Findings of trigonelline demethylating enzyme activity in various organisms and some properties of the enzyme from hog liver.
Trigonelline demethylating enzyme activity was found widely in animals, plants and microorganisms. Very high enzyme activity of this enzyme was detected in hog liver. Properties of the hog liver enzyme were investigated. Optimum pH for the enzymic reaction was observed at 8.5. The Km value for trigonelline was calculated at 2.77 mM. Addition of any cofactor is not required for the reaction The enzyme activity was inhibited by heavy metal ions. The reaction product was identified as nicotinic acid. Proposed enzyme reaction mechanism and the role of this enzyme in biosynthesis and metabolism of NAD are discussed.
D000470:Alkaloids; D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D004524:Eels; D004926:Escherichia coli; D006863:Hydrogen-Ion Concentration; D008099:Liver / Q000201:enzymology*; D009539:Nicotinic Acids / Q000378:metabolism*; D010089:Oxidoreductases, N-Demethylating / Q000302:isolation & purification*; D010944:Plants; D051381:Rats; D012441:Saccharomyces cerevisiae; D013045:Species Specificity; D013552:Swine
D000470:Alkaloids; D009539:Nicotinic Acids; C009560:trigonelline; D010089:Oxidoreductases, N-Demethylating