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Our website will not work 5 />Please update to a newer version or download a new web browser, such as Chrome or 5 />The GPD1 protein was expressed in Escherichia coli, and purified as a fusion protein w.
Homo sapiens L-alpha-glycerol-3-phosphate dehydrogenase https://chmall.ru/100/internet-ip-kamera-s-oblachnim-servisom-trassir-tr-d7121ir1w.html GPD1 catalyzes the reversible biological conversion of dihydroxyacetone DHAP 5 glycerol-3-phosphate.
The GPD1 protein was expressed in Escherichia coli, and purified as https://chmall.ru/100/akkumulyatornaya-drel-shurupovert-dwt-abs-96.html fusion 5 with glutathione S-transferase.
Here we report the apoenzyme structure of GPD1 determined by multiwavelength anomalous diffraction phasing, and other complex structures with small molecules NAD+ and DHAP by the molecular replacement method.
This enzyme structure 5 organized into two distinct domains, the N-terminal eight-stranded beta-sheet sandwich domain and the C-terminal helical substrate-binding domain.
An electrophilic catalytic mechanism by the epsilon-NH3+ group of Lys204 is proposed on the basis of the structural analyses.
In 5, the inhibitory effects of zinc and sulfate on GPDHs are assayed and discussed.
Organizational Affiliation: National Laboratory of Biomacromolecules, Institute of Biophysics 5Chinese Academy 5 Sciences, Beijing 100101, China.