Differential inactivation of alcohol dehydrogenase isoenzymes in Zymomonas mobilis by oxygen

Journal of Bacteriology

Volumn 179, Issue 4, 1997, Pages 1102-1104

  Tamarit, Jordi ^a   Cabiscol, Elisa ^a   Aguilar, Juan ^b   Ros, Joaquim ^a  

^a Universitat de Lleida Facultat de Medicina Sabadell   (Spain)

^b UNIVERSITY OF BARCELONA   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL DEHYDROGENASE;

ARTICLE; CONFORMATIONAL TRANSITION; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME DEGRADATION; ENZYME INACTIVATION; ENZYME SUBSTRATE COMPLEX; METAL BINDING; NONHUMAN; OXIDATION; PRIORITY JOURNAL; ZYMOMONAS MOBILIS;

ZYMOMONAS MOBILIS;

EID: 0031046388     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.4.1102-1104.1997     Document Type: Article

References (19)

1. Becker, A. B., and R. A. Roth. 1993. Identification of glutamate-169 as the third zinc-binding residue in proteinase III, a member of the family of insulin-degrading enzymes. Biochem. J. 292:137-142.
2. Bode, W., F. X. Gomis Ruth, and W. Stockler. 1993. Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins.' FEBS Lett. 331:134-140.
3. Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
4. Bray, T. M., and W. J. Bettger. 1990. The physiological role of zinc as an antioxidant. Free Radical Biol. Med. 8:281-291.
5. 2+ dehydrogenases. Consensus target sequence between propanediol oxidoreductase of Escherichia coli and alcohol dehydrogenase II of Zymomonas mobilis. J. Biol. Chem. 269:6592-6597.
6. Cabiscol, E., J. Badia, L. Baldoma, E. Hidalgo, J. Aguilar, and J. Ros. 1992. Inactivation of propanediol oxidoreductase of Escherichia coli by metal-catalyzed oxidation. Biochim. Biophys. Acta 1118:155-160.
7. Conway, T., and L. O. Ingram. 1989. Similarity of Escherichia coli propanediol oxidoreductase (fucO product) and an unusual alcohol dehydrogenase from Zymomonas mobilis and Saccharomyces cerevisiae. J. Bacteriol. 171:3754-3759.
8. Fersht, A. 1985. Enzyme structure and mechanism. Freeman and Co., New York, N.Y.
9. Jornvall, H., B. Persson, and J. Jeffrey. 1987. Characteristics of alcohol/ polyol dehydrogenases: the zinc-containing long-chain alcohol dehydrogenases. Eur. J. Biochem. 167:195-201.
10. Keshav, K. F., L. P. Yomano, H. An, and L. O. Ingram. 1990. Cloning of the Zymomonas mobilis structural gene encoding alcohol dehydrogenase I (adhA): sequence comparison and expression in Escherichia coli. J. Bacteriol. 172:2491-2497.
11. Kinoshita, S., T. Kakizono, K. Kadota, K. Das, and H. Taguchi. 1985. Purification of two alcohol dehydrogenases from Zymomonas mobilis and their properties. Appl. Microbiol. Biotechnol. 22:249-254.
12. Levine, R. L., J. A. Williams, E. R, Stadtman, and E. Schacter. 1994. Carbonyl assays for determination of oxidatively modified proteins. Methods Enzymol. 233:346-357.
13. Mackenzie, K. F., C. K. Eddy, and L. O. Ingram. 1989. Modulation of alcohol dehydrogenase isoenzyme levels in Zymomonas mobilis by iron and zinc. J. Bacteriol. 171:1063-1067.
14. Neale, A. D., R. K. Scopes, R. E. H. Wettenhall, and N. J. Hoogenraad. 1985. The two alcohol dehydrogenases of Zymomonas mobilis. Eur. J. Biochem. 154:119-124.
15. Reid, M. F., and C. A. Fewson. 1994. Molecular characterization of microbial alcohol dehydrogenases. Crit. Rev. Microbiol. 20:13-56.
16. Stadtman, E. R. 1993. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu. Rev. Biochem. 62:797-821.
17. Suzuki, H., K. Kishimoto, T. Yoshimoto, S. Yamamoto, F. Kanai, Y. Ebina, A. Miyatake, and T. Tanabe. 1994. Site-directed mutagenesis studies on the iron-binding domain and the determinant for the substrate oxygenation site of porcine leukocyte arachidonate 12-lipoxygenase. Biochim. Biophys. Acta 1210:308-316.
18. Tse, P., R. K. Scopes, A. G. Wedd, E. Bakshi, and K. S. Murray. 1988. An iron-activated alcohol dehydrogenase: metal dissociation constants and magnetic and spectroscopic properties. J. Am. Chem. Soc. 110:1295-1297.
19. Wilkins, G. M., and D. S. Leake. 1994. The oxidation of low density lipoprotein by cells or iron is inhibited by zinc. FEBS Lett. 341:259-262.