Abstract
The superreactive cysteine was first identified in human cytoplasmic aldehyde dehydrogenase El isozyme, before its primary structure was known, as a part of 35 residue tryptic peptide (Hempel, 1981; Hempel and Pietruszko, 1981; Hempel et al., 1982) by employing iodoacetamide. When the primary structures of the El and E2 isozymes were established (Hempel et al., 1984, 1985; Hsu et al., 1985), this cysteine was found to occupy position 302 in a 500 amino acid residue polypeptide chain. Iodoacetamide fulfilled all criteria for an aldehyde-competitive, active-site-directed reagent with the exception of total inactivation of the mitochondrial E2 isozyme. Since that time, other investigators have also attempted to identify active site residues. Coenzyme-based affinity reagents (von Bahr-Lindstrom et al., 1985) identified cysteines 369 and 302, Nethylmaleimide identified cysteine 49 and 162 (Tu and Weiner, 1988 a,b) and dimethylaminocinnamaldehyde identified serine 74 (Loomes et al., 1990). Our laboratory developed a substrate-based affinity reagent, bromo-acetophenone (MacKerell et al., 1986), which identified glutamate 268 (Abriola et al., 1987).
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References
Abriola, D.P., Fields, R., Stein, S., MacKerell, A.D., Jr. and Pietruszko, R., 1987, Active site of human aldehyde dehydrogenase,Biochemistry, 26:5679.
Abriola, D.P., MacKerell, A.D., Jr. and Pietruszko, R., 1990, Correlation of loss of activity of human aldehyde dehydrogenase with reaction of bromoacetophenone with glutamic acid-268 and cysteine-302 residues. Partial-sites reactivity of aldehyde dehydrogenase, Biochem. J., 266:179.
von Bahr-Lindstrom, Hempel, J. and Jornvall, H., 1984, The cytoplasmic isoenzyme of horse liver aldehyde dehydrogenase. Relationship to the corresponding human isoenzyme, Eur. J. Biochem., 141:37.
von Bahr-Lindstrom, Jeck, R., Woenckhaus, C., Sohn, S., Hempel, J. and Jornvall, H., 1985, Characterization of coenzyme binding site of liver aldehyde dehydrogenase: Differential reactivity of coenzyme analogues, Biochemistry, 24:5847.
Blatter, E.E., Tasayco, M.L., Prestwich, G. and Pietruszko, R., 1990, Chemical modification of aldehyde dehydrogenase by a vinyl ketone analog of an insect pheromone, Biochem. J., in press.
Carey, F.A. and Sundberg, R.J., 1984, Advanced Organic Chemistry. Second Edition. Part A: Structure and Mechanisms, Plenum Press, New York and London, p. 207.
Ding, Y.-S. and Prestwich, G.D., 1988, Chemical studies of proteins that degrade pheromones: cyclopropanated, fluorinated, and electrophilic analogs of unsaturated aldehyde pheromones, J. Chem. Ecol., 14:2033.
Dunn, T.J., Koleske, A.J., Lindahl, R. and Pitot, H.C., 1989,Phenobarbital-inducible aldehyde dehydrogenase in the rat. cDNA sequence and regulation of the mRNA by phenobarbital in responsive rats, J. Biol. Chem., 264:13057.
Durst, D., Milano, M., Kikta, E.J., Jr., Connelly, S.A. and Gruska, E., 1975, Phenacyl esters of fatty acids via crown ether catalysts for enhanced ultraviolet detection in liquid chromatography, Analyt. Chem., 47:1797.
Farres, J., Guan, K.-L. and Weiner, H., 1989, Primary structure of rat and bovine liver mitochondrial aldehyde dehydrogenases deduced from cDNA sequences, Eur. J. Biochem., 180:67.
Fukaya, M., Tayama, K., Tamaki, T., Tagami, H., Okumura, H., Kawamura, Y.. and Beppu, T., 1989, Cloning of the membrane-bound aldehyde dehydrogenase gene of Acetobacter polyoxogenesand improvement of acetic acid production by use of the cloned gene, Appl, Environ. Microbiol., 55:171.
Hempel, J.D., 1981, Chemical modification of human liver aldehyde dehydrogenase isoenzymes El and E2. Doctoral Dissertation, Rutgers University. Dissertation Abstracts International 42:3664B, University Microfilms No. DA80204216.
Hempel, J.D. and Pietruszko, R., 1981, Selective chemical modification of human liver aldehyde dehydrogenases El and E2 by iodoacetamide, J. Biol. Chem., 256:10889.
Hempel, J.D., Pietruszko, R., Fietzek, P. andJornvall, H., 1982, Identification of a segment containing a reactive, cysteine residue in human liver cytoplasmic aldehyde dehydrogenase (isoenzyme El)., Biochemistry, 21:6834.
