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Purification and characterization of dipeptidase hydrolyzing L-cysteinylglycine from radish cotyledon
Henri-Obadja Kumada1, Yukio Koizumi, Jiro Sekiya
1Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto, Japan.
Bioscience, Biotechnology, and Biochemistry
|December 12, 2007
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.
