title: Purification and characterization of dipeptidase hydrolyzing L-cysteinylglycine from radish cotyledon.
abstract: 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.
authors: Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto, Japan.
authors: Henri-Obadja
authors: HO
authors: Kumada
authors: Yukio
authors: Y
authors: Koizumi
authors: Jiro
authors: J
authors: Sekiya
mesh_terms: 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
chemical_list: D004151:Dipeptides; D010940:Plant Proteins; C028505:cysteinylglycine; D004150:Dipeptidases; C038937:dipeptidase