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Literature summary for 1.1.1.363 extracted from

  • Naylor, C.E., Gover, S.; Basak, A.K.; Cosgrove, M.S.; Levy, H.R.; Adams, M.J.
    NADP+ and NAD+ binding to the dual coenzyme specific enzyme Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: different interdomain hinge angles are seen in different binary and ternary complexes (2001), Acta Crystallogr. Sect. D, 57, 635-648.
    View publication on PubMed

Crystallization (Commentary)

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

Organism UniProt Comment Textmining
Leuconostoc mesenteroides P11411
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-

Purification (Commentary)

Purification (Comment) Organism
-
Leuconostoc mesenteroides

Synonyms

Synonyms Comment Organism
G6PD
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Leuconostoc mesenteroides

Cofactor

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