1.1.1.292: 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming)

This is an abbreviated version!
For detailed information about 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming), go to the full flat file.

Reaction

1,5-anhydro-D-mannitol
+
NADP+
=
1,5-Anhydro-D-fructose
+
NADPH
+
H+

Synonyms

1,5-anhydro-D-fructose reductase, 1,5-anhydro-D-fructose reductase (ambiguous), AF reductase, AFR, AKR1E1, More, NADPH dependent 1,5-anhydro-D-fructose reductase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.292 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming)

Crystallization

Crystallization on EC 1.1.1.292 - 1,5-anhydro-D-fructose reductase (1,5-anhydro-D-mannitol-forming)

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, enzyme crystallized in complex with the cofactor NADP(H) and its structure is determined to 2.2 A resolution using selenomethionine single-wavelength anomalous dispersion
-
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