Sandbox Reserved 1094

This Sandbox is Reserved from 25/11/2019, through 30/9/2020 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1091 through Sandbox Reserved 1115.

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Glucose-6-Phosphate Dehydrogenase from Leuconostoc mesenteroides

The protein Glycose-6-Phosphate Dehydrogenase is an enzyme involved in the metabolic pathways of the majority of organisms. Leuconostoc mesenteroides is a Bacilli Gram-positive bacterium that expresses this enzyme.

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function The Glucose-6-Phosphate Dehydrogenase is involved in the processing of carbohydrates as it has important roles in the glucose metabolic process (glycolysis and pentose phosphate pathway). It also has a role in protecting cells from destruction as it produces the co-factor NADPH which plays a role in protecting cells from reactive oxygen species . Genomic context It is coded by the G6PD gene (1461 nucleotides). Catalytic activity D-glucose 6-phosphate + NAD+ → 6-phospho-D-glucono-1,5-lactone + H+ + NADH KM=114 µM for G6PD (with NADP), KM=69 µM for G6PD (with NAD), KM=8.0 µM for NADP, KM=160 µM for NAD. Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway. Optimal activity conditions Optimum pH is 5.4 - 8.9. Evolutionary conservation The different structures conserved evolutionary can be observed according to the scale following. Check, as determined by ConSurfDB. Mutations Mutagenesis inducing catalytic activity loss: +200 mutations have been identified. A change of amino acids leads to disruption of the normal structure/function/reduce the expression of enzymes. Structural highlights It is formed of a homodimer, so a dimer of two identical monomers. Each monomer is composed of 2 domains, 1 red and 1 green. Depending on several conditions, it can dimerize to form tetramers. Each monomer in the complex has a substrate binding site that binds to G6P, and a catalytic coenzyme binding site that binds to NADP+/NADPH using the Rossman fold. This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein.

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