Worms take the 'phyto' out of 'phytochelatins'

Trends Biotechnol. 2002 Feb;20(2):61-4. doi: 10.1016/s0167-7799(01)01873-x.

Abstract

Phytochelatin synthase is the enzyme responsible for the synthesis of heavy-metal-binding peptides (phytochelatins) from glutathione and related thiols. It has recently been determined that it is not only restricted to plants and some fungi, as was once thought, but also has an essential role in heavy-metal detoxification in the model nematode Caenorhabditis elegans. These findings and others that demonstrate phytochelatin synthase-coding sequences in the genomes of several other invertebrates, including pathogenic nematodes, schistosomes and roundworms, herald a new era in phytochelatin research, in which these novel post-translationally synthesized peptides will not only be investigated in the context of phytoremediation but also from a clinical parasitological standpoint.

Publication types

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

MeSH terms

  • Aminoacyltransferases / genetics
  • Aminoacyltransferases / metabolism*
  • Animals
  • Antidotes / metabolism
  • Caenorhabditis / enzymology
  • Caenorhabditis / genetics
  • Glutathione
  • Inactivation, Metabolic / physiology
  • Metalloproteins / biosynthesis
  • Metalloproteins / metabolism*
  • Metals, Heavy / metabolism*
  • Models, Animal
  • Osmosis
  • Phytochelatins
  • Schistosoma / enzymology
  • Schistosoma / genetics
  • Schistosoma / parasitology

Substances

  • Antidotes
  • Metalloproteins
  • Metals, Heavy
  • Phytochelatins
  • Aminoacyltransferases
  • glutathione gamma-glutamylcysteinyltransferase
  • Glutathione