The novel pathway for ketodiene oxylipin biosynthesis in Jerusalem artichoke (Helianthus tuberosus) tubers

被引:8
作者
Chechetkin, IR [1 ]
Medvedeva, NV [1 ]
Grechkin, AN [1 ]
机构
[1] Russian Acad Sci, Kazan Inst Biochem & Biophys, Lab Oxylipins, Kazan 420111, Russia
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS | 2004年 / 1686卷 / 1-2期
基金
俄罗斯基础研究基金会;
关键词
lipoxygenase pathway; ketodiene oxylipin; hydroxydiene dehydrogenase; Jerusalem artichoke (Helianthus tuberosus);
D O I
10.1016/j.bbalip.2004.07.001
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The new route of the plant lipoxygenase pathway, directed specifically towards the ketodiene formation, was detected during in vitro experiments with Jerusalem artichoke (Helianthus tuberosus) tubers. Through this pathway (9Z,11E,13S)-13-hydroperoxy-9,11-octadecadienoic acid (13-HPOD) is reduced to corresponding 13-hydroxy acid (13-HOD), which is in turn dehydrogenated into ketodiene (9Z,11E,13S)-13-oxo-9,11-octadecadienoic acid (13-KOD). Dehydrogenation of 13-HOD into 13-KOD was not dependent on the presence of either NAD or NADP, but was strongly dependent on the presence of oxygen. Under anoxic conditions, 13-HOD dehydrogenation was blocked, but addition of 2,6-dichlorophenolindophenol restored it. Sulfite addition fully suppressed the aerobic dehydrogenation of 13-HOD. Hydrogen peroxide is a by-product formed by the enzyme along with 13-KOD. These data suggest that the ketodiene biosynthesis in H. tuberosus tubers is catalyzed by flavin dehydrogenase. (9S, 10E, 12Z)-9-Hydroxy-10, 12-octadecadienoic acid (9-HOD) is dehydrogenated by this enzyme as effectively as 13-HOD, while alpha-ketol, (9Z)-12-oxo-13-hydroxy-9-octadecenoic acid, and ricinoleic acid did not act as substrates for dehydrogenase. The enzyme was soluble and possessed a pH optimum at pH 7.0-9.0. The only 13-HOD dehydrogenase known so far was detected in rat colon. However, unlike the H. tuberosus enzyme, the rat dehydrogenase is NAD-dependent. (C) 2004 Elsevier B.V All rights reserved.
引用
收藏
页码:7 / 14
页数:8
相关论文
共 31 条
[1]   Reactive electrophile species activate defense gene expression in Arabidopsis [J].
Alméras, E ;
Stolz, S ;
Vollenweider, S ;
Reymond, P ;
Mène-Saffrané, L ;
Farmer, EE .
PLANT JOURNAL, 2003, 34 (02) :202-216
[2]   Catalysis of diaphorase reactions by Mycobacterium tuberculosis lipoamide dehydrogenase occurs at the EH4 level [J].
Argyrou, A ;
Sun, GX ;
Palfey, BA ;
Blanchard, JS .
BIOCHEMISTRY, 2003, 42 (07) :2218-2228
[3]   Substrate specificity and characterization of partially purified rat liver 13-hydroxyoctadecadienoic acid (13-HODE) dehydrogenase [J].
Bronstein, JC ;
Bull, AW .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1997, 348 (01) :219-225
[4]   PRODUCTION OF UNSATURATED CARBONYL-COMPOUNDS DURING METABOLISM OF HYDROPEROXY FATTY-ACIDS BY COLONIC HOMOGENATES [J].
BULL, AW ;
BRONSTEIN, JC .
CARCINOGENESIS, 1990, 11 (10) :1699-1704
[5]   METABOLISM OF OXIDIZED LINOLEIC-ACID - DISTRIBUTION OF ACTIVITY FOR THE ENZYMATIC OXIDATION OF 13-HYDROXYOCTADECADIENOIC ACID TO 13-OXOOCTADECADIENOIC ACID IN RAT-TISSUES [J].
BULL, AW ;
EARLES, SM ;
BRONSTEIN, JC .
PROSTAGLANDINS, 1991, 41 (01) :43-50
[6]   Purification and characterization of broad bean lipoxygenase isoenzymes [J].
Clemente, A ;
Olías, R ;
Olías, JM .
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2000, 48 (04) :1070-1075
[7]   PRODUCTION, PURIFICATION AND CHARACTERIZATION OF AN ALCOHOL OXIDASE OF THE LIGNINOLYTIC FUNGUS PENIOPHORA-GIGANTEA [J].
DANNEEL, HJ ;
REICHERT, A ;
GIFFHORN, F .
JOURNAL OF BIOTECHNOLOGY, 1994, 33 (01) :33-41
[8]   RAPID ISOLATION OF A PLANT MICROSOMAL FRACTION BY MG2+-PRECIPITATION [J].
DIESPERGER, H ;
MULLER, CR ;
SANDERMANN, H .
FEBS LETTERS, 1974, 43 (02) :155-158
[9]   The intraflavin hydrogen bond in human electron transfer flavoprotein modulates redox potentials and may participate in electron transfer [J].
Dwyer, TM ;
Mortl, S ;
Kemter, K ;
Bacher, A ;
Fauq, A ;
Frerman, FE .
BIOCHEMISTRY, 1999, 38 (30) :9735-9745
[10]   METABOLISM OF OXIDIZED LINOLEIC-ACID - CHARACTERIZATION OF 13-HYDROXYOCTADECADIENOIC ACID DEHYDROGENASE-ACTIVITY FROM RAT COLONIC TISSUE [J].
EARLES, SM ;
BRONSTEIN, JC ;
WINNER, DL ;
BULL, AW .
BIOCHIMICA ET BIOPHYSICA ACTA, 1991, 1081 (02) :174-180