Human Liver High Km Aldehyde Dehydrogenase (ALDH4): Properties and Structural Relationship to the Glutamic γ-Semialdehyde Dehydrogenase

Author:

Agarwal Dharam P.,Eckey Rolf,Hempel John,Goedde H. Werner

Publisher

Springer US

Reference8 articles.

1. Agarwal, D.P., Eckey, R., Rudnay, A.C., Volkens, T., and Goedde, H.W., 1989, High Km aldehyde dehydrogenase isozymes in human tissues: constitutive and tumor-associated forms, in: Progress in Clinical and Biological Research, Vol. 290: “Enzymology and Molecular Biology of Carbonyl Metabolism 2”, H. Weiner and T.G. Flynn, eds., Alan R. Liss, New York, p. 119.

2. Harada, S., Agarwal, D.P., and Goedde, H.W., 1980, Electrophoretic and biochemical studies of human aldehyde dehydrogenase isozymes in various tissues. Life Sci. 26: 1771.

3. Eckey, R., Agarwal, D.P., Hempel, J., Timmann, R., and Goedde, H.W., 1991, Biochemical, immunological, and molecular characterization of a “high Km” aldehyde dehydrogenase, in: Advances in Experimental Medicine and Biology, Vol. 284: “Enzymology and Molecular Biology of Carbonyl Metabolism 3”, H. Weiner, B. Wermuth and D.W. Crabb, eds., Plenum Press, New York, p. 43.

4. Forte-McRobbie, C.M. and Pietruszko, R., 1986, Purification and characterization of human liver high Km aldehyde dehydrogenase and its identification as glutamic γ-semialdehyde dehydrogenase. J. Biol. Chem. 261: 2154.

5. 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. 4: 2837.

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