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FBP2 — TXN

Text-mined interactions from Literome

Collin et al., Plant Physiol 2004 : Both Trx y were poor activators of fructose-1,6-bisphosphatase and NADP-MDH ; however, a detailed study of the activation of NADP-MDH using site directed mutants of its regulatory cysteines suggested that Trx y was able to reduce the less negative regulatory disulfide but not the more negative regulatory disulfide
Corley et al., Biochem Biophys Res Commun 1983 : The activation of chloroplast fructose-1,6-bisphosphatase by fructose-1,6-bisphosphate, Ca2+, DTT and chloroplast thioredoxin-f is prevented by either spermidine or spermine ; on the contrary, other amino compounds do not replace polyamines in this reversible effect
Häberlein et al., Biochim Biophys Acta 1995 : Obviously, physiologically relevant investigations of the thioredoxin dependent regulation of fructose 1,6-bisphosphatase activity can only be performed in homologous enzyme-thioredoxin combinations
Geck et al., J Biol Chem 1996 : Kinetics of activation of oxidized recombinant sorghum leaf NADP dependent malate dehydrogenase and oxidized spinach chloroplastic fructose-1,6-bisphosphatase by wild-type Trx f, wild-type Trx m, and Trx f mutants were compared