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Titolo:
A dual function alpha-dioxygenase-peroxidase and NAD(+) oxidoreductase active enzyme from germinating pea rationalizing alpha-oxidation of fatty acids in plants
Autore:
Saffert, A; Hartmann-Schreier, J; Schon, A; Schreier, P;
Indirizzi:
Univ Wurzburg, Inst Pharm & Food Chem, D-97074 Wurzburg, Germany Univ Wurzburg Wurzburg Germany D-97074 d Chem, D-97074 Wurzburg, Germany Univ Wurzburg, Inst Biochem, D-97074 Wurzburg, Germany Univ Wurzburg Wurzburg Germany D-97074 iochem, D-97074 Wurzburg, Germany
Titolo Testata:
PLANT PHYSIOLOGY
fascicolo: 4, volume: 123, anno: 2000,
pagine: 1545 - 1551
SICI:
0032-0889(200008)123:4<1545:ADFAAN>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
LIPOXYGENASE PATHWAY; ULVA-PERTUSA; BIOSYNTHESIS; OXYGENASE; IDENTIFICATION; CYCLOOXYGENASE; BIOCHEMISTRY; EPOXIDATION; EXPRESSION; ALDEHYDES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Schreier, P Univ Wurzburg, Inst Pharm & Food Chem, Hubland, D-97074 Wurzburg, Germany Univ Wurzburg Hubland Wurzburg Germany D-97074 zburg, Germany
Citazione:
A. Saffert et al., "A dual function alpha-dioxygenase-peroxidase and NAD(+) oxidoreductase active enzyme from germinating pea rationalizing alpha-oxidation of fatty acids in plants", PLANT PHYSL, 123(4), 2000, pp. 1545-1551

Abstract

An enzyme with fatty acid alpha-oxidation activity (49 nkat mg(-1); substrate: lauric acid) was purified from germinating pea (Pisum Sativum) by a five-step procedure to apparent homogeneity. The purified protein was found to be a 230-kD oligomer with two dominant: subunits, i.e. a 50-kD subunit with NAD oxidoreductase activity and a 70-kD subunit, homolog to a pathogen-induced oxygenase, which in turn shows significant homology to animal cyclooxygenase. On-line liquid chromatography-electrospray ionization-tandem massspectrometry revealed rapid alpha-oxidation of palmitic acid incubated at 0 degrees C with the purified alpha-oxidation enzyme, leading to (R)-2-hydroperoxypalmitic acid as the major product together with (R)-2-hydroxyyalmitic acid, 1-pentadecanal, and pentadecanoic acid. Inherent peroxidase activity of the 70-kD fraction decreased the amount of the (R)-2-hydroperoxy product rapidly and increased the level of (R)-2-hydroxypalmitic acid. Incubations at room temperature accelerated the decline toward the chain-shortened aldehyde. With the identification of the dual function alpha-dioxygenase-peroxidase (70-kD unit) and the related NAD(+) oxidoreductase (50-kD unit) weprovided novel data to rationalize all steps of the classical scheme of alpha-oxidation in plants.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/08/20 alle ore 02:54:48