Dehydrogenases some generalizations

Biellmann, J.F. (1986) Chemistry and structure of alcohol dehydrogenase some general considerations on binding mode variability. Acc. Chem. Res.,... 

The structures of several dehydrogenases have now been solved. The work on these has been reviewed in depth in the literature, as have their physical and kinetic properties.1,9,10 Some generalizations can be made. As was discussed in Chapter 1, section D6, the subunits may be divided into two domains a catalytic domain, which can be quite variable in structure, and a nucleotide-binding domain, which is formed from a similar overall folding of the polypeptide chain for all the dehydrogenases. The detailed geometry of the nucleotide-binding... 

Everse and Kaplan (1) have recently reviewed the properties of LDH, while those of the coenzyme are discussed in Popjak s contribution to The Enzymes. A review of dehydrogenases in general has been given by Colowick et al. 3). More recent work is summarized in the article of the symposium edited by Sund (4). Although some lower organisms contain D-specific LDH (EC 1.1.1.28), we shall confine this review primarily to the L-specific enzyme. 

These enzymes catalyze the two-electron oxidation of purines, aldehydes and pyrimidines, sulfite, formate and nicotinic acid in the general reaction shown in equation (49). These enzymes show some differences in properties. Xanthine oxidase, xanthine dehydrogenase and aldehyde oxidase all have relatively low redox potentials and a unique cyanolyzable sulfur atom, and so will be discussed together. 

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