J.O.1    McKinley-Mckee, J.S.2
  • 37
    • 0020488217 scopus 로고
    • Alcohol dehydrogenase from the fruitfly Drosophila melanogaster. Substrate specificity of the alleloenzymes AdhS and AdhUF
    • 6807351 1:CAS:528:DyaL38XktF2ksr4%3D
    • JO Winberg DR Thatcher JS McKinley-McKee 1982 Alcohol dehydrogenase from the fruitfly Drosophila melanogaster. Substrate specificity of the alleloenzymes AdhS and AdhUF Biochim Biophys Acta 704 7 16 6807351 1:CAS:528: DyaL38XktF2ksr4%3D
    • (1982) Biochim Biophys Acta , vol.704 , pp. 7-16
    • Winberg, J.O.1    Thatcher, D.R.2    McKinley-Mckee, J.S.3
  • 38
    • 0023049398 scopus 로고
    • Biochemical properties of alcohol dehydrogenase from Drosophila lebanonensis
    • 2943270 1:CAS:528:DyaL28Xit1Wit7c%3D
    • JO Winberg R Hovik JS McKinley-McKee E Juan R Gonzalez-Duarte 1986 Biochemical properties of alcohol dehydrogenase from Drosophila lebanonensis Biochem J 235 481 490 2943270 1:CAS:528:DyaL28Xit1Wit7c%3D
    • (1986) Biochem J , vol.235 , pp. 481-490
    • Winberg, J.O.1    Hovik, R.2    McKinley-Mckee, J.S.3    Juan, E.4    Gonzalez-Duarte, R.5
  • 39
    • 0033607498 scopus 로고    scopus 로고
    • The catalytic triad in Drosophila alcohol dehydrogenase: PH, temperature and molecular modelling studies
    • 10.1006/jmbi.1999.3235 10610783 1:CAS:528:DyaK1MXotFeku7w%3D
    • JO Winberg MK Brendskag I Sylte RI Lindstad JS McKinley-McKee 1999 The catalytic triad in Drosophila alcohol dehydrogenase: pH, temperature and molecular modelling studies J Mol Biol 294 601 616 10.1006/jmbi.1999.3235 10610783 1:CAS:528:DyaK1MXotFeku7w%3D
    • (1999) J Mol Biol , vol.294 , pp. 601-616
    • Winberg, J.O.1    Brendskag, M.K.2    Sylte, I.3    Lindstad, R.I.4    McKinley-Mckee, J.S.5
  • 41
    • 18044378220 scopus 로고    scopus 로고
    • Translational effects of differential codon usage among intragenic domains of new genes in Drosophila
    • 15833448 1:CAS:528:DC%2BD2MXjs1Cmt7c%3D
    • J Zhang M Long L Li 2005 Translational effects of differential codon usage among intragenic domains of new genes in Drosophila Biochim Biophys Acta 1728 3 135 142 15833448 1:CAS:528:DC%2BD2MXjs1Cmt7c%3D
    • (2005) Biochim Biophys Acta , vol.1728 , Issue.3 , pp. 135-142
    • Zhang, J.1    Long, M.2    Li, L.3


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