Structure of mitochondrial aldehyde dehydrogenase: The genetic component of ethanol aversion

Structure

Volumn 5, Issue 5, 1997, Pages 701-711

  Steinmetz, Curtis G ^a   Xie, Peiguang ^a   Weiner, Henry ^b   Hurley, Thomas D ^a  

^a INDIANA UNIVERSITY   (United States)

^b PURDUE UNIVERSITY   (United States)

Author keywords

aldehyde dehydrogenase; dinucleotide fold; multiple isomorphous replacement; phenotypic dominance

Indexed keywords

EID: 0031570328     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00224-4     Document Type: Article

References (54)

1. Hsu, L.C., Chang, W.-C., Lin, S.W. & Yoshida, A. (1995). Cloning and characterization of genes encoding four additional human aldehyde dehydrogenase isoenzymes. In Enzymology and Molecular Biology of Carbonyl Metabolism. (Weiner, H., Holmes, R.S. & Wermuth, B., eds), pp. 159-168, Plenum Press, NY, USA.
2. Lin, S.W., Chen, J.C., Hsu, L.C., Hsieh, C.L. & Yoshida, A. (1996). Human gamma-aminobutyraldehyde dehydrogenase (ALDH9): cDNA sequence, genomic organization, polymorphism, chromosomal localization, and tissue expression. Genomics 34, 376-380.
3. Ehrig, T., Bosron, W.F. & Li, T.-K. (1990). Alcohol and aldehyde dehydrogenase. Alcohol Alcohol. 25, 105-116.
4. Hart, B.W. & Faiman, M.D. (1992). In vitro and in vivo inhibition of rat liver aldehyde dehydrogenase S-methyl N,N-diethylthiolcarbamate sufloxide, a new metabolite of disulfiram. Biochem. Pharmacol. 43, 403-406.
5. Rose, J.P., Hempel, J., Kuo, I., Lindahl, R. & Wang, B.-C. (1991). Preliminary crystallographic analysis of class 3 rat liver aldehyde dehydrogenase. Proteins 8, 305-308.
6. Hempel, J., Nicholas, H. & Lindahl, R. (1993). Aldehyde dehydrogenases: a widespread structural and functional diversity within a shared framework. Protein Sci. 2, 1890-1900.
7. Liu, Z.-J., et al., & Wang, B.-C. (1997). The first structure of an aldehyde dehydrogenase reveals novel interactions between NAD and the Rossmann fold. Nat. Struct. Biol. 4, 317-326.
8. Hempel, J. & Pietruszko, R. (1981). Selective chemical modification of human liver aldehyde dehydrogenases E1 and E2 with iodoacetamide. J. Biol. Chem. 256, 10889-10896
9. Hempel, J., Pietruszko, R., Fietek, P. & Jörnvall, H. (1982) Identification of a segment containing a reactive cysteine residue in human liver cytoplasmic aldehyde dehydrogenase (isoenzyme E1). Biochemistry 21, 6834-6838.
10. Abriola, D.P., Fields, R., Stein, S., Mackerell, A.D. Jr. & Pietruszko, R. (1987). Active site of aldehyde dehydrogenase. Biochemistry 26, 5679-5684.
11. Farrés, J., Wang, T.T.Y., Cunningham, S.J. & Weiner, H. (1995). Investigation of the active site cysteine residue of rat liver mitochondrial aldehyde dehydrogenase by site-directed mutagenesis. Biochemistry 34, 2592-2598.
12. Wang, X.-P. & Weiner, H. (1995). Involvement of glutamate 268 in the active site of human liver mitochondrial aldehyde dehydrogenase as probed by site-directed mutagenesis. Biochemistry 34, 237-243.
13. Goedde, H.W., Harada, S. & Agarwal, D.P. (1979). Racial differences in alcohol sensitivity: a new hypothesis. Human Genetics 51, 331-334.
14. Harada, S., Agarwal, D.P., Goedde, H.W., Tagaki, S. & Ishikawa, B. (1982). Possible protective role against alcoholism for aldehyde dehydrogenase isoenzyme deficiency in Japan. Lancet 2, 827.
15. Teng, Y.-S. (1981). Human liver aldehyde dehydrogenase in Chinese and Asiatic Indians: gene deletion and its possible implications in alcohol metabolism. Biochem. Genet. 19, 107-114.
