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3. Liver alcohol dehydrogenase inhibition by fatty acid amides, N-alkylformamides and monoalkylureas. Porter CC; Titus DC; DeFelice MJ Life Sci; 1976 May; 18(9):953-9. PubMed ID: 1271964 [No Abstract] [Full Text] [Related]
4. Site-specific substituted cobalt(II) horse liver alcohol dehydrogenases. Preparation and characterization in solution, crystalline and immobilized state. Maret W; Andersson I; Dietrich H; Schneider-Bernlöhr H; Einarsson R; Zeppezauer M Eur J Biochem; 1979 Aug; 98(2):501-12. PubMed ID: 488110 [TBL] [Abstract][Full Text] [Related]
5. Active site specific cadmium(II)-substituted horse liver alcohol dehydrogenase: crystal structures of the free enzyme, its binary complex with NADH, and the ternary complex with NADH and bound p-bromobenzyl alcohol. Schneider G; Cedergren-Zeppezauer E; Knight S; Eklund H; Zeppezauer M Biochemistry; 1985 Dec; 24(25):7503-10. PubMed ID: 2935190 [TBL] [Abstract][Full Text] [Related]
6. Coordination environment of the active-site metal ion of liver alcohol dehydrogenase. Makinen MW; Yim MB Proc Natl Acad Sci U S A; 1981 Oct; 78(10):6221-5. PubMed ID: 6273859 [TBL] [Abstract][Full Text] [Related]
7. Metal ion substitution at the catalytic site of horse-liver alcohol dehydrogenase: results from solvent magnetic relaxation studies. 1. Copper(II) and cobalt(II) ions. Andersson I; Maret W; Zeppezauer M; Brown RD; Koenig SH Biochemistry; 1981 Jun; 20(12):3424-32. PubMed ID: 7020751 [No Abstract] [Full Text] [Related]
8. Metal ion substitution at the catalytic site of horse-liver alcohol dehydrogenase: results from solvent magnetic relaxation studies. 2. Binding of manganese(II) and competition with zinc(II) and cadmium(II) ions. Andersson I; Maret W; Zeppezauer M; Brown RD; Koenig SH Biochemistry; 1981 Jun; 20(12):3433-8. PubMed ID: 7020752 [TBL] [Abstract][Full Text] [Related]
9. Crystal structures of the active site in specifically metal-depleted and cobalt-substituted horse liver alcohol dehydrogenase derivatives. Schneider G; Eklund H; Cedergren-Zeppezauer E; Zeppezauer M Proc Natl Acad Sci U S A; 1983 Sep; 80(17):5289-93. PubMed ID: 6351056 [TBL] [Abstract][Full Text] [Related]
10. Investigation of intermediates and transition states in the catalytic mechanisms of active site substituted cobalt(II), nickel(II), zinc(II), and cadmium(II) horse liver alcohol dehydrogenase. Dunn MF; Dietrich H; MacGibbon AK; Koerber SC; Zeppezauer M Biochemistry; 1982 Jan; 21(2):354-63. PubMed ID: 7041961 [No Abstract] [Full Text] [Related]
11. The binding of 1,10-phenanthroline to specifically active-site cobalt(II)-substituted horse-liver alcohol dehydrogenase. A probe for the open-enzyme conformation. Sartorius C; Dunn MF; Zeppezauer M Eur J Biochem; 1988 Nov; 177(3):493-9. PubMed ID: 3197713 [TBL] [Abstract][Full Text] [Related]
12. Active-site-specific reconstituted cobalt(II) horse-liver alcohol dehydrogenase. Changes of the spectra of the substrate trans-4-(N,N-dimethylamino)-cinnamaldehyde and of the catalytic cobalt ion upon ternary complex formation with NADH and 1,4,5,6-tetrahydronicotinamide--adenine dinucleotide. Dietrich H; Maret W; Wallén L; Zeppezauer M Eur J Biochem; 1979 Oct; 100(1):267-70. PubMed ID: 226360 [No Abstract] [Full Text] [Related]
13. The role of metal in liver alcohol dehydrogenase catalysis. Spectral and kinetic studies with cobalt-substituted enzyme. Shore JD; Santiago D J Biol Chem; 1975 Mar; 250(6):2008-12. PubMed ID: 234953 [TBL] [Abstract][Full Text] [Related]
15. Neutral metal-bound water is the base catalyst in liver alcohol dehydrogenase. Makinen MW; Maret W; Yim MB Proc Natl Acad Sci U S A; 1983 May; 80(9):2584-8. PubMed ID: 6302696 [TBL] [Abstract][Full Text] [Related]
16. The interaction of catalytic metal ions and ionizing groups in equilibrium studies and in transient intermediates of metal-substituted alcohol dehydrogenases. Maret W; Gerber M; Zeppezauer M; Dunn MF Prog Clin Biol Res; 1985; 174():181-91. PubMed ID: 3885258 [TBL] [Abstract][Full Text] [Related]
17. The catalytic metal atoms of cobalt substituted liver alcohol dehydrogenase. Sytkowski AJ; Vallee BL Biochem Biophys Res Commun; 1975 Dec; 67(4):1488-93. PubMed ID: 1239290 [No Abstract] [Full Text] [Related]
18. Structural evidence for a ligand coordination switch in liver alcohol dehydrogenase. Meijers R; Adolph HW; Dauter Z; Wilson KS; Lamzin VS; Cedergren-Zeppezauer ES Biochemistry; 2007 May; 46(18):5446-54. PubMed ID: 17429946 [TBL] [Abstract][Full Text] [Related]
19. Nuclear magnetic resonance studies of substrate interaction with cobalt substituted alcohol dehydrogenase from liver. Sloan DL; Young JM; Mildvan AS Biochemistry; 1975 May; 14(9):1998-2008. PubMed ID: 164901 [TBL] [Abstract][Full Text] [Related]
20. THE EFFECTS OF COENZYMES AND SUBSTRATES ON THE RATE OF ZINC EXCHANGE IN HORSE LIVER ALCOHOL DEHYDROGENASE. DRUYAN R; VALLEE BL Biochemistry; 1964 Jul; 3():944-9. PubMed ID: 14214085 [No Abstract] [Full Text] [Related] [Next] [New Search]