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Literature summary 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)

EC Number Cloned (Comment) Organism
1.1.1.263 expression in Escherichia coli Sinorhizobium meliloti
1.1.1.292 expresssion in Escherichia coli Sinorhizobium meliloti

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.263 to 1.93 A resolution. The structure displays an empty substrate-binding site in an open conformation reflecting 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 seems to function as a molecular switch Sinorhizobium meliloti
1.1.1.292 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

EC Number Organism UniProt Comment Textmining
1.1.1.263 Sinorhizobium meliloti Q92KZ3
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1.1.1.292 Sinorhizobium meliloti Q92KZ3
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