PARTIAL-PURIFICATION AND CHARACTERIZATION OF 4-HYDROXYBENZOATE-POLYPRENYLTRANSFERASE IN UBIQUINONE BIOSYNTHESIS OF PSEUDOMONAS-PUTIDA

被引：6

作者：

KAWAHARA, K ^{[1
]}

KOIZUMI, N ^{[1
]}

KAWAJI, H ^{[1
]}

OISHI, K ^{[1
]}

AIDA, K ^{[1
]}

UCHIDA, K ^{[1
]}

机构：

[1] UNIV TOKYO, INST APPL MICROBIOL, 1-1-1 YAYOI, BUNKYO KU, TOKYO 113, JAPAN

来源：

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

关键词：

D O I：

10.1080/00021369.1991.10870951

中图分类号：

S3 [农学（农艺学）];

学科分类号：

0901 ;

摘要：

4-Hydroxybenzoate-polyprenyltransferase, an enzyme in ubiquinone biosynthesis, from Pseudomonas putida was partially purified by ion-exchange and gel filtration column chromatography. The enzyme required phospholipid as an essential factor for activity. Hexaprenyl pyrophosphate(-PP) and pentaprenyl-PP as well as nonaprenyl-PP were used as polyprenyl donors, but tetraprenyl- and farnesyl-PPs were scarcely transferred to 4-hydroxybenzoic acid. No inhibition was observed by the end-product, ubiquinone-9 of P. putida. Long chain acyl-CoA, free fatty acids, or isopentenyl-PP strongly inhibited the enzyme activity. A possible regulatory role of the enzyme in bacterial ubiquinone biosynthesis is discussed.

引用

页码：2307 / 2311

页数：5

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