Thioredoxin regulates G6PDH activity by changing redox states of OpcA in the nitrogen-fixing cyanobacterium

Autor: Shoko, Mihara, Hitomi, Wakao, Keisuke, Yoshida, Akiyoshi, Higo, Kazunori, Sugiura, Akihiro, Tsuchiya, Jiro, Nomata, Ken-Ichi, Wakabayashi, Toru, Hisabori
Rok vydání: 2017
Předmět:
Zdroj: The Biochemical journal. 475(6)
ISSN: 1470-8728
Popis: Glucose 6-phosphate dehydrogenase (G6PDH) catalyzes the first reaction in the oxidative pentose phosphate pathway. In green plant chloroplasts, G6PDH is a unique redox-regulated enzyme, since it is inactivated under the reducing conditions. This regulation is accomplished using a redox-active cysteine pair, which is conserved in plant G6PDH. The inactivation of this enzyme under conditions of light must be beneficial to prevent release of CO
Databáze: OpenAIRE