메뉴 건너뛰기




Volumn 5, Issue 4, 1996, Pages 663-671

Crystal structure of cod liver class I alcohol dehydrogenase: Substrate pocket and structurally variable segments

Author keywords

alcohol dehydrogenase; domain rotation; protein structure; proton relay system; refinement; substrate cleft; X ray crystallography

Indexed keywords

ALCOHOL DEHYDROGENASE; ALCOHOL DEHYDROGENASE 1; UNCLASSIFIED DRUG;

EID: 0029988542     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050410     Document Type: Article
Times cited : (52)

References (37)
  • 2
    • 0001897686 scopus 로고
    • Assessment of phase accuracy by cross validation: The free R value, methods and applications
    • Brunger AT. 1993. Assessment of phase accuracy by cross validation: The free R value, methods and applications. Acta Crystallogr D 49:24-36.
    • (1993) Acta Crystallogr D , vol.49 , pp. 24-36
    • Brunger, A.T.1
  • 3
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brunger AT, Kuriyan J, Karplus M. 1987. Crystallographic R factor refinement by molecular dynamics. Science 235:458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brunger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 4
    • 0028103275 scopus 로고
    • CCP4 suite: Programs for protein crystallography by collaborative computational project number 4
    • CCP4 suite. 1994. CCP4 suite: Programs for protein crystallography by collaborative computational project number 4. Acta Crystallogr D 50: 760-763.
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
  • 5
    • 0020492993 scopus 로고
    • Crystal structure determinations of coenzyme analogue and substrate complexes of liver alcohol dehydrogenase: Binding of 1,4,5,6-tetrahydronicotinamide adenine dinucleotide and trans-4-(N,N-dimethylamino)cinnamaldehyde to the enzyme
    • Cedergren-Zeppezauer E, Samama JP, Eklund H. 1982. Crystal structure determinations of coenzyme analogue and substrate complexes of liver alcohol dehydrogenase: Binding of 1,4,5,6-tetrahydronicotinamide adenine dinucleotide and trans-4-(N,N-dimethylamino)cinnamaldehyde to the enzyme. Biochemistry 21:4895-4908.
    • (1982) Biochemistry , vol.21 , pp. 4895-4908
    • Cedergren-Zeppezauer, E.1    Samama, J.P.2    Eklund, H.3
  • 8
    • 0026780717 scopus 로고
    • The major piscine liver alcohol dehydrogenase has class-mixed properties in relation to mammalian alcohol dehydrogenase of class I and III
    • Danielsson O, Eklund H, Jörnvall H. 1992. The major piscine liver alcohol dehydrogenase has class-mixed properties in relation to mammalian alcohol dehydrogenase of class I and III. Biochemistry 31:3751-3759.
    • (1992) Biochemistry , vol.31 , pp. 3751-3759
    • Danielsson, O.1    Eklund, H.2    Jörnvall, H.3
  • 9
    • 0028104158 scopus 로고
    • Alcohol dehydrogenase class III contrasted to class I. Characterization of the cyclostome enzyme, the existence of multiple forms as for the human enzyme, and distant cross-species hybridization
    • Danielsson O, Shafqat J, Estomus M, Jornvall H. 1994b. Alcohol dehydrogenase class III contrasted to class I. Characterization of the cyclostome enzyme, the existence of multiple forms as for the human enzyme, and distant cross-species hybridization. Eur J Biochem 225:1081-1088.
    • (1994) Eur J Biochem , vol.225 , pp. 1081-1088
    • Danielsson, O.1    Shafqat, J.2    Estomus, M.3    Jornvall, H.4
  • 10
    • 0026092212 scopus 로고
    • General base catalysis in a glutamine for histidine mutant at position 51 of human liver alcohol dehydrogenase
    • Ehrig T, Hurley TD, Edenberg HJ, Bosron WF. 1991. General base catalysis in a glutamine for histidine mutant at position 51 of human liver alcohol dehydrogenase. Biochemistry 30:1062-1068
    • (1991) Biochemistry , vol.30 , pp. 1062-1068
    • Ehrig, T.1    Hurley, T.D.2    Edenberg, H.J.3    Bosron, W.F.4
  • 11
  • 12
    • 15844426238 scopus 로고    scopus 로고
    • New York: Wiley and Sons
    • Eklund H, Brändén CI. 1987. Alcohol dehydrogenase. Biological Molecules and Assemblies 3:73-142. In: Jurnak F, McPherson A, eds. Active sites of enzymes. New York: Wiley and Sons.
    • Active Sites of Enzymes
    • Jurnak, F.1    McPherson, A.2
  • 13
    • 0022332394 scopus 로고
    • Molecular aspects of functional differences between alcohol and sorbitol dehydrogenases
    • Eklund H, Horjales E, Jornvall H, Brändén CI, Jeffery J. 1985. Molecular aspects of functional differences between alcohol and sorbitol dehydrogenases. Biochemistry 24:8005-8012.
    • (1985) Biochemistry , vol.24 , pp. 8005-8012
    • Eklund, H.1    Horjales, E.2    Jornvall, H.3    Brändén, C.I.4    Jeffery, J.5
  • 16
    • 0020479867 scopus 로고
    • Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase
    • Eklund H, Plapp BV, Samama JP, Brandén CI. 1982. Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase J Biol Chem 257:14349-14358.
    • (1982) J Biol Chem , vol.257 , pp. 14349-14358
    • Eklund, H.1    Plapp, B.V.2    Samama, J.P.3    Brandén, C.I.4
  • 17
    • 0021701199 scopus 로고
    • Crystallographic investigations of nicotinamide adenine dinucleotide binding to horse liver alcohol dehydrogenase
    • Eklund H, Samama JP, Jones TA. 1984. Crystallographic investigations of nicotinamide adenine dinucleotide binding to horse liver alcohol dehydrogenase. Biochemistry 23:5982-5996.
    • (1984) Biochemistry , vol.23 , pp. 5982-5996
    • Eklund, H.1    Samama, J.P.2    Jones, T.A.3
  • 18
    • 0019880506 scopus 로고
    • Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 Å resolution
    • Eklund H, Samama JP, Wallén L, Brandén CI, Åkeson Å, Jones TA. 1981. Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 Å resolution. J Mol Biol 146:561-587.
    • (1981) J Mol Biol , vol.146 , pp. 561-587
    • Eklund, H.1    Samama, J.P.2    Wallén, L.3    Brandén, C.I.4    Åkeson, Å.5    Jones, T.A.6
  • 20
    • 0026504082 scopus 로고
    • A single-residue exchange gives human recombinant ββ alcohol dehydrogenase γγ isoenzyme properties
    • Hoög JO, Eklund H, Jornvall H. 1992. A single-residue exchange gives human recombinant ββ alcohol dehydrogenase γγ isoenzyme properties. Eur J Biochem 205:519-526.
    • (1992) Eur J Biochem , vol.205 , pp. 519-526
    • Hoög, J.O.1    Eklund, H.2    Jornvall, H.3
  • 21
    • 0025873327 scopus 로고
    • Structure of human β1β1 alcohol dehydrogenase catalytic effects of non-active site substitutions
    • Hurley TD, Bosron WF, Hamilton JA, Amzel LM. 1991. Structure of human β1β1 alcohol dehydrogenase catalytic effects of non-active site substitutions. Proc Natl Acad Sci USA 88:8149-8153.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8149-8153
    • Hurley, T.D.1    Bosron, W.F.2    Hamilton, J.A.3    Amzel, L.M.4
  • 22
    • 0028773470 scopus 로고
    • The crystal structure of glucose dehydrogenase from thermoplasma acidophilum
    • John J, Crennel SJ, Hough DW, Danson MJ, Taylor GL. 1994. The crystal structure of glucose dehydrogenase from thermoplasma acidophilum. Structure 2:385-393.
    • (1994) Structure , vol.2 , pp. 385-393
    • John, J.1    Crennel, S.J.2    Hough, D.W.3    Danson, M.J.4    Taylor, G.L.5
  • 23
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr 47:110-119.
    • (1991) Acta Crystallogr , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 24
    • 0023244840 scopus 로고
    • Mammalian alcohol dehydrogenases of separate classes: Intermediates between different enzymes and intraclass isozymes
    • Jörnvall H, Höög JO, von Bahr-Lindstrom H, Vallee BL. 1987. Mammalian alcohol dehydrogenases of separate classes: Intermediates between different enzymes and intraclass isozymes. Proc Natl Acad Sci USA 84:2580-2584.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 2580-2584
    • Jörnvall, H.1    Höög, J.O.2    Von Bahr-Lindstrom, H.3    Vallee, B.L.4
  • 26
    • 0027489769 scopus 로고
    • Origin of the human alcohol dehydrogenase system. Implications from the structure and properties of the octopus protein
    • Kaiser R, Fernández MR, Parés X, Jornvall H. 1993. Origin of the human alcohol dehydrogenase system. Implications from the structure and properties of the octopus protein. Proc Natl Acad Sci USA: 11222-11226.
    • (1993) Proc Natl Acad Sci USA , pp. 11222-11226
    • Kaiser, R.1    Fernández, M.R.2    Parés, X.3    Jornvall, H.4
  • 27
    • 0000127585 scopus 로고
    • Automated refinement of proteins models
