MOLYBDENUM COFACTOR BIOSYNTHESIS AND MOLYBDENUM ENZYMES
- 1 June 2006
- journal article
- review article
- Published by Annual Reviews in Annual Review of Plant Biology
- Vol. 57 (1), 623-647
- https://doi.org/10.1146/annurev.arplant.57.032905.105437
Abstract
The molybdenum cofactor (Moco) forms the active site of all eukaryotic molybdenum (Mo) enzymes. Moco consists of molybdenum covalently bound to two sulfur atoms of a unique tricyclic pterin moiety referred to as molybdopterin. Moco is synthesized from GTP by an ancient and conserved biosynthetic pathway that can be divided into four steps involving the biosynthetic intermediates cyclic pyranopterin monophosphate, molybdopterin, and adenylated molybdopterin. In a fifth step, sulfuration or bond formation between Mo and a protein cysteine result in two different catalytic Mo centers. There are four Mo enzymes in plants: (1) nitrate reductase catalyzes the first and rate-limiting step in nitrate assimilation and is structurally similar to the recently identified, (2) peroxisomal sulfite oxidase that detoxifies excessive sulfite. (3) Aldehyde oxidase catalyzes the last step of abscisic acid biosynthesis, and (4) xanthine dehydrogenase is essential for purine degradation and stress response.Keywords
This publication has 135 references indexed in Scilit:
- Molybdenum Cofactor Biosynthesis in Humans: Identification of a Persulfide Group in the Rhodanese-like Domain of MOCS3 by Mass SpectrometryBiochemistry, 2005
- Structure of the molybdopterin-bound Cnx1G domain links molybdenum and copper metabolismNature, 2004
- Mechanistic and Mutational Studies of Escherichia coli Molybdopterin Synthase Clarify the Final Step of Molybdopterin BiosynthesisJournal of Biological Chemistry, 2003
- Thiocarboxylation of Molybdopterin Synthase Provides Evidence for the Mechanism of Dithiolene Formation in Metal-binding PterinsPublished by Elsevier ,2001
- Pre-steady-state Kinetic Analysis of Recombinant Arabidopsis NADH:Nitrate ReductaseJournal of Biological Chemistry, 2001
- A Sulfurtransferase Is Required in the Transfer of Cysteine Sulfur in the in Vitro Synthesis of Molybdopterin from Precursor Z in Escherichia coliJournal of Biological Chemistry, 2001
- Mutation of Human Molybdenum Cofactor Sulfurase Gene Is Responsible for Classical Xanthinuria Type IIBiochemical and Biophysical Research Communications, 2001
- Xanthine Dehydrogenase from Leaves of Leguminous Plants: Purification, Characterization and Properties of the EnzymeJournal of Plant Physiology, 2000
- Spectroscopic and Kinetic Characterization of the Recombinant Cytochrome c Reductase Fragment of Nitrate ReductasePublished by Elsevier ,1997
- Structural Studies on Corn Nitrate Reductase: Refined Structure of the CytochromebReductase Fragment at 2.5 Å, its ADP Complex and an Active-site Mutant and Modeling of the CytochromebDomainJournal of Molecular Biology, 1995