95014-75-8Relevant articles and documents
Cadmium(II)-stimulated enzyme activation of Arabidopsis thaliana phytochelatin synthase 1
Ogawa, Shinya,Yoshidomi, Takahiro,Yoshimura, Etsuro
, p. 111 - 117 (2011)
Phytochelatin (PC), a class of heavy metal-binding peptides, is synthesized from the tripeptide glutathione (GSH) and/or previously synthesized PC in a reaction mediated by PC synthase (PCS). In the present study, the PC production rate catalyzed by recombinant Arabidopsis PCS1 (rAtPCS1) in the presence of a constant free Cd(II) level increased steadily and the kinetic parameters were approximated using a substituted-enzyme mechanism in which GSH and bis(glutathionato)cadmium acted as co-substrates. In contrast, the PC production rate as a function of GSH concentration at a constant total Cd(II) concentration reached a maximum, which shifted toward higher GSH concentrations as the concentration of Cd(II) was increased. These observations are consistent with the suggestion that rAtPCS1 possesses a Cd(II) binding site where Cd(II) binds to activate the enzyme. The affinity constant, optimized using a one-site mathematical model, successfully simulated the experimental data for the assay system using lower concentrations of Cd(II) (5 or 10 μM) but not for the assay using higher concentrations (50 or 500 μM), where a sigmoidal increase in PCS activity was evident. Furthermore, the PCS activity determined at a constant GSH concentration as a function of Cd(II) concentration also reached a maximum. These findings demonstrate that rAtPCS1 also possesses a second Cd(II) binding site where Cd(II) binds to induce an inhibitory effect. A two-site mathematical model was applied successfully to account for the observed phenomena, supporting the suggestion that rAtPCS1 possesses two Cd(II) binding sites.
Conversion of Glutathione into Cadystins and Their Analogs Catalyzed by Carboxypeptidase Y
Imai, Kunio,Obata, Hitoshi,Shimizu, Keisuke,Komiya, Takashi
, p. 1193 - 1194 (2007/10/03)
Cadystins induced in a fission yeast treated with Cd2+ are the higher homologs of glutathione. In the present work, glutathione was incubated with Carboxypeptidase Y at a high substrate concentration. The reaction afforded not only the degraded product, but also cadystins and their analogs. A possible transformation pathway for glutathione by this enzyme is proposed.
Amino acids and peptides. XXVII. Synthesis of phytochelatin-related peptides and examination of their heavy metal-binding properties
Matsumoto,Okada,Min,Onosaka,Tanaka
, p. 2364 - 2368 (2007/10/02)
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