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Characterization of two sulfurtransferase isozymes from Arabidopsis thaliana by Jutta Papenbrock; Ahlert Schmidt is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Sulfurtransferases transfer a sulfane atom from a donor substrate to a thiophilic acceptor molecule. Recently a sulfurtransferase specific for the substrate 3‐mercaptopyruvate was isolated from __Arabidopsis thaliana__[Papenbrock, J. & Schmidt, A. (2000) __Eur. J. Biochem__. **267**, 145–154]. In this study a second sulfurtransferase from __Arabidopsis__ was characterized and compared to the enzyme described previously. Sequences of the mature proteins had an identity of 77.7%. The plant sulfurtransferases formed a distinct group within the known eukaryotic sulfurtransferases. When Southern blots were hybridized with labelled cDNA fragments from each of the plant sulfurtransferases the same pattern of bands was obtained indicating the existence of only these two closely related sulfurtransferases. The new sulfurtransferase was expressed in __Escherichia coli__ fused with an N‐terminal His~6~‐tag, purified and tested for enzyme activity. Like the first enzyme, the newly isolated protein preferred 3‐mercaptopyruvate to thiosulfate as substrate. The __K__~m~ of both enzymes determined for 3‐mercaptopyruvate and cyanide were almost identical. As a result of database searches it became

Who reads Characterization of two sulfurtransferase isozymes from Arabidopsis thaliana?

Author

Jutta Papenbrock; Ahlert Schmidt

Publisher

John Wiley and Sons; Springer; Wiley (Blackwell Publishing); Springer-Verlag; Blackwell Publishing Inc.; Springer Verlag; Wiley; Springer Science and Business Media LLC (ISSN 1432-1327)

Published

2000

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)