Abstract
An enzyme that uses GTP as a substrate for the formation of formate and a 2.4.5-triamino-6-hydroxypyrimidine derivative has been determined in the riboflavin overproducing yeast Pichia guilliermondii. In rib 1 mutants this enzyme is absent. This implies an involvement of the enzyme in the riboflavin biosynthesis and indicates that GTP is a purine precursor of riboflavin. Some properties of the GTP cyclohydrolase (substrate specificity, pH and temperature optima, activators and inhibitors, molecular weight, stability) were studied using a partly purified enzyme preparation. Cells grown under riboflavin overproducing conditions (iron deficiency) have 20–40-fold increased enzyme activity as compared with non-overproducing cultures (supplemented with iron).
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Abbreviations
- RF:
-
riboflavin
- DHRiboyslAP £:
-
2.5-diamino-6-hydroxy-4-(1′-d-ribosylamino)pyrimidine-5′-phosphate
- DHRibitylAP:
-
2.5-diamino-6-hydroxy-4-(1′-ribitylamino)pyrimidine
- neopterin:
-
6-(trihydroxypropyl)pterin
- DMP:
-
6.7-dimethylpterin
- Fe:
-
iron deficient condition
- +Fe:
-
supplemented with iron
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Shavlovsky, G.M., Logvinenko, E.M., Benndorf, R. et al. First reaction of riboflavin biosynthesis —Catalysis by a guanosine triphosphate cyclohydrolase from yeast. Arch. Microbiol. 124, 255–259 (1980). https://doi.org/10.1007/BF00427735
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DOI: https://doi.org/10.1007/BF00427735