Bacterial molybdoenzymes: old enzymes for new purposes

FEMS Microbiol Rev. 2016 Jan;40(1):1-18. doi: 10.1093/femsre/fuv043. Epub 2015 Oct 13.

Abstract

Molybdoenzymes are widespread in eukaryotic and prokaryotic organisms where they play crucial functions in detoxification reactions in the metabolism of humans and bacteria, in nitrate assimilation in plants and in anaerobic respiration in bacteria. To be fully active, these enzymes require complex molybdenum-containing cofactors, which are inserted into the apoenzymes after folding. For almost all the bacterial molybdoenzymes, molybdenum cofactor insertion requires the involvement of specific chaperones. In this review, an overview on the molybdenum cofactor biosynthetic pathway is given together with the role of specific chaperones dedicated for molybdenum cofactor insertion and maturation. Many bacteria are involved in geochemical cycles on earth and therefore have an environmental impact. The roles of molybdoenzymes in bioremediation and for environmental applications are presented.

Keywords: TorD family; XdhC; bioremediation; molybdenum cofactor; molybdoenzyme maturation; specific chaperons.

Publication types

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

MeSH terms

  • Apoenzymes / metabolism*
  • Bacteria / enzymology*
  • Bacterial Proteins / metabolism*
  • Coenzymes / biosynthesis*
  • Coenzymes / metabolism
  • Environmental Microbiology
  • Metalloproteins / biosynthesis*
  • Metalloproteins / metabolism
  • Molecular Chaperones / metabolism*
  • Molybdenum Cofactors
  • Pteridines / metabolism

Substances

  • Apoenzymes
  • Bacterial Proteins
  • Coenzymes
  • Metalloproteins
  • Molecular Chaperones
  • Molybdenum Cofactors
  • Pteridines
  • molybdenum cofactor