Abstract
The efforts to characterize the enzymes involved in carbonyl metabolism have led in the past decade to the establishment of several classes of proteins, e.g. the aldo-keto reductase superfamily or to several classes of alcohol dehydrogenases (Jörnvall et al., 1981; Persson et al., 1991; Krozowsky, 1992; Bohren et al., 1989, Wales and Fewson, 1990). The relationship or ancestry to procaryotic proteins was revealed (Baker, 1991; Bohren et al., 1989) and led to the conclusion that — in the case of the short chain alcohol dehydrogenase superfamily (SCAD) — some vertebrate-type cellular communication and signal transduction pathways already have procaryotic and lower eucaryotic analogs (Baker, 1992; Lenard, 1992) which might have evolved from the confrontation of procaryonts with hydrophobic molecules like flavonoids or perhydrocyclopentanophenanthrenes i.e. steroids (Baker, 1992; Karlson, 1983). Vertebrate-type steroid hormone action is a consequence of intracellular hormone receptor specificity and its availability in the cell, hormone-receptor interaction with its cis acting HRE’s (hormone responsive elements) and for example in the case of mineralocorticoid action the existence of 11ß-hydroxysteroid dehydrogenases which regulate the intracellular active hormone level (Beato, 1989; Truss et al., 1992; Whorwood et al., 1992; Roy, 1992). This resembles in many aspects the situation in Rhizobia/plant signal transduction, where plant flavonoids and bacterial compounds act as signal molecules (Kondorosi, 1991; Baker, 1991). The complex process of signalling is achieved by different gene products, some of them e.g. NodG and fixR, belonging to the short chain alcohol dehydrogenase family. The relationship of these and other steroid dehydrogenases to other procaryotic and eucaryotic proteins and their membership to the SCAD family is established and underlines the importance of this protein family in uni- and multicellular physiology.
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Oppermann, U.C.T., Netter, K.J., Maser, E. (1993). Carbonyl Reduction by 3α-HSD from Comamonas Testosteroni — New Properties and its Relationship to the SCAD Family. In: Weiner, H., Crabb, D.W., Flynn, T.G. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 4. Advances in Experimental Medicine and Biology, vol 328. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2904-0_40
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DOI: https://doi.org/10.1007/978-1-4615-2904-0_40
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