Crystallization (Comment) | Organism |
---|---|
cocrystallization of and mutant enzyme Q365, mutant enzymen S215, mutant enzyme S215 with NAD+ and mutant enzyme Q365 with NADP+, hanging-drop vapour diffusion method, structures of NADP+- and NAD+-complexed enzymes are determined at 2.2 and 2.5 A resolution | Leuconostoc mesenteroides |
Organism | UniProt | Comment | Textmining |
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Leuconostoc mesenteroides | P11411 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Leuconostoc mesenteroides |
Synonyms | Comment | Organism |
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G6PD | - |
Leuconostoc mesenteroides |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | the NAD+/enzyme complex is half-open. It is suggested that if NAD+ approaches the open form of the enzyme, and this approach generates a conformation change, initially to the half-open form. The concomitant movement of the coenzyme sheet allows Gln47 to approach the adenine ribose 20-hydroxyl and moves away the side chain of Arg46 | Leuconostoc mesenteroides | |
NADP+ | binds to the furthest open form of the enzyme. Of the residues within the coenzyme domain, only Arg46 moves, interacting with the 20-phosphate and adenine. NAD+ is less well defined in the binding site | Leuconostoc mesenteroides |