title: [The activity of enzymes involved in synthesis and hydrolysis of flavin adenine dinucleotide is Pichia guilliermondii studies at different levels of flavinogenesis].
abstract: The activity of FAD-pyrophosphorylase and FAD-hydrolase (nucleotidepyrophosphatase) was studied in extracts of Pichia guilliermondii ATCC 9058 capable of riboflavin over-production. The specific activity of the enzymes was highest at the logarithmic growth phase (2.6 and 3.8 mcmoles of FAD per 1 min per 1 mg of protein X10(-5), respectively), and did not increase upon the induction of riboflavin overproduction. A decrease in the content of hemin compounds and a low content of flavins in the cells of Pichia guilliermondii mutants had no considerable effect on the activity of the two enzymes. When the yeast was cultivated on a medium containing hexadecane, an increase in the content of FAD in the cells was not accompanied with a rise in the activity of FAD-pyrophosphorylase. The activity of the enzyme did not change when succinate and lactate, the substrates of FAD-containing enzymes, were used as the source of carbon. The activity of FAD-pyrophosphorylase increased only when iron-deficient cells of the yeast were grown or incubated on a medium containing glycine; this stimulation was inhibited by cycloheximide.
mesh_terms: D001203:Ascomycota / Q000378:metabolism*; D005182:Flavin-Adenine Dinucleotide / Q000378:metabolism*; D007700:Kinetics; D009713:Nucleotidyltransferases / Q000378:metabolism; D010843:Pichia / Q000378:metabolism*; D011755:Pyrophosphatases / Q000378:metabolism
chemical_list: D005182:Flavin-Adenine Dinucleotide; D009713:Nucleotidyltransferases; D011755:Pyrophosphatases
vernacular_title: Issledovanie aktivnosti fermentov, uchastvuiushchikh v sinteze i gidrolize flavinadenin-dinkleotida u drozhzheĭ Pichia guilliermondii pri razlichnykh urovniakh flavinogeneza.