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Catabolism of indole‐3‐acetic acid in citrus leaves: identification and characterization of indole‐3‐aldehyde oxidase

Identifieur interne : 003861 ( Main/Exploration ); précédent : 003860; suivant : 003862

Catabolism of indole‐3‐acetic acid in citrus leaves: identification and characterization of indole‐3‐aldehyde oxidase

Auteurs : Leo Winer [Israël] ; Joseph Riov [Israël] ; Raphael Goren [Israël]

Source :

Physiologia Plantarum [ 0031-9317 ] ; 1993-09.

RBID : ISTEX:52120CE6FAB00FBC4D4FDA091454537E31462B95

Descripteurs français

Pascal (Inist)
- Activité enzymatique, Auxine, Catabolisme, Citrus sinensis, Cultivar, Feuille végétal, Indole-3-aldehyde oxidase, Indoleacétique acide, Isolement, Purification, Substance croissance végétal, cv Shamouti.

English descriptors

KwdEn :
- Auxin, Catabolism, Citrus sinensis, Cultivar, Enzymatic activity, IAA, IAA catabolism, Indoleacetic acid, Isolation, Plant growth substance, Plant leaf, Purification, indole‐3‐aldehyde, indole‐3‐carboxylic acid.

Abstract

A new enzyme, named indole‐3‐aldehyde oxidase (IAldO), was identified in citrus (Citrus sinensis L. Osbeck cv. Shamouti) leaves. The enzyme was partially purified by (NH4)2SO4 fractionation. Sephadex G‐200 gel filtration and DEAE‐cellulose ion exchange chromatography. IAldO catalyzes the oxidation of indole‐3‐aldehyde (IAld) to indole‐3‐carboxylic acid (ICA) with the production of H2O2. The enzyme is highly specific for IAld. The apparent KM of the enzyme for IAld is 19 μM. The optimum oxidation of IAld occurs at pH 7. 5. The molecular mass of the enzyme, as determined by Sepharose‐6B gel filtration, is about 200 kDa. Based on inhibitor studies, it is concluded that IAldO is not a flavin‐linked oxidase and there is no requirement for free sulfhydryl groups or divalent cations for maximum activity. The enzyme is strongly inhibited by benzaldehyde. Ethylene pretreatment, wounding and aging of leaf tissues did not affect enzyme activity, suggesting that the enzyme is constitutive in citrus tissues.

Url:

https://api.istex.fr/document/52120CE6FAB00FBC4D4FDA091454537E31462B95/fulltext/pdf

DOI: 10.1111/j.1399-3054.1993.tb01809.x

Affiliations:

Israël

Le document en format XML

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<term>IAA</term>
<term>IAA catabolism</term>
<term>Indoleacetic acid</term>
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<front><div type="abstract" xml:lang="en">A new enzyme, named indole‐3‐aldehyde oxidase (IAldO), was identified in citrus (Citrus sinensis L. Osbeck cv. Shamouti) leaves. The enzyme was partially purified by (NH4)2SO4 fractionation. Sephadex G‐200 gel filtration and DEAE‐cellulose ion exchange chromatography. IAldO catalyzes the oxidation of indole‐3‐aldehyde (IAld) to indole‐3‐carboxylic acid (ICA) with the production of H2O2. The enzyme is highly specific for IAld. The apparent KM of the enzyme for IAld is 19 μM. The optimum oxidation of IAld occurs at pH 7. 5. The molecular mass of the enzyme, as determined by Sepharose‐6B gel filtration, is about 200 kDa. Based on inhibitor studies, it is concluded that IAldO is not a flavin‐linked oxidase and there is no requirement for free sulfhydryl groups or divalent cations for maximum activity. The enzyme is strongly inhibited by benzaldehyde. Ethylene pretreatment, wounding and aging of leaf tissues did not affect enzyme activity, suggesting that the enzyme is constitutive in citrus tissues.</div>
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Catabolism of indole‐3‐acetic acid in citrus leaves: identification and characterization of indole‐3‐aldehyde oxidase

Catabolism of indole‐3‐acetic acid in citrus leaves: identification and characterization of indole‐3‐aldehyde oxidase

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

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