Differential centrifugation, precipitation with ammonium sulphate and chromatography on DEAE-cellulose led to a twenty-fold purification of glucosyltransferase from Streptomyces aureofaciens B 96. The Michaelis constants for glucosyluridyl diphosphate (UDP-glucose) was 10.8 microM for 1,2-dihydroxy-9,10-anthraquinone (alizarin) 110 microM; the maximum rate of glucosylation reaction was 5.32 mumol per s per mg protein. The pH optimum was at 7.1; the flat temperature optimum was at 30 degrees C. Using some hydroxy derivatives of 9,10-anthraquinone it was found that the production of glucosides from aglycones with alpha-hydroxyl groups was about 1/8 of the values obtained with beta-hydroxyl substrates. In both types of aglycones the presence of another hydroxyl group led to a higher glucoside production.

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Folia Microbiol (Praha). 1978;23(5):337-40 PubMed

Folia Microbiol (Praha). 1974;19(4):307-16 PubMed

Biochim Biophys Acta. 1957 Sep;25(3):575-8 PubMed

Folia Microbiol (Praha). 1969;14(3):215-25 PubMed

J Biol Chem. 1951 Nov;193(1):265-75 PubMed

Science. 1957 Jan 4;125(3236):12-5 PubMed

Alizarin glucosyl transferase activity in Streptomyces aureofaciens mutants

Microbial glucosidation of 1,2,4-trihydroxy-9,10-anthraquinone (purpurin)

Compounds isolated at the Department of Biogenesis of Natural Substances, Institute of Microbiology, Czechoslovak Academy of Sciences, in 1954-1983