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Molybdenum cofactor biosynthesis and molybdenum enzymes
Günter Schwarz1, Ralf R Mendel
1Institute of Plant Biology, Technical University Braunschweig, 38023 Braunschweig, Germany. gschwarz@uni-koeln.de
Annual Review of Plant Biology
|May 4, 2006
Summary
The molybdenum cofactor (Moco) is essential for plant enzymes involved in nitrate assimilation, sulfite detoxification, hormone biosynthesis, and purine degradation. Its synthesis involves a conserved pathway from GTP, crucial for plant health and stress response.
Area of Science:
- Biochemistry
- Plant Physiology
- Enzymology
Background:
- The molybdenum cofactor (Moco) is vital for the active site of all eukaryotic molybdenum (Mo) enzymes.
- Moco comprises molybdenum bound to a unique molybdopterin moiety, synthesized via a conserved pathway from GTP.
Purpose of the Study:
- To elucidate the synthesis and function of the Moco in plants.
- To detail the roles of four key plant Mo-enzymes: nitrate reductase, sulfite oxidase, aldehyde oxidase, and xanthine dehydrogenase.
Main Methods:
- Review of the established Moco biosynthetic pathway from GTP.
- Identification and functional categorization of four distinct molybdenum enzymes in plants.
Main Results:
- Moco synthesis involves intermediates like cyclic pyranopterin monophosphate and adenylated molybdopterin.
- Four plant Mo-enzymes perform critical functions: nitrate assimilation, sulfite detoxification, abscisic acid biosynthesis, and purine degradation.
Conclusions:
- The conserved Moco biosynthesis pathway is fundamental to plant metabolism.
- Plant Mo-enzymes play essential roles in nutrient assimilation, detoxification, hormone regulation, and stress response.