Degradation of glutathione S-conjugates by a carboxypeptidase in the plant vacuole

Wolf AE, Dietz K-J, Schröder P (1996)
FEBS Letters 384(1): 31-34.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
For plants, glutathione conjugation is a major pathway to detoxify organic xenobiotic. Glutathione S-conjugates (SG-conjugates) are formed in the cytosol, the in vitro transport over the tonoplast has been described and a final storage in the vacuole has been postulated. We show here that alachlor rapidly accumulates as GS-conjugates in the plant vacuole and that the first step of its degradation, the formation of the respective gamma-glutamylcysteinyl-S-conjugate, is catalyzed by a vacuolar carboxypeptidase, These results suggest the glutathione conjugate as a transport form but not a storage form of xenobiotic molecules.
Erscheinungsjahr
Zeitschriftentitel
FEBS Letters
Band
384
Zeitschriftennummer
1
Seite
31-34
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Wolf AE, Dietz K-J, Schröder P. Degradation of glutathione S-conjugates by a carboxypeptidase in the plant vacuole. FEBS Letters. 1996;384(1):31-34.
Wolf, A. E., Dietz, K. - J., & Schröder, P. (1996). Degradation of glutathione S-conjugates by a carboxypeptidase in the plant vacuole. FEBS Letters, 384(1), 31-34. doi:10.1016/0014-5793(96)00272-4
Wolf, A. E., Dietz, K. - J., and Schröder, P. (1996). Degradation of glutathione S-conjugates by a carboxypeptidase in the plant vacuole. FEBS Letters 384, 31-34.
Wolf, A.E., Dietz, K.-J., & Schröder, P., 1996. Degradation of glutathione S-conjugates by a carboxypeptidase in the plant vacuole. FEBS Letters, 384(1), p 31-34.
A.E. Wolf, K.-J. Dietz, and P. Schröder, “Degradation of glutathione S-conjugates by a carboxypeptidase in the plant vacuole”, FEBS Letters, vol. 384, 1996, pp. 31-34.
Wolf, A.E., Dietz, K.-J., Schröder, P.: Degradation of glutathione S-conjugates by a carboxypeptidase in the plant vacuole. FEBS Letters. 384, 31-34 (1996).
Wolf, A. E., Dietz, Karl-Josef, and Schröder, P. “Degradation of glutathione S-conjugates by a carboxypeptidase in the plant vacuole”. FEBS Letters 384.1 (1996): 31-34.

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