Abstract
Aldehyde dehydrogenase has the ability to catalyse the hydrolysis of p-nitrophenyl esters as well as the dehydrogenation of aldehydes by NAD+. Some work has been interpreted in terms of two different types of active site (Blackwell et al., 1983), but much other evidence points to the identity of the dehydrogenase and esterase sites (Loomes and Kitson, 1986; Kitson et al., 1991). In particular, Cys-302 has been identified as the nucleophile that becomes acylated by the aldehyde substrate trans-4-(N,N-dimethylamino)cinnamaldehyde (Pietruszko et al., 1993) and by the ester substrate analogue p-nitrophenyl dimethylcar-bamate (Kitson et al., 1991). Thus studying the esterase activity of aldehyde dehydrogenase should be capable of giving information about the active site of relevance to the dehydrogenase activity.
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References
Blackwell, L.F., Bennett, A.F. and Buckley, P.D., 1983, Relationship between the mechanisms of the esterase and dehydrogenase activities of the cytoplasmic aldehyde dehydrogenase from sheep liver. An alternative view, Biochemistry, 22: 3784–3791.
Blackwell, L.F., MacGibbon, A.K.H. and Buckley, P.D., 1989, Aldehyde dehydrogenases — kinetic characterisation, In Human Metabolism of Alcohol, vol. II (Crow, K.E. and Batt, R.D., eds), pp. 89–104, CRC Press, Boca Raton, Florida.
Blatter, E.E., Tasayco, M.L., Prestwich, G. and Pietruszko, R., 1990, Chemical modification of aldehyde dehydrogenase by a vinyl ketone analogue of an insect pheromone, Biochem. J., 272: 351–358.
Ghenbot, G. and Weiner, H., 1992, Purification of liver aldehyde dehydrogenase by p-hydroxyacetophenone-Sepharose affinity matrix and the coelution of chloramphenicol acetyl transferase from the same matrix with recombinantly expressed aldehyde dehydrogenase, Protein Expression Purif., 3: 470–478.
Hempel, J.D., Nicholas, H. and Lindahl, R., 1993, Aldehyde dehydrogenases: widespread structural and functional diversity within a shared framework, Protein Science, 2: 1890–1900.
Kitson, T.M., 1989a, Kinetics of p-nitrophenyl pivalate hydrolysis catalysed by cytoplasmic aldehyde dehydrogenase, Biochem. J., 257: 573–578.
Kitson, T.M., 1989b, The action of cytoplasmic aldehyde dehydrogenase on methy p-nitrophenyl carbonate and p-nitrophenyl dimethylcarbamate, Biochem. J., 251: 579–584.
Kitson, T.M. and Kitson, K.E., 1994, Probing the active site of cytoplasmic aldehyde dehydrogenase with a chromophoric reporter group, Biochem. J., 300: 25–30.
Kitson, T.M., Hill, J.P. and Midwinter, G.G., 1991, Identification of a catalytically essential nucleophilic residue in sheep liver cytoplasmic aldehyde dehydrogenase, Biochem. J., 275: 207–210.
Leatherbarrow, R.J., 1987, Enzfitter Manual, Elsevier Science Publishers, Amsterdam.
Loomes, K.M. and Kitson, T.M., 1986, Aldehyde dehydrogenase catalyses acetaldehyde formation from 4-nitrophenyl acetate and NADH, Biochem. J., 238: 617–619.
Pietruszko, R., Abriola, D.P., Blatter, E.E. and Mukerjee, N., 1993, Aldehyde dehydrogenase: aldehyde dehydrogenation and ester hydrolysis, In Enzymology and Molecular Biology of Carbonyl Metabolism 4, (Weiner, H., Crabb, D.W. and Flynn, T.G., eds), pp. 221–232, Plenum Press, New York and London.
Ragsdale, C.W. and Brockes, J.P., 1991, Retinoids and their targets in vertebrate development, Current Opinion in Cell Biol., 3: 928–934.
Tobias, P., Heidema, J.H., Lo, K.W., Kaiser, E.T. and KEzdy, F.J., 1969, The α-chymotrypsin-catalysed hydrolysis of lactones, J. Amer. Chem. Soc, 91: 202–203.
Yoshida, A., Hsu, L.C. and Yanagawa, Y., 1993, Biological role of human cytosolic aldehyde dehydrogenase 1: hormonal response, retinal oxidation and implication in testicular feminisation, In Enzymology and Molecular Biology of Carbonyl Metabolism 4, (Weiner, H., Crabb, D.W. and Flynn, T.G., eds), pp. 37–44, Plenum Press, New York and London.
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© 1995 Springer Science+Business Media New York
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Kitson, K.E., Blythe, T.J., Kitson, T.M. (1995). Studies of the Esterase Activity of Cytosolic Aldehyde Dehydrogenase Using Sterically Hindered and Cyclic Substrates. In: Weiner, H., Holmes, R.S., Wermuth, B. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 5. Advances in Experimental Medicine and Biology, vol 372. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1965-2_6
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DOI: https://doi.org/10.1007/978-1-4615-1965-2_6
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