16. Impraim, C., Wang, B. & Yoshida, A. (1982). Structural mutations in a major human aldehyde dehydrogenase gene results in loss of enzyme activity. Am. J. Hum. Genet. 34, 837-841.
17. Mizoi, Y., Ijiri, I., Tatsuno, Y., Kijima, T., Fujiwara, S. & Adachi, J. (1979). Relationship between facial flushing and blood acetaldehyde levels after alcohol intake. Pharmcol. Biochem. Behav. 10, 303-311.
18. Harada, S., Agarwal, D.P. & Goedde, H.W. (1981). Aldehyde dehydrogenase deficiency as cause of facial flushing reaction to alcohol in Japanese. Lancet 2, 982.
19. m aldehyde dehydrogenase phenotype and drinking behavior in Japanese. J. Stud. Alcohol. 53, 170-175.
20. Higuchi, S., Matsushita, S., Imazeki, H., Kinoshita, T., Takagi, S. & Kono, H. (1994). Aldehyde dehydrogenase genotypes in Japanese alcoholics. Lancet 343, 741-742.
21. Svanas, G.W. & Weiner, H. (1985). Aldehyde dehydrogenase activity as the rate-limiting factor for acetaldehyde metabolism in rat liver. Arch. Biochem. Biophys. 236, 36-46
22. Cao, Q.-N., Tu, G.-C. & Weiner, H. (1988). Mitochondria as the primary site for acetaldehyde metabolism. Alcohol. Clin. Exp. Res. 12, 720-723.
23. Ikawa, M., Impraim, C., Wang, G. & Yoshida, A. (1983). Isolation and characterization of aldehyde dehydrogenase isoenzymes from usual and atypical human livers. J. Biol. Chem. 258, 6282-6827.
24. Yoshida, A., Huang, I.-Y. & Ikawa, M. (1984). Molecular abnormality in an inactive aldehyde dehydrogenase variant commonly found in Orientals. Proc. Natl. Acad. Sci. USA 81, 258-261.
25. Farrés, J., Wang, X.-P., Takahashi, K., Cunningham, S.J., Wang, T.T.Y. & Weiner, H. (1994). Effect of changing glutamate to lysine in rat and human liver mitochondrial aldehyde dehydrogenase: a model to study human (Oriental type) class 2 aldehyde dehydrogenase. J. Biol. Chem. 269, 13854-13860.
26. Crabb, D.W., Edenberg, H.J., Bosron, W.F. & Li, T.-K. (1989). Genotypes for aldehyde dehydrogenase deficiency and alcohol sensitivity. The inactive ALDH2*2 allele is dominant. J. Clin. Invest. 83, 314-316.
27. Wang, X.-P., Sheikh, S., Saigal, D., Robinson, L. & Weiner, H. (1996). Heterotetramers of human liver mitochondrial (class 2) aldehyde dehydrogenase expressed in Escherichia coli. J. Biol. Chem. 271, 31172-31178.
28. Xiao, Q.X., Weiner, H., Johnston, T. & Crabb, D.W. (1995). The aldehyde dehydrogenase ALDH2*2 allele exhibits dominance over ALDH2*1 in transduced HeLa cells. J. Clin. Invest. 96, 2180-2186
29. Xiao, Q.X., Weiner, H. & Crabb, D.W. (1996). The mutation in the mitochondrial aldehyde dehydrogenase (ALDH2) gene responsible for alcohol flushing increases turnover of the enzyme tetramers in a dominant fashion. J. Clin. Invest. 98, 2027-2032.
30. Takahashi, K. & Weiner, H. (1980). Magnesium simulation of catalytic activity of horse liver aldehyde dehydrogenase. J. Biol. Chem. 255, 8208-8209.
31. Takahashi, K., Weiner, H. & Hu, J.H.J. (1980). Increase in the stoichiometry of the functioning active sites of horse liver aldehyde dehydrogenase in the presence of magnesium ions. Arch. Biochem. Biophys. 205, 571-578
32. Takahashi, K., Weiner, H. & Filmer, D.L. (1981). Effects of pH on horse liver aldehyde dehydrogenase: alterations in metal ion activation, number of functioning active sites, and hydrolysis of the acyl intermediate. Biochemistry 21, 6225-6230
