Abstract
The sub-unit structure of many NAD-linked dehydrogenases is now firmly established. Thus the active forms of glyceraldehyde 3-phosphate dehydrogenase (GPDH) (1), yeast alcohol dehydrogenase (Y-ADH) (2a,b; 3) and lactic dehydrogenases (LDH) (4,5) are known to be tetramers, whereas alcohol dehydrogenases from horse liver (L-ADH) are dimers (6,7). Recent work on a number of monomeric enzymes such as lysozyme (8), ribonuclease (9), chymotrypsin (10), and carboxypeptidase (11) has illustrated how a knowledge of the molecular structure of an enzyme aids in the understanding of its mechanism of action. At present the detailed structure of an enzyme in three dimensions is best obtained from the results of X-ray diffraction analysis of crystals interpreted in conjunction with a knowledge of the amino acid sequence of its constituent polypeptide chains.
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