Functional aspects of dinucleotide binding domains

Matrix Showing Relationships betw een Mono- and Dinticleotidb Binding Structures in Terms of Minimum Base Changes per Codon  

Velick, in Light and Life (W. D. McElroy and M. B. Glass, eds.), p. 108. Johns Hopkins Press, Baltimore, Marj-land, 1961. 

The similarities of the coenzyme conformation when bound to the dehydrogenases reflect the similarities of the fold in the dinucleotide binding domains and of detailed similarities in those regions that are actually involved in binding. Unfortunately, details on the interaction between 

NAD+ and s-MDH are not available because of lack of sequence information, but instead a schematic view of the important interactions between GAPDH and NAD are given in Fig. 10. 

Parameter (A) s-MDH (holo) s-MDH (apo) LDH LADH (ternary) (ADPR binary) GAPDH (holo, averaged) 

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