BENZOIC-ACID 2-HYDROXYLASE, A SOLUBLE OXYGENASE FROM TOBACCO, CATALYZES SALICYLIC-ACID BIOSYNTHESIS

被引：145

作者：

LEON, J ^{[1
]}

SHULAEV, V ^{[1
]}

YALPANI, N ^{[1
]}

LAWTON, MA ^{[1
]}

RASKIN, I ^{[1
]}

机构：

[1] RUTGERS STATE UNIV,CTR AGR MOLEC BIOL,NEW BRUNSWICK,NJ 08903

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1995年 / 92卷 / 22期

关键词：

NICOTIANA TABACUM; TOBACCO MOSAIC VIRUS; CYTOCHROME P450; ACQUIRED RESISTANCE;

D O I：

10.1073/pnas.92.22.10413

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Benzoic acid 2-hydroxylase (BA2H) catalyzes the biosynthesis of salicylic acid from benzoic acid. The enzyme has been partially purified and characterized as a soluble protein of 160 kDa. High-efficiency in vivo labeling of salicylic acid with O-18(2) suggested that BA2H is an oxygenase that specifically hydroxylates the ortho position of benzoic acid. The enzyme was strongly induced by either tobacco mosaic virus inoculation or benzoic acid infiltration of tobacco leaves and it was inhibited by CO and other inhibitors of cytochrome P450 hydroxylases. The BA2H activity was immunodepleted by antibodies raised against SU2, a soluble cytochrome P450 from Streptomyces griseolus. The anti-SU2 antibodies immunoprecipitated a radiolabeled polypeptide of around 160 kDa from the soluble protein extracts of L-[S-35]-methionine-fed tobacco leaves. Purified BA2H showed CO-difference spectra with a maximum at 457 nm. These data suggest that BA2H belongs to a novel class of soluble, high molecular weight cytochrome P450 enzymes.

引用

页码：10413 / 10417

页数：5

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