Plant Physiology Preview
Published on July 18, 2002; 10.1104/pp.002626
Received January 13, 2002
Returned for revision March 22, 2002
Accepted April 22, 2002
Redox Regulation of Arabidopsis 3-Deoxy-D-arabino-Heptulosonate 7-Phosphate Synthase
Robert Entus , Michael Poling , and Klaus M. Herrmann *
Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907
* Corresponding author; email: herrmann{at}purdue.edu.
The cDNA for 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase of Arabidopsis encodes a polypeptide with an amino-terminal signal sequence for plastid import. A cDNA fragment encoding the processed form of the enzyme was expressed in Escherichia coli. The resulting protein was purified to electrophoretic homogeneity. The enzyme requires Mn2+ and reduced thioredoxin (TRX) for activity. Spinach (Spinacia oleracea) TRX f has an apparent dissociation constant for the enzyme of about 0.2 µM. The corresponding constant for TRX m is orders of magnitude higher. In the absence of TRX, dithiothreitol partially activates the enzyme. Upon alkylation of the enzyme with iodoacetamide, the dependence on a reducing agent is lost. These results indicate that the first enzyme in the shikimate pathway of Arabidopsis appears to be regulated by the ferredoxin/TRX redox control of the chloroplast.
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