Conversion of glutathione into cadystins and their analogs catalyzed by carboxypeptidase Y.
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.
Imai
K
K
School of Bio-resources, Mie University, Japan.
Obata
H
H
Shimizu
K
K
Komiya
T
T
D000595:Amino Acid Sequence; D002104:Cadmium / Q000378:metabolism* / Q000494:pharmacology; D002268:Carboxypeptidases / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D043402:Cathepsin A; D002851:Chromatography, High Pressure Liquid; D005656:Fungal Proteins / Q000378:metabolism*; D005978:Glutathione / Q000378:metabolism*; D047908:Intracellular Signaling Peptides and Proteins; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012568:Schizosaccharomyces / Q000201:enzymology*; D029702:Schizosaccharomyces pombe Proteins; D013056:Spectrophotometry, Ultraviolet
D002352:Carrier Proteins; D005656:Fungal Proteins; D047908:Intracellular Signaling Peptides and Proteins; D029702:Schizosaccharomyces pombe Proteins; D002104:Cadmium; C055088:cadystin protein, S pombe; D002268:Carboxypeptidases; D043402:Cathepsin A; D005978:Glutathione