Sandbox Reserved 1094: Difference between revisions
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Loana Prost (talk | contribs) No edit summary |
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KM=8.0 µM for NADP, KM=160 µM for 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. | Its regulation depends on the concentration of substrate and coenzyme, rate limiting step in pentose phosphate pathway<ref>PMID: 12033926</ref>. | ||
== Optimal activity conditions == | == Optimal activity conditions == | ||
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== Structural highlights == | == Structural highlights == | ||
It is formed of a homodimer, so a dimer of two identical monomers. Each monomer is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/1'>1 red and 1 green.</scene> | It is formed of a homodimer, so a dimer of two identical monomers<ref>PMID: 7881907</ref>. Each monomer is composed of 2 domains, <scene name='82/829347/Homodimer_g6pd/1'>1 red and 1 green.</scene> | ||
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. | 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. | ||
