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Wetzel, A. ; Sandermann, H.J.

Plant biochemistry of xenobiotics: Isolation and characterization of a soybean O-glucosyltransferase of DDT metabolism.

Arch. Biochem. Biophys. 314, 323-328 (1994)
DOI PMC
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
The insecticide DDT is metabolized in soybean and wheat cell cultures to the acylglucoside of 2,2-bis-(4-chlorophenyl)-acetic acid (DDA) (M. Arjmand and H. Sandermann, 1985, Pesticide Biochem. Physiol. 23, 389-397). An enzyme catalyzing the conjugation reaction has been highly purified from the soluble enzyme fraction of cultured soybean cells. After the initial ammonium sulfate fractionation, quercetin and pentachlorophenol were preferentially glucosylated. In the course of 367-fold purification, DDA became the preferred substrate. The purified enzyme was unstable. A molecular weight of ~50 kDa was estimated for the native enzyme (gel permeation chromatography) as well as the denatured protein (sodium dodecyl sulfate-gel electrophoresis). The isoelectric point for the enzyme was near pH 4.9. Apparent K(m) values of about 170 μM were determined for UDP-glucose as well as DDA. The maximal velocity was 257 μkat/kg protein, corresponding to a conjugation capacity of 855 μg DDA/h/g fresh weight of cells.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter Dda, 2,2-bis-(4-chlorophenyl)-acetic Acid ; Ddt, 1,1,1-trich-loro-2,2,-(bis-4-cholorphenyl)-ethane ; Enzyme Evolution ; O-glucosyltransferase ; Soybean (glycine Max L.) Cell Cultures
ISSN (print) / ISBN 0003-9861
e-ISSN 1096-0384
Zeitschrift Archives of Biochemistry and Biophysics
Quellenangaben Band: 314, Heft: 2, Seiten: 323-328 Artikelnummer: , Supplement: ,
Verlag Elsevier
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Biochemical Plant Pathology (BIOP)