Phytochelatins, the heavy-metal-binding peptides of plants, are synthesized from glutathione by a specific gamma-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase).

An enzyme has been discovered and characterized from Silene cucubalus cell suspension cultures that catalyzes the transfer of the gamma-glutamylcysteine dipeptide moiety of glutathione to an acceptor glutathione molecule or a growing chain of [Glu(-Cys)](n)-Gly oligomers, thus synthesizing phytochelatins, the metal-binding peptides of higher plants and select fungi. The enzyme was named gamma-glutamylcysteine dipeptidyl transpeptidase and given the trivial name phytochelatin synthase. The primary reaction catalyzed is [Glu(-Cys)]-Gly + [Glu(-Cys)](n)-Gly --> [Glu(-Cys)](n+1)-Gly + Gly. The enzyme is isoelectric near pH 4.8 and has temperature and pH optima at 35 degrees C and 7.9, respectively. Phytochelatin synthase is constitutively present in cell cultures of various plant species and its formation is not noticeably induced by heavy metal ions in the growth medium. The enzyme (M(r)95,000) seems to be composed of four subunits, the dimer (M(r)50,000) being also catalytically active. Cd(2+) is by far the best metal activator of the enzyme followed by Ag(+), Bi(3+), Pb(2+), Zn(2+), Cu(2+), Hg(2+), and Au(+). The K(m) for glutathione is 6.7 mM. The enzyme activity seems to be self-regulated in that the product of the reaction (the phytochelatins) chelates the enzyme-activating metal, thus terminating the enzyme reaction. The molar ratio of the gamma-glutamylcysteine dipeptide in phytochelatin to Cd(2+) in the newly formed complex was 2:1.