Molybdenum cofactor biosynthesis and deficiency |
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Authors: | G Schwarz |
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Institution: | Institute of Plant Biology, Technical University Braunschweig, Spielmannstrasse 7, 38106, Braunschweig, Germany. |
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Abstract: | The molybdenum cofactor (Moco) forms the active site of all molybdenum (Mo) enzymes, except nitrogenase. Mo enzymes catalyze
important redox reactions in global metabolic cycles. Moco consists of Mo covalently bound to one or two dithiolates attached
to a unique tricyclic pterin moiety commonly referred to as molybdopterin (MPT). Moco is synthesized by an ancient and conserved
biosynthetic pathway that can be divided into four steps, according to the biosynthetic intermediates precursor Z (cyclic
pyranopterin monophosphate), MPT and adenylated MPT. In a fifth step modifications such as attachment of nucleotides, sulfuration
or bond formation between Mo and the protein result in different catalytic Mo centers. A defect in any of the steps of Moco
biosynthesis results in the pleiotropic loss of all Mo enzyme activities. Human Moco deficiency is a hereditary metabolic
disorder characterized by severe neurodegeneration resulting in early childhood death. Recently, a first substitution therapy
was established.
Received 17 June 2005; received after revision 18 August 2005; accepted 1 September 2005 |
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Keywords: | Molybdenum cofactor molybdopterin cyclic pyranopterin monophosphate copper biosynthesis deficiency therapy |
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