Abstract
Aldehyde and alcohol dehydrogenases (ALDHs and ADHs) are both highly multiple enzymes with many different forms in metabolically linked functional pathways. However, they are derived from separate protein families with distinct properties. Those of the vertebrate ADHs have been well characterized since long, and their different classes belong to the MDR protein family of known structures from several sources. However, the properties and multiplicity of the ALDHs have only recently been partly characterized. Presently, just three of the at least twelve different ALDH classes (Yoshida et al., 1998) are kn in three-dimensional structure (Liu et al., 1997; Steinmetz et al., 1997; Johansson et al.998), several have not been purified and characterized enzymatically, and little is known about their species or class variabilities.
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Hjelmqvist, L., El-Ahmad, M., Johansson, K., Norin, A., Ramaswamy, S., Jörnvall, H. (1999). Structure and Function of Betaine Aldehyde Dehydrogenase. In: Weiner, H., Maser, E., Crabb, D.W., Lindahl, R. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 7. Advances in Experimental Medicine and Biology, vol 463. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4735-8_5
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DOI: https://doi.org/10.1007/978-1-4615-4735-8_5
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