Screening of riboflavin kinase activity in microorganisms
2009
I. S. Bilinska | L. R. Fayura | I. O. Mukalov | V. E. Kashchenko
The riboflavin kinase activity was measured in different species of bacteria, yeasts and molds. The activity of enzyme in eucaryotic microorganisms was mainly higher comparing to procaryotes. It was shown that bacterial and yeasts riboflavin kinases of investigated strain besides riboflavin can utilize its reduced form – 1,5 dihydroriboflavin as a substrate. Quantum chemical calculation of three-dimentional model of structure of oxidized and reduced form of riboflavin showed substantial differences in their configuration. No correlation between the activity of riboflavin kinase and dihydroriboflavin kinase in obligate aerobes and microaerophiles was observed.
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