SOLUBILIZATION OF 4-HYDROXYBENZOATE-POLYPRENYLTRANSFERASE FROM CELL-MEMBRANE OF PSEUDOMONAS-PUTIDA AND ITS PROPERTIES

被引：5

作者：

UCHIDA, K

KOIZUMI, N

KAWAJI, H

KAWAHARA, K

AIDA, K

机构：

[1] Institute of Applied Microbiology, The University of Tokyo, Bunkyo-ku, Tokyo, 113

[2] Pharmaceutical Research Center, Meiji Seika Kaisha, Ltd., Kohoku-ku, Yokohama, 222

[3] Research Laboratories of Nippon Chemipher, Misato, Saitama, 341

[4] The Kitasato Institute, Minato-ku, Tokyo, 108

[5] Otsuma Women’s University, Chiyoda-ku, Tokyo, 102

来源：

AGRICULTURAL AND BIOLOGICAL CHEMISTRY | 1991年 / 55卷 / 09期

关键词：

D O I：

10.1080/00021369.1991.10870950

中图分类号：

S3 [农学（农艺学）];

学科分类号：

0901 ;

摘要：

The enzyme of the first step in ubiquinone biosynthesis, 4-hydroxybenzoate-polyprenyltransferase was solubilized with 0.3% Triton X-100 from a membrane fraction of Pseudomonas putida IAM 1219. The enzyme had an optimum pH at 7.0-7.2 in 50 mM imidazole buffer and the apparent Km was 1.4 x 10(-4) M for nonaprenylpyrophosphate and 0.54 x 10(-5) M for 4-hydroxybenzoate. The enzyme required magnesium ion, and was completely inhibited by Cd2+, Cu2+, Ag+, Hg2+ at 0.1 mM concentration, and was also strongly inhibited by the thiol reagents, 4-chloromercuribenzoate and N-ethylmaleimide, indicating that the transferase is a thiol enzyme. The enzyme was strongly activated by adding phospholipids extracted from the bacterial cells, of which phosphatidylethanolamine was most effective.

引用

页码：2299 / 2305

页数：7

共 23 条

[1] 4-HYDROXYBENZOATE - POLYPRENYL TRANSFERASE AND PRENYLATION OF 4-AMINOBENZOATE IN MAMMALIAN-TISSUES [J].