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Literature summary for 1.1.1.292 extracted from

  • Schu, M.; Faust, A.; Stosik, B.; Kohring, G.W.; Giffhorn, F.; Scheidig, A.J.
    The structure of substrate-free 1,5-anhydro-D-fructose reductase from Sinorhizobium meliloti 1021 reveals an open enzyme conformation (2013), Acta Crystallogr. Sect. F, 69, 844-849.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expresssion in Escherichia coli Sinorhizobium meliloti

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with NADP(H), to 1.93 A resolution. The structure displays an empty substrate-binding, showing an open conformation of the enzyme state shortly after the release of product, presumably with bound oxidized cofactor NADP+. Amino-acid residues Lys94, His151, Trp162, Arg163, Asp176 and His180 are involved in substrate binding, catalysis or product release. The side chain of Lys94 may function as a molecular switch Sinorhizobium meliloti

Organism

Organism UniProt Comment Textmining
Sinorhizobium meliloti Q92KZ3
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