Isolation and Properties of Spiramycin I 3–Hydroxyl
- 1 December 1979
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 86 (6) , 1753-1758
- https://doi.org/10.1093/oxfordjournals.jbchem.a132696
Abstract
An enzyme preparation able to acylate the hydroxyl group at C–3 of the lactone ring of spira-mycin was obtained from the spiramycin-producing strain, Streptomyces ambofaciens ISP-5053. The enzyme was purified about 33-fold from the crude extract by means of ammonium sulfate fractionsation, diethylaminoethyl (DEAE) cellulose batchwise elution and DEAE cellulose column chromatography. The optimum pH for the enzyme activity was 8.5. The enzyme was activated by Ca2+, Mg2+, in this order, but was inhibited by various SH reagents. Spiramycin I was the best substrate for the enzyme. The enzyme showed no preference between acetyl-CoA and propionyl-CoA.This publication has 0 references indexed in Scilit: