By Walker D.
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Close to the FBP molecule. In the oxidised inactive enzyme the position of the glutamate is occupied by the side chain of a valine residue. As this amino acid is not charged, it is believed that the catalytic Mg2+ ion cannot bind rendering the enzyme inactive. The proposed mechanism for activation of the enzyme suggests that upon reduction, the loop containing the regulatory sequence is relaxed, allowing two critical (5 strands, linking the regulatory loop to the active site region, to move outwards.
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Natl. Acad. Sci. USA (in press). , Marion, D. P. (2000) NMR structures of thioredoxin m from green alga Chlamydomonas reinhardtii. Proteins, 41, 334-349. , Labarre, J. B. (1999) A new antioxidant with alkyl hydroperoxide defense properties in yeast. /. Biol. , 274, 4537-4544. H. L. (2000) Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase. Science, 289, 1190-1194. P. etal. (1997) High-yield expression of pea thioredoxin m and assessment of its efficiency in chloroplast fructose-1,6-bisphosphatase activation.