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Plastidic glucose-6-phosphate dehydrogenases are regulated to maintain activity in the light

Journal Article · · Biochemical Journal
DOI:https://doi.org/10.1042/BCJ20190234· OSTI ID:1607897
 [1];  [2];  [2];  [2]
  1. Michigan State Univ., East Lansing, MI (United States); MSU DOE Plant Research Laboratory
  2. Michigan State Univ., East Lansing, MI (United States)

Glucose-6-phosphate dehydrogenase (G6PDH) can initiate the glucose-6-phosphate (G6P) shunt around the Calvin–Benson cycle. To understand the regulation of flux through this pathway, we have characterized the biochemical parameters and redox regulation of the three functional plastidic isoforms of Arabidopsis G6PDH. When purified, recombinant proteins were measured, all three exhibited significant substrate inhibition by G6P but not NADP+, making the determination of enzyme kinetic parameters complex. We found that the half-saturation concentration of G6PDH isoform 1 is increased under reducing conditions. The other two isoforms exhibit less redox regulation, however, isoform 2 is strongly inhibited by NADPH. Redox regulation of G6PDH1 can be partially reversed by hydrogen peroxide or protected against by the presence of its substrate, G6P. Finally, our results support the conclusion that G6PDH can have significant activity throughout the day and can be dynamically regulated to allow or prevent flux through the glucose-6-phosphate shunt.

Research Organization:
Michigan State Univ., East Lansing, MI (United States). MSU-DOE Plant Research Laboratory
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Grant/Contract Number:
FG02-91ER20021; SC0007101
OSTI ID:
1607897
Journal Information:
Biochemical Journal, Journal Name: Biochemical Journal Journal Issue: 10 Vol. 476; ISSN 0264-6021
Publisher:
Biochemical SocietyCopyright Statement
Country of Publication:
United States
Language:
English

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Cited By (1)