Cellular and Molecular Life Sciences CMLS

, Volume 62, Issue 23, pp 2792–2810

Molybdenum cofactor biosynthesis and deficiency


DOI: 10.1007/s00018-005-5269-y

Cite this article as:
Schwarz, G. Cell. Mol. Life Sci. (2005) 62: 2792. doi:10.1007/s00018-005-5269-y


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.

Key words.

Molybdenum cofactormolybdopterincyclic pyranopterin monophosphatecopperbiosynthesisdeficiencytherapy

Copyright information

© Birkhäuser Verlag, Basel 2005

Authors and Affiliations

  1. 1.Institute of Plant BiologyTechnical University BraunschweigBraunschweigGermany
  2. 2.Institute of BiochemistryUniversity of CologneKölnGermany