33. Weiner, H. & Takahashi, K. (1983). Effects of magnesium and calcium on mitochondrial and cytosolic liver aldehyde dehydrogenase. Pharmac. Biochem. Behav. 18, 109-112.
34. Guan, K.-L., Pak, Y.K., Tu, G.-C., Cao, Q.-N. & Weiner, H. (1988). Purification and characterization of beef and pig liver aldehyde dehydrogenases. Alcohol. Clin. Exp. Res. 12, 713-719.
35. Rossmann, M.G., Moras, D. & Olsen, K.W. (1974). Chemical and biological evolution of a nucleotide-binding protein. Nature 250, 194-199.
36. Sheikh, S., Ni, L., Hurley, T.D. & Weiner, H. (1997). The potential roles of the conserved amino acids in human liver aldehyde dehydrogenase. J. Biol. Chem., in press.
37. Ni, L., Shiekh, S. & Weiner H. (1997) Involvement of Glutamate 399 and Lysine 192 in the mechanism of human liver aldehyde dehydrogenase. J. Biol. Chem., in press.
38. Corkey, B.E., Duszynski, J., Rich, T.L., Matschinsky, B. & Williamson, J.R. (1986) Regulation of free and bound magnesium in rat hepatocytes and isolated mitochondria. J. Biol. Chem. 261, 2567-2574.
39. Eklund, H., Samama, J.-P., Wallén, L., Bränden, C.-I., Åkeson, Å & Jones, T.A. (1981). Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 Å resolution. J. Mol. Biol. 146, 561-587.
40. Moras, D., Olsen, K.W., Sabesan, M.N., Buehner, M., Ford, G.C. & Rossmann, M.G. (1975). Studies of asymmetry in the three-dimensional structure of lobster D-glyceraldehyde-3-phosphate dehydrogenase. J. Biol. Chem. 250, 9137-9162.
41. Rout, U. & Weiner, H. (1994). Involvement of S74 in the enzyme-coenzyme interaction of rat liver mitochondrial aldehyde dehydrogenase. Biochemistry 33, 8955-8961.
42. Jones, K.H., Lindahl, R., Baker, D.C. & Timkovich, R. (1987). Hydride transfer stereospecificity of rat liver aldehyde dehydrogenase. J. Biol. Chem. 262, 10911-10913.
43. Farrés, J., Guan, K.-L. & Weiner, H. (1989). Primary structure of rat and bovine liver mitochondrial aldehyde dehydrogenases deduced from cDNA sequences. Eur. J. Biochem. 180, 67-74.
44. Hurley, T.D. & Weiner, H. (1992). Crystallization and preliminary X-ray investigation of bovine liver mitochondrial aldehyde dehydrogenase J. Mol. Biol. 227, 1255-1257.
45. McRee, D.E. (1992). A visual protein crystallographic software system for X11/XView. J. Mol. Graphics 10, 44-46.
46. Terwilliger, T.C., Kim, S.-H. & D. Eisenberg. (1987). Generalized method of determining heavy-atom positions using the difference Patterson function. Acta Cryst. A 43, 1-5.
47. Furey, W. & Swaminathan, S. (1990). PHASES: a program package for the processing and analysis of diffraction data from macromolecules. Am. Cryst. Assoc. Meeting Suppl. 18, 73.
48. Jones, T.A., Cowan, S., Zou, J.-Y. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron-density maps and location of errors in these models. Acta Cryst. A 47, 110-119.
49. Brünger, A.T., Kuriyan, J. & Karplus, M. (1987). Crystallographic R factor refinement by molecular dynamics. Science 235, 458-460.
50. Brünger, A.T. (1992). X-PLOR, Version 3. 1: a System for X-ray Crystallography and NMR. Yale University Press, New Haven, CT.
51. Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
52. Kraulis, P.J. (1991). MOLSCRIPT: a program to program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
53. Bacon, D.J. & Anderson, W.F. (1988). A fast algorithm for rendering space-filling molecule pictures. J. Mol. Graphics 6, 219-220.
54. Merritt, E.A. & Murphy, M.E.P. (1994). Raster3D version 2.0: a program for photorealistic molecular graphics. Acta Cryst. D 50, 869-873.