%0 Journal Article
%T A study on indolepyruvic acid methyltransferase in chuangxinmycin-producing strain<br>创新霉素产生菌吲哚丙酮酸甲基转移酶的研究
%A J Cao
%A T Q Qi
%A <br>曹兢
%A 戚天庆
%J 微生物学报
%D 1989
%I 
%X The indolepyruvic acid methyltransferase, perhaps which is active in the biosynthetic pathway of the antibiotic chuangxinmycin, has been detected and partially purified from cell-free extracts of Actinoplanes jinanensis n. sp., This enzyme catalyzes the transfer of a methyl group from S-adenosylmethionine to indolepyruvic acid. The methyltransferase has been purified 60-fold by ammonium sulfate fractionation and DEAE-cellulose column chromatography. The enzyme optimal substrate is indolepyruvic acid. The enzyme has a pH optimum of 7.5. The double reciprocal plots gave Km values of 4.0 X 10(-5) mol/L for S-adenosylmethionine and 1.8 X 10(-7) mol/L for indolepyruvic acid. A molecular weight of 55000 +/- 5000 has been determined by Sephadex G-150 gel filtration.
%K 创新霉素生物合成
%K 吲哚丙酮酸甲基转移酶分离
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A3C6BA55AB623B90FA9104CFFC826F3C&aid=9D4495AC2B00B56E53410BF9765E4F03&yid=1833A6AA51F779C1&vid=771469D9D58C34FF&iid=CA4FD0336C81A37A&sid=E84BBBDDD74F497C&eid=5D71B28100102720&journal_id=0001-6209&journal_name=微生物学报&referenced_num=0&reference_num=3