    • Lamzin VS, Wilson KS. 1993. Automated refinement of proteins models. Acta Crystallogr D 49:129-147.
    • (1993) Acta Crystallogr D , vol.49 , pp. 129-147
    • Lamzin, V.S.1    Wilson, K.S.2
  • 28
    • 0000243829 scopus 로고
    • PRO-CHECK: A program to check the stereochemical quality of protein structures
    • Laskowski RA, McArthur MW, Moss DS, Thornton JM. 1993. PRO-CHECK: A program to check the stereochemical quality of protein structures J Appl Crystallogr 26:282-291.
    • (1993) J Appl Crystallogr , vol.26 , pp. 282-291
    • Laskowski, R.A.1    McArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 29
    • 0002452464 scopus 로고
    • Data collection and processing
    • Sawyer L, Issacs N, Bailey S, eds. Warrington, UK: SERC Daresbury Laboratory
    • Otwinowski Z. 1993. Data collection and processing. In: Sawyer L, Issacs N, Bailey S, eds. Proceedings of the CCP4 study weekend. Warrington, UK: SERC Daresbury Laboratory. pp 56-62.
    • (1993) Proceedings of the CCP4 Study Weekend , pp. 56-62
    • Otwinowski, Z.1
  • 30
    • 0028930478 scopus 로고
    • Site-directed mutagenesis: A tool for studying enzyme catalysis
    • Plapp BV. 1995. Site-directed mutagenesis: A tool for studying enzyme catalysis. Methods Enzymol 249:91-119.
    • (1995) Methods Enzymol , vol.249 , pp. 91-119
    • Plapp, B.V.1
  • 32
    • 0028151542 scopus 로고
    • A super-family of medium-chain dehydrogenases/reductases (MDR). Sub-lines including z-crystallin, alcohol and polyol dehydrogenases, quinone oxidoreductases, enoyl reductases, VAT-1 and other proteins
    • Persson B, Zigler JS Jr, Jörnvall H. 1994. A super-family of medium-chain dehydrogenases/reductases (MDR). Sub-lines including z-crystallin, alcohol and polyol dehydrogenases, quinone oxidoreductases, enoyl reductases, VAT-1 and other proteins. Eur J Biochem 226:15-22.
    • (1994) Eur J Biochem , vol.226 , pp. 15-22
    • Persson, B.1    Zigler Jr., J.S.2    Jörnvall, H.3
  • 33
    • 0028300618 scopus 로고
    • Structures of horse liver alcohol dehydrogenase complexed with NAD+ and substituted benzyl alcohols determined in two crystal forms
    • Ramaswamy S, Eklund H, Plapp BV. 1994a. Structures of horse liver alcohol dehydrogenase complexed with NAD+ and substituted benzyl alcohols determined in two crystal forms. Biochemistry 33:5230-5237.
    • (1994) Biochemistry , vol.33 , pp. 5230-5237
    • Ramaswamy, S.1    Eklund, H.2    Plapp, B.V.3
  • 34
    • 0027991575 scopus 로고
    • Crystallisation and crystallographic investigations of cod alcohol dehydrogenase class I and class III enzymes
    • Ramaswamy S, El-Ahmad M, Danielsson O, Jornvall H, Eklund H. 1994b. Crystallisation and crystallographic investigations of cod alcohol dehydrogenase class I and class III enzymes. FEBS Lett 350:122-124.
    • (1994) FEBS Lett , vol.350 , pp. 122-124
    • Ramaswamy, S.1    El-Ahmad, M.2    Danielsson, O.3    Jornvall, H.4    Eklund, H.5
  • 35
    • 0017752247 scopus 로고
    • The crystal structure of complexes between horse liver alcohol dehydrogenase and the coenzyme analogues 3-iodopyridine-adenine dinucleotide and pyridine-adenine dinucleotide
    • Samama JP, Zeppezauer E, Biellmann JF, Brandén CI. 1977. The crystal structure of complexes between horse liver alcohol dehydrogenase and the coenzyme analogues 3-iodopyridine-adenine dinucleotide and pyridine-adenine dinucleotide. Eur J Biochem 81:403-409.
    • (1977) Eur J Biochem , vol.81 , pp. 403-409
    • Samama, J.P.1    Zeppezauer, E.2    Biellmann, J.F.3    Brandén, C.I.4
  • 36
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • Sippl MJ. 1993. Recognition of errors in three-dimensional structures of proteins. Proteins Struct Fund Genet 17:355-362.
    • (1993) Proteins Struct Fund Genet , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 37
    • 0028977970 scopus 로고
    • Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH
    • Thorn JM, Barton JD, Dixon NE, Ollis DL, Edwards KJ. 1995. Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH. J Mol Biol 249:785-799.
    • (1995) J Mol Biol , vol.249 , pp. 785-799
    • Thorn, J.M.1    Barton, J.D.2    Dixon, N.E.3    Ollis, D.L.4    Edwards, K.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.