Article

Redox regulation of Arabidopsis 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase.

Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907, USA.
Plant physiology (Impact Factor: 6.56). 09/2002; 129(4):1866-71. DOI: 10.1104/pp.002626
Source: PubMed

ABSTRACT 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 Mn(2+) and reduced thioredoxin (TRX) for activity. Spinach (Spinacia oleracea) TRX f has an apparent dissociation constant for the enzyme of about 0.2 microM. 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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