The molybdenum cofactor

J Biol Chem. 2013 May 10;288(19):13165-72. doi: 10.1074/jbc.R113.455311. Epub 2013 Mar 28.

Abstract

The transition element molybdenum needs to be complexed by a special cofactor to gain catalytic activity. Molybdenum is bound to a unique pterin, thus forming the molybdenum cofactor (Moco), which, in different variants, is the active compound at the catalytic site of all molybdenum-containing enzymes in nature, except bacterial molybdenum nitrogenase. The biosynthesis of Moco involves the complex interaction of six proteins and is a process of four steps, which also require iron, ATP, and copper. After its synthesis, Moco is distributed, involving Moco-binding proteins. A deficiency in the biosynthesis of Moco has lethal consequences for the respective organisms.

Keywords: Iron; Metalloenzymes; Metalloproteins; Metals; Molybdenum.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Biosynthetic Pathways
  • Coenzymes / biosynthesis*
  • Coenzymes / chemistry
  • Humans
  • Metalloexopeptidases
  • Metalloproteins / biosynthesis*
  • Metalloproteins / chemistry
  • Metalloproteins / metabolism
  • Molybdenum / chemistry
  • Molybdenum / metabolism*
  • Organophosphorus Compounds / metabolism
  • Pteridines / chemistry
  • Pterins / metabolism

Substances

  • Coenzymes
  • Metalloproteins
  • Organophosphorus Compounds
  • Pteridines
  • Pterins
  • cyclic pyranopterin monophosphate
  • Molybdenum
  • molybdenum cofactor
  • Metalloexopeptidases