Tetrameric NAD-dependent alcohol dehydrogenase

Chemico-Biological Interactions

Volumn 143-144, Issue , 2003, Pages 239-245

  Karlsson, Andreas ^a   El Ahmad, Mustapha ^b   Johansson, Kenth ^a   Shafqat, Jawed ^b   Jörnvall, Hans ^b   Eklund, Hans ^a   Ramaswamy, S ^c  

^a SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

^b KAROLINSKA INSTITUTE   (Sweden)

^c UNIVERSITY OF IOWA   (United States)

Author keywords

Quaternary structure; X ray crystallography; Zinc coordination

Indexed keywords

ALCOHOL; ALCOHOL DEHYDROGENASE; BACTERIAL ENZYME; DIMER; ISOENZYME; NICOTINAMIDE ADENINE DINUCLEOTIDE; TETRAMER; ZINC;

CATALYSIS; COMPARATIVE STUDY; CONFERENCE PAPER; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME STRUCTURE; ESCHERICHIA COLI; SURFACE PROPERTY;

ALCOHOL DEHYDROGENASE; AMINO ACID SEQUENCE; BIOPOLYMERS; CATALYSIS; ESCHERICHIA COLI; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NAD; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID; ZINC;

ESCHERICHIA COLI; MAMMALIA;

EID: 0345073681     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(02)00222-3     Document Type: Conference Paper

References (26)

1. Brändén C.-I., Eklund H., Furugren B. Alcohol dehydrogenases. Boyer P. The Enzymes. XI:1975;103-190 Academic Press, New York.
2. Jörnvall H. The primary structure of yeast alcohol dehydrogenase. Eur. J. Biochem. 72:1977;425-442.
3. Nordling E., Jörnvall H., Persson B. Medium-chain dehydrogenases/reductases (MDR): family characterizations including genome comparisons and active site modelling. Eur. J. Biochem. 269:2002;4267-4276.
4. Jörnvall H., Eklund H., Brändén C.-I. Subunit conformation of yeast alcohol dehydrogenase. J. Biol. Chem. 253:1978;8414-8419.
5. Eklund H., Nordström B., Zeppezauer E., Söderlund G., Ohlsson I., Boiwe T., Söderberg B.O., Tapia O., Brändén C.-I., Åkeson Å. Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 Å resolution. J. Mol. Biol. 102:1976;27-59.
6. 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions. Proc. Natl. Acad. Sci. USA. 88:1991;8149-8153.
7. 3 alcohol dehydrogenase. The contribution of ionic interactions to coenzyme binding. J. Biol. Chem. 271:1996;17057-17061.
8. Hurley T.D., Bosron W.F., Stone C.L., Amzel L.M. Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences. J. Mol. Biol. 239:1994;415-429.
9. Eklund H., Brändén C.-I. Alcohol dehydrogenase. Jurnak F., McPherson A. Biological Molecules and Assemblies: Enzymes. 3:1987;73-142 Wiley, New York.
10. Ramaswamy S., El Ahmad M., Danielsson O., Jörnvall H., Eklund H. Crystal structure of cod liver class I alcohol dehydrogenase: substrate pocket and structurally variable segments. Protein Sci. 5:1996;663-671.
11. Yang Z.N., Bosron W.F., Hurley T.D. Structure of human χχ alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase. J. Mol. Biol. 265:1997;330-343.
12. Xie P., Parsons S.H., Speckhard D.C., Bosron W.F., Hurley T.D. X-ray structure of human class IV σσ alcohol dehydrogenase. Structural basis for substrate specificity. J. Biol. Chem. 272:1997;18558-18563.
13. Svensson S., Höög J.O., Schneider G., Sandalova T. Crystal structures of mouse class II alcohol dehydrogenase reveal determinants of substrate specificity and catalytic efficiency. J. Mol. Biol. 302:2000;441-453.
14. Niederhut M.S., Gibbons B.J., Perez-Miller S., Hurley T.D. Three-dimensional structures of the three human class I alcohol dehydrogenases. Protein Sci. 10:2001;697-706.
15. Sanghani P.C., Robinson H., Bosron W.F., Hurley T.D. Human glutathione-dependent formaldehyde dehydrogenase. Structures of apo, binary, and inhibitory ternary complexes. Biochemistry. 41:2002;10778-10786.
16. Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F. NADP-dependent bacterial alcohol dehydrogenases: crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii. J. Mol. Biol. 278:1998;967-981.
17. Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F. Oligomeric integrity - the structural key to thermal stability in bacterial alcohol dehydrogenases. Protein Sci. 8:1999;1241-1249.
18. Li C., Heatwole J., Soelaiman S., Shoham M. Crystal structure of a thermophilic alcohol dehydrogenase substrate complex suggests determinants of substrate specificity and thermostability. Proteins. 37:1999;619-627.
19. Esposito L., Sica F., Raia C.A., Giordano A., Rossi M., Mazzarella L., Zagari A. Crystal structure of the alcohol dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus at 1.85 Å resolution. J. Mol. Biol. 318:2002;463-477.
20. Banfield M.J., Salvucci M.E., Baker E.N., Smith C.A. Crystal structure of the NADP(H)-dependent ketose reductase from Bemisia argentifolii at 2.3 A resolution. J. Mol. Biol. 306:2001;239-250.
21. Johansson K., El-Ahmad M., Kaiser C., Jörnvall H., Eklund H., Höög J., Ramaswamy S. Crystal structure of sorbitol dehydrogenase. Chem. Biol. Interact. 130-132:2001;351-358.
22. Shafqat J., Höög J.O., Hjelmqvist L., Oppermann U.C., Ibanez C., Jörnvall H. An ethanol-inducible MDR ethanol dehydrogenase/acetaldehyde reductase in Escherichia coli: structural and enzymatic relationships to the eukaryotic protein forms. Eur. J. Biochem. 263:1999;305-311.
23. A. Karlsson, M. El-Ahmad, K. Johansson, J. Shafqat, Jörnvall, H. Eklund, S. Ramaswamy, Domain rotation, variable zinc-coordination in tetrameric NAD-dependent alcohol dehydrogenase and their relation to coenzyme binding, (2002) in preparation.
24. Ganzhorn A.J., Plapp B.V. Carboxyl groups near the active site zinc contribute to catalysis in yeast alcohol dehydrogenase. J. Biol. Chem. 263:1988;5446-5454.
25. Ryde U. Molecular dynamics simulations of alcohol dehydrogenase with a four- or five-coordinate catalytic zinc ion. Proteins. 21:1995;40-56.
26. Ryde U. The coordination of the catalytic zinc in alcohol dehydrogenase studied by combined quantum-chemical and molecular mechanics calculations. J. Comput. Aided Mol. Des. 10:1996;153-164.