
The properties, regularities of biosynthesis and biochemical functions are considered of GTP-cyclohydrolases of microorganisms. The existence of two groups of these enzymes is established. The first group enzymes convert GTP into 7,8-dihydroneopterin-triphosphate and formiate. They participate in biosynthesis of tetrahydrofolic acid, tetrahydrobiopterin, molybdenic cofactor, pyrrolopyrimidine antibiotics and in a series of pigments. Representatives of the second group of cyclohydrolases convert GTP into 2,5-diamino-4-oxy-6-ribosylaminopyrimidine-5'-phosphate, formiate and pyrophosphate. They catalyze the first stages of formation of 6,7-dimethyl-8-ribityllumazine, flavins and their derivatives, toxoflavin (azapteridine antibiotics). The regulation of biosynthesis and activity of GTP-cyclohydrolases is studied only for individual enzymes of this group.
Binding Sites, Bacteria, Chemical Phenomena, Protein Conformation, Anti-Bacterial Agents, Pterins, Chemistry, Kinetics, Aminohydrolases, Flavins, Yeasts, Escherichia coli, Energy Metabolism, GTP Cyclohydrolase
Binding Sites, Bacteria, Chemical Phenomena, Protein Conformation, Anti-Bacterial Agents, Pterins, Chemistry, Kinetics, Aminohydrolases, Flavins, Yeasts, Escherichia coli, Energy Metabolism, GTP Cyclohydrolase
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