| Literature DB >> 23539623 |
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.Entities:
Keywords: Iron; Metalloenzymes; Metalloproteins; Metals; Molybdenum
Mesh:
Substances:
Year: 2013 PMID: 23539623 PMCID: PMC3650355 DOI: 10.1074/jbc.R113.455311
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157