Molybdenum cofactor and human disease.

Guenter Schwarz

Journal: Current opinion in chemical biology 2017;31():179-87

PMID: 27055119

Full Text on Elsevier Science View on PubMed

Abstract

Four molybdenum-dependent enzymes are known in humans, each harboring a pterin-based molybdenum cofactor (Moco) in the active site. They catalyze redox reactions using water as oxygen acceptor or donator. Moco is synthesized by a conserved biosynthetic pathway. Moco deficiency results in a severe inborn error of metabolism causing often early childhood death. Disease-causing symptoms mainly go back to the lack of sulfite oxidase (SO) activity, an enzyme in cysteine catabolism. Besides their name-giving functions, Mo-enzymes have been recognized to catalyze novel reactions, including the reduction of nitrite to nitric oxide. In this review we cover the biosynthesis of Moco, key features of Moco-enzymes and focus on their deficiency. Underlying disease mechanisms as well as treatment options will be discussed.

Address: Institute of Biochemistry, Department of Chemistry and Center for Molecular Medicine Cologne and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases, University of Cologne, Zuelpicher Str. 47, 50674 Koeln, Germany. Electronic address: [email protected].

DOI: 10.1016/j.cbpa.2016.03.016

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MeSH Terms: Coenzymes, Cysteine, Cytosol, Disease, Humans, Metalloproteins, Mitochondria, Molybdenum Cofactors, Pteridines, Sulfites, Therapeutics