Feb 1, 1976

Purification and properties of the riboflavin kinase of the yeast Pichia guilliermondii

Biokhimii︠a︡
V E Kashchenko, Shavlovskiĭ

Abstract

Riboflavin kinase (E.C.2.7.1.26) was isolated from the cells of the yeast Pichia guilliermondii. The enzyme was 680-fold purified uzing ammonium sulphate fractionation, chromatography on DEAE-Sephadex A-50 and CM-Sephadex C-50 and gel-filtration through Sephadex G-75. Purified enzyme preparation was free from phosphatases and FAD-synthetase. The pH optimum was 8,7, the temperature optimum-45 degrees C. The enzyme was activated by Zn2+, Mg2+ and Co2+ ions. Km for riboflavin was 1,0x10(-5) M, for ATP -- 6,7X10(-6) M. Riboflavin kinase catalyzed the phosphorylation of riboflavin analogues with the substitution of methyl groups at positions 7 and 8. UTP, GTP, ADP and CTP, besides ATP, were phosphate donors. AMP inhibited the enzyme activity. Molecular weight of the enzyme was 28000, as estimated by gel-filtration through Sephadex G-150. Purified riboflavin kinase was stable under storage.

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Mentioned in this Paper

Sephadex G
Pichia guilliermondii
Filtration
Phosphoric Monoester Hydrolases
Chromatography
Protein Phosphorylation
Phosphate Measurement
Riboflavin
DEAE-Sephadex A-50
Enzyme agent

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