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Plastidic P2 glucose-6P dehydrogenase from poplar is modulated by thioredoxin m-type: Distinct roles of cysteine residues in redox regulation and NADPH inhibition

Academic Article
Publication Date:
2016
abstract:
A cDNA coding for a plastidic P2-type G6PDH isoform from poplar (Populus tremula x tremuloides) has been used to express and purify to homogeneity the mature recombinant protein with a N-terminus His-tag. The study of the kinetic properties of the recombinant enzyme showed an in vitro redox sensing modulation exerted by reduced DTT. The interaction with thioredoxins (TRX5) was then investigated.
Iris type:
01.01 Articolo in rivista
Keywords:
Cysteine; Oxidative pentose phosphate pathway; Populus; Thioredoxins
List of contributors:
Castiglia, Daniela
Authors of the University:
CASTIGLIA DANIELA
Handle:
https://iris.cnr.it/handle/20.500.14243/443100
Published in:
PLANT SCIENCE (LIMERICK)
Journal
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