Purification and characterization of dipeptidase hydrolyzing L-cysteinylglycine from radish cotyledon.
Dipeptidase activity was detected in the soluble fraction of radish (Raphanus sativus L.) cotyledon, and the purified enzyme had a specific activity of 7.32 nkat/mg protein for hydrolyzing L-cysteinylglycine. The dipeptidase was found to be a hexameric metalloenzyme, composed of homological 55 kDa-subunits. This is the first glutathione catabolism-related dipeptidase isolated from higher plants.
Kumada
Henri-Obadja
HO
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto, Japan.
Koizumi
Yukio
Y
Sekiya
Jiro
J
D018548:Cotyledon / Q000201:enzymology*; D004150:Dipeptidases / Q000302:isolation & purification / Q000378:metabolism*; D004151:Dipeptides / Q000378:metabolism*; D006868:Hydrolysis; D010940:Plant Proteins / Q000302:isolation & purification / Q000378:metabolism*; D031224:Raphanus / Q000201:enzymology*; D013237:Stereoisomerism
D004151:Dipeptides; D010940:Plant Proteins; C028505:cysteinylglycine; D004150:Dipeptidases; C038937:dipeptidase