Hempel, J., von Bahr-Lindstrom, H. and Jornvall, H., 1984, Aldehyde dehydrogenase from human liver. Primary structure of the cytoplasmic isoenzyme, Eur. J. Biochem., 141:21.
Hempel, J., Kaiser, R. and Jornvall, J., 1985, Mitochondrial aldehyde dehydrogenase from human liver. Primary structure, differences in relation to the cytosolic enzyme, and functional correlations, Eur. J. Biochem., 153:13.
Hsu, L.C., Tani, K., Fujiyoshi, T., Kurachi, K. and Yoshida, A., 1985, Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2, Proc. Natl. Acad. Sci., USA, 82:3771.
Johansson, J., von Bahr-Lindstrom, Jeck, R., Woenckhaus, C. and Jornvall, H., 1988, Mitochondrial aldehyde dehydrogenase from horse liver. Correlations of the same species variants for both the cytosolic and the mitochondrial forms of an enzyme, Eur. J. Biochem., 172:527.
Jones, D.E., Jr., Brennan, M.D., Hempel, J. and Lindahl, R., 1988, Cloning and complete nucleotide sequence of a full-length cDNA encoding a catalytically functional tumor-associated aldehyde dehydrogenase, Proc. Natl. Acad. Sci. USA, 85:1782.
Kok, M., Oldenhuis, R., van der Linden, M.P.G., Meulenberg, C.H.C., Kingma, J. and Witholt, B., 1989, The Pseudonomas olevoransalkBAC operon encodes two structurally related rubredoxins and an aldehyde dehydrogenase, J. Biol. Chem., 264:5442.
Krzywicki, K.A. and Brandriss, M.C., 1984, Primary structure of the nuclear PUT2 gene involved in the mitochondrial pathway for proline utilization in Saccharomyces cerevisiae, Mol. Cell. Biol., 1984, 4:2837.
Loomes, K.M., Midwinter, G.G.,Blackwell, L.F. and Buckley, P.D., 1990, Evidence for reactivity of serine-74 with trans-4-(N,N-dimethyl- amino)cinnamaldehyde during oxidation by the cytoplasmic aldehyde dehydrogenase from sheep liver, Biochemistry, 29:2070.
MacKerell, A.D., Jr., MacWright, R.S. and Pietruszko, R., 1986, Bromoacetophenone as an affinity reagent for human liver aldehyde dehydrogenase, Biochemistry 25:5182.
Pedersen, C.J. and Frensdorff, K.H., 1972, Macrocyclic polyethers and their complexes, Angew. Chem., Int. Ed. Engl. 11:16.
Pickett, M., Gwynne, D.I., Buxton, F.P., Elliott, R., Davies, R.W., Lockington, R.A., Scazzocchio, C. and Sealy-Lewis, H.M., 1987, Cloning and characterization of the aldA gene of Aspergillus idulans, Gene, 51:217.
Pietruszko, R. and Yonetani, T., 1980, Aldehyde dehydrogenase from liver, In: Methods in Enzymology, Collowick and Kaplan (Eds.), 71:772.
Prestwich, G.D., Graham, S. McG., Handley, M., Latli, B., Streinz, L. and Tasayco J., M.L., 1988, Enzymatic processing of pheromones and pheromone analogs, Experientia, 45:267.
Shaw, E., 1970, Chemical modification by active-site-directed reagents. In: The Enzymes (Student Edition), Vol. 1, Structure and Control, Academic Press, p. 91.
Tasayco J., M.L. and Prestwich, G.D., 1990a, A specific affinity reagent to distinguish aldehyde dehydrogenases and oxidases, J. Biochem. Chem., 265:3094.
Tasayco J., M.L. and Prestwich, G.D., 1990b, Aldehyde-oxidizing enzymes in a adult moth: in vitro study of aldehyde metabolism in Heliothis virescens, Arch. Biochem. Biophys., 276:444.
Tu, G.-C. and Weiner, H., 1988a, Identification of the cysteine residue in the active site of horse liver mitochondrial aldehyde dehydrogenase, J. Biol. Chem., 263:1212.
Tu, G.-C. and Weiner, H., 1988b, Evidence for two distinct active sites on aldehyde dehydrogenase, J. Biol. Chem., 263:1218.
Weretilnyk, E.A. and Hanson, A.D., 1990, Molecular cloning of a plant etaine-aldehyde dehydrogenase, an enzyme implicated in adaptation to alinity and drought, Proc. Natl. Acad. Sci. USA, 87:2745.
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© 1990 Plenum Press, New York
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Pietruszko, R., Blatter, E., Abriola, D.P., Prestwich, G. (1990). Localization of Cysteine 302 at the Active Site of Aldehyde Dehydrogenase. In: Weiner, H., Wermuth, B., Crabb, D.W. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 3. Advances in Experimental Medicine and Biology, vol 284. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5901-2_4
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