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(EC 2.4.2.19) from hog kidney were investigated. Phthalic acid and Pyrazine-2, 3-dicarboxylic acid were both competitive inhibitors for quinolinic acid. The enzyme activity was inhibited by heavy metal divalent cations and trivalent cations. Nucleoside triphosphates also inhibited the enzyme activity and this inhibition was recovered by raising the MgCl2 concentration. Glycerol activated the enzyme activity at pH from 4.0 to 4.4, while it inhibited at above pH 5.0. Isoleucine content of the crystalline enzyme was extremely low (17 residues

Crystalline quinolinate phosphoribosyltransfease from hog kidney: characteristic properties and chemical modifications.