Cd2+ activates the enzyme. Extremely efficient alternative cadmium sequestration pathways in leaves of cadmium hyperaccumulators prevent activation of phytochelatin synthase by cadmium ions
the enzyme possesses two Cd2+ binding sites, Cd2+ binds to one of these sites to activate the enzyme. In the presence of 0.01 mM Cd2+, activity increases and reaches the maximum rate with an increase in GSH concentration up to 15 mM
activates the enzyme at 0.036-0.36 mM about 4-9fold. PCS activation is self-regulated, because its product poly(4-glutamyl-cysteinyl)glycine chelates Cd2+, and the reaction stops when free Cd2+ ions are no longer available. Cd2+ also activates the enzymes peptidase activity. Presence of PC2, PC3, and PC4 oligomers is evident in extracts from gametophytes exposed to Cd2+ for 7 days, determined by HPLC-ESI-MS-MS analysis
Cd2+ activates the enzyme. Extremely efficient alternative cadmium sequestration pathways in leaves of cadmium hyperaccumulators prevent activation of phytochelatin synthase by cadmium ions
neither in vivo nor in vitro exposure to Zn2+ results in PCS activation, while Fe(II)/(III) and Cd2+ are able to activate enzyme PCS in vitro, as well as to induce phytochelatin (PC) accumulation in vivo. The enzyme activity depends on divalent cations, overview
2.3.2.15 glutathione gamma-glutamylcysteinyltransferase
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