Sandbox Reserved 1094: Difference between revisions

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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.

== ~~Disease~~ ==

== Genomic context ==

It is coded by the G6PD gene (1461 nucleotides).

== ~~Relevance~~ ==

== 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 <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

Sandbox Reserved 1094: Difference between revisions

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@@ Line 9: / Line 9: @@
 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.
-== Disease ==
+== Genomic context ==
+It is coded by the G6PD gene (1461 nucleotides).
-== Relevance ==
+== 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 <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.