Molybdoenzymes and molybdenum cofactor in plants

The transition element molybdenum (Mo) is essential for (nearly) all organisms and occurs in more than 40 enzymes catalysing diverse redox reactions, however, only four of them have been found in plants. (1) Nitrate reductase catalyses the key step in inorganic nitrogen assimilation, (2) aldehyde ox...

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Veröffentlicht in:Journal of experimental botany. - 1985. - 53(2002), 375 vom: 04. Aug., Seite 1689-98
1. Verfasser: Mendel, Ralf R (VerfasserIn)
Weitere Verfasser: Hänsch, Robert
Format: Aufsatz
Sprache:English
Veröffentlicht: 2002
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Review Arabidopsis Proteins Cnx protein, Arabidopsis Coenzymes Enzymes Metalloproteins Molybdenum Cofactors Pteridines Sulfur mehr... 70FD1KFU70 Abscisic Acid 72S9A8J5GW Molybdenum 81AH48963U molybdenum cofactor ATN6EG42UQ Xanthine Dehydrogenase EC 1.17.1.4 Aldehyde Oxidoreductases EC 1.2.- Aldehyde Oxidase EC 1.2.3.1 Nitrate Reductases EC 1.7.- Nitrate Reductase EC 1.7.99.4 Oxidoreductases Acting on Sulfur Group Donors EC 1.8.-
Beschreibung
Zusammenfassung:The transition element molybdenum (Mo) is essential for (nearly) all organisms and occurs in more than 40 enzymes catalysing diverse redox reactions, however, only four of them have been found in plants. (1) Nitrate reductase catalyses the key step in inorganic nitrogen assimilation, (2) aldehyde oxidase(s) have been shown to catalyse the last step in the biosynthesis of the phytohormone abscisic acid, (3) xanthine dehydrogenase is involved in purine catabolism and stress reactions, and (4) sulphite oxidase is probably involved in detoxifying excess sulphite. Among Mo-enzymes, the alignment of amino acid sequences permits domains that are well conserved to be defined. With the exception of bacterial nitrogenase, Mo-enzymes share a similar pterin compound at their catalytic sites, the molybdenum cofactor. Mo itself seems to be biologically inactive unless it is complexed by the cofactor. This molybdenum cofactor combines with diverse apoproteins where it is responsible for the correct anchoring and positioning of the Mo-centre within the holo-enzyme so that the Mo-centre can interact with other components of the enzyme's electron transport chain. A model for the three-step biosynthesis of Moco involving the complex interaction of six proteins will be described. A putative Moco-storage protein distributing Moco to the apoproteins of Mo-enzymes will be discussed. After insertion, xanthine dehydrogenase and aldehyde oxidase, but not nitrate reductase and sulphite oxidase, require the addition of a terminal sulphur ligand to their Mo-site, which is catalysed by the sulphur transferase ABA3
Beschreibung:Date Completed 17.12.2002
Date Revised 03.12.2021
published: Print
Citation Status MEDLINE
ISSN:1460-2431