Lactic oxidative decarboxylase

Studies on the properties and mechanisms of oxygenases have been greatly hampered by the fact that none of the oxygenases, except lactic oxidative decarboxylase, has thus far been obtained in crystalline form. 

More recently, L-lysine oxidase was shown to catalyze incorporation of atmospheric oxygen. The over-all reaction is quite similar to that catalyzed by lactic oxidative decarboxylase and is shown below (Itada et al., 1961) (Eq. 27). 

See also Oxidative Phosphorylation (from Chapter 15), Regulation of Glycolysis, Fructose-2,6-Bisphosphate Regulation (from Chapter 16), Reactions/Energies of Glycolysis, Lactic Acid fermentation. Pyruvate Decarboxylase, Alcohol Dehydrogenase, Alcoholic Fermentation, Aerobic vs. Anaerobic Glycolysis... 

The demonstration by Phillips and Laiigdon (1956) that the level of TPNH-cytochromc c reductase is increased in the livers of hyperthyroid rats and reduced in those of hypothyroid animals is of particular interest. Since the activity of this enzyme results in the production of triphospho-pyridiiie nucleotide (TPN), a cofactor required for many oxidative enzymes, this change is probably a direct reflection of the general over-all acceleration of oxidative processes, and, more specifically, of those which are TPN-linked. Decreased activity of lactic dehydrogenase (Vcstling and Knocpfelmacher, 1950) is compatible with the demonstrated ability of thyroxine to inhibit this enzyme in vitro (Wolff and Wolff, 1957 Radsma et al., 1957). Decreases in the in vivo activity of such enzymes as tyrosine oxidase, DOPA-decarboxylase, betaine-homocysteine transmethylase, and... 

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