Purification and Characterization of Dipeptidase Hydrolyzing <small>L</small>-Cysteinylglycine from Radish Cotyledon

Henri-Obadja KUMADA; Yukio KOIZUMI; Jiro SEKIYA

doi:10.1271/bbb.70443

This article has now been updated. Please use the final version.

Purification and Characterization of Dipeptidase Hydrolyzing L-Cysteinylglycine from Radish Cotyledon

Henri-Obadja KUMADA, Yukio KOIZUMI, Jiro SEKIYA

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Keywords: L-cysteinylglycine, dipeptidase, glutathione catabolism, radish, Raphanus sativus L.

JOURNAL FREE ACCESS Advance online publication

Article ID: 70443

DOI https://doi.org/10.1271/bbb.70443

The final version of this article is now available: Vol. 71 (2007) , No. 12 p.3102

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Abstract

Dipeptidase activity was detected in the soluble fraction of radish (Raphanus sativus L.) cotyledon, and the purified enzyme had a specific activity of 7.3 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.

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