Phytochelatins are oligomers of glutathione, produced by the enzyme phytochelatin synthase. They are found in plants, fungi, nematodes and all groups of algae including cyanobacteria. Phytochelatins act as chelators, and are important for heavy metal detoxification. They are abbreviated PC2 through PC1.
A mutant Arabidopsis thaliana lacking phytochelatin synthase is very sensitive to cadmium, but it grows just as well as the wild-type plant at normal concentrations of zinc and copper, two essential metal ions, indicating that phytochelatin is only involved in resistance to metal poisoning.
Because phytochelatin synthase uses glutathione with a blocked thiol group in the synthesis of phytochelatin, the presence of heavy metal ions that bind to glutathione causes the enzyme to work faster. Therefore, the amount of phytochelatin increases when the cell needs more phytochelatin to survive in an environment with high concentrations of metal ions.
|Type||Structure||Has been found in||Precursor|
|Desglycine phytochelatin||(γGlu-Cys)n||maize, yeasts|
Phytochelatin was first discovered in 1981 in fission yeast, and was named cadystin. It was then found in higher plants in 1985 and was named phytochelatin. In 1989 its enzyme, phytochelatin synthase, was discovered.
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- InterPro database page on phytochelatin synthase
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- Kondo, Naoto; Imai, Kunio; Isobe, Minoru; Goto, Toshio; Murasugi, Akira; Wada-Nakagawa, Chiaki; Hayashi, Yukimasa (1984). "Cadystin A and B, Major Unit Peptides Comprising Cadmium Binding Peptides Induced in a Fission Yeast----Separation, Revision of Structures and Synthesis". Tetrahedron Lett. 25: 3869–3872. doi:10.1016/S0040-4039(01)91190-6.