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.

To get started: Click the edit this page tab at the top. Save the page after each step, then edit it again. show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page. Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc. More help: Help:Editing

Glucose-6-Phosphate Dehydrogenase from Leuconostoc mesenteroides

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol to the rescue. Function It 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 because it produces a cofactor 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 We will keep the interactivity that exist on the page: a box can be checked to observe the different structures conserved evolutionary. 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 (dimer of two identical monomers). 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. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.