Arthur C. Gentile

The effect of 3-amino-1,2,4-triazole on phosphorylase of Oscillatoria princeps.

Abstract 1. 1. The inhibitory effect of 3-AT on Oscillatoria princeps phosphorylase is probably due to the chelation by 3-AT of the essential metal required by this enzyme. 2. 2. The inhibition of this phosphorylase by 3-AT can be effectively reversed by the addition of manganous or ferric ions only in the proper concentrations for forming the bivalent and trivalent chelates. 3. 3. Evidence is presented for the 3:1 structure of the ferric chelate of 3-AT.

The structure of the d-glucose adduct of 3-amino-1,2,4-triazole: Infrared absorption studies

Abstract Chemical tests and infrared absorption spectra indicate that the d -glucose adduct of 3-amino-1,2,4-triazole is a definite chemical compound, an amine glucoside or secondary amine. The participation of this amine glucoside in phosphorylating reactions is discussed with respect to the observed effects on carbohydrate-metabolizing enzymes such as hexokinase and phosphorylase.

Physico-chemical studies of the metabolic end-product of 3-amino-1,2,4-triazole in yeast

Abstract The first step in the metabolism of the phytotoxic compound, 3-amino-1,2,4-triazole in yeast is its linking with glucose to form an amine glucoside. This compound may then be phosphorylated by hexokinase and split by yeast aldolase. Isolation of the end-product of this metabolism has made possible the delineation of its physico-chemical properties and an interpretation of its molecular structure via infrared studies.

The stability constant of the manganese chelate of 3-amino-1,2,4-triazole

Abstract 1. 1. The stability constant, log K , for the manganese chelate of 3-amino-1,2,4-tri-azole (3-AT) has been determined via ion-exchange methods to be 2.3–2.4. 2. 2. In light of the fact that this log K is ten times smaller than that of the enzyme, it is seriously doubted that the inhibition of Oscillatoria phosphorylase by 3-AT can be explained by chelation phenomenon. 3. 3. The possibility is advanced that a glucose complex formed by the interaction of 3-AT and glucose 1-phosphate causes a competitive type of inhibition of this enzyme.