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Literature summary extracted from

  • Dambe, T.R.; Kuehn, A.M.; Brossette, T.; Giffhorn, F.; Scheidig, A.J.
    Crystal structure of NADP(H)-dependent 1,5-anhydro-D-fructose reductase from Sinorhizobium morelense at 2.2 A resolution: construction of a NADH-accepting mutant and its application in rare sugar synthesis (2006), Biochemistry, 45, 10030-10042.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.263 expressed in Escherichia coli Ensifer adhaerens
1.1.1.292 expression in Escherichia coli Ensifer adhaerens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.263 hanging-drop vapour diffusion Ensifer adhaerens
1.1.1.292 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 Ensifer adhaerens

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.263 A13G decreased activity Ensifer adhaerens
1.1.1.263 A13G/S10G decreased activity Ensifer adhaerens
1.1.1.263 A13G/S33D increased activity Ensifer adhaerens
1.1.1.263 D176A decreased activity Ensifer adhaerens
1.1.1.263 G206I decreased activity Ensifer adhaerens
1.1.1.263 H180A decreased activity Ensifer adhaerens
1.1.1.263 K94G decreased activity Ensifer adhaerens
1.1.1.263 S10G increased activity Ensifer adhaerens
1.1.1.263 S33D decreased activity Ensifer adhaerens
1.1.1.292 A13G kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 1.8fold higher than wild type value. Mutant enzyme shows activity with NADH as cofactor Ensifer adhaerens
1.1.1.292 G206I kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 1.4fold lower than wild type value Ensifer adhaerens
1.1.1.292 H180A kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 61.9fold lower than wild type value Ensifer adhaerens
1.1.1.292 K94G kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 137fold lower than wild type value Ensifer adhaerens
1.1.1.292 S10G kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 1.3fold higher than wild type value Ensifer adhaerens
1.1.1.292 S10G/A13G kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 2fold higher than wild type value. Mutant enzyme shows activity with NADH as cofactor Ensifer adhaerens
1.1.1.292 S176A kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 1001fold lower than wild type value Ensifer adhaerens
1.1.1.292 S33D no activity Ensifer adhaerens
1.1.1.292 S33D/A13G kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 84fold lower than wild type value. Mutant enzyme shows activity with NADH as cofactor Ensifer adhaerens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.263 0.02
-
 NADPH mutant A13G in the presence of 1,5-anhydro-D-fructose Ensifer adhaerens
1.1.1.263 0.06
-
 NADPH mutant G206I in the presence of 1,5-anhydro-D-fructose Ensifer adhaerens
1.1.1.263 0.06
-
 NADPH recombinant wild type enzyme in the presence of 1,5-anhydro-D-fructose Ensifer adhaerens
1.1.1.263 0.1
-
 NADPH native wild type enzyme in the presence of 1,5-anhydro-D-fructose Ensifer adhaerens
1.1.1.263 0.2
-
 NADPH mutant K94G in the presence of 1,5-anhydro-D-fructose Ensifer adhaerens
1.1.1.263 0.27
-
 NADPH mutant S10G in the presence of 1,5-anhydro-D-fructose Ensifer adhaerens
1.1.1.263 0.38
-
 NADPH mutant A13G/S10G in the presence of 1,5-anhydro-D-fructose Ensifer adhaerens
1.1.1.263 1
-
 NADPH mutant A13G/S33D in the presence of 1,5-anhydro-D-fructose Ensifer adhaerens
1.1.1.263 1.1
-
 NADH mutant A13G in the presence of 1,5-anhydro-D-fructose Ensifer adhaerens
1.1.1.263 1.1
-
 NADH mutant A13G/S33D in the presence of 1,5-anhydro-D-fructose Ensifer adhaerens
1.1.1.263 1.2
-
 NADH mutant A13G/S10G in the presence of 1,5-anhydro-D-fructose Ensifer adhaerens
1.1.1.263 3.2
-
 1,5-Anhydro-D-fructose mutant A13G/S33D in the presence of NADH Ensifer adhaerens
1.1.1.263 3.5
-
 1,5-Anhydro-D-fructose mutant S10G in the presence of NADPH Ensifer adhaerens
1.1.1.263 6.4
-
 1,5-Anhydro-D-fructose recombinant wild type enzyme in the presence of NADPH Ensifer adhaerens
1.1.1.263 7.1
-
 1,5-Anhydro-D-fructose mutant A13G/S10Gin the presence of NADPH Ensifer adhaerens
1.1.1.263 8.3
-
 1,5-Anhydro-D-fructose mutant G206I in the presence of NADPH Ensifer adhaerens
1.1.1.263 8.3
-
 1,5-Anhydro-D-fructose native wild type enzyme in the presence of NADPH Ensifer adhaerens
1.1.1.263 8.5
-
 1,5-Anhydro-D-fructose mutant A13G in the presence of NADPH Ensifer adhaerens
1.1.1.263 8.9
-
 1,5-Anhydro-D-fructose mutant H108A in the presence of NADPH Ensifer adhaerens
1.1.1.263 11.1
-
 1,5-Anhydro-D-fructose mutant A13G in the presence of NADH Ensifer adhaerens
1.1.1.263 20.2
-
 1,5-Anhydro-D-fructose mutant A13G/S33D in the presence of NADPH Ensifer adhaerens
1.1.1.263 22.5
-
 1,5-Anhydro-D-fructose mutant K94G in the presence of NADPH Ensifer adhaerens
1.1.1.263 39
-
 1,5-Anhydro-D-fructose mutant A13G/S10G in the presence of NADH Ensifer adhaerens
1.1.1.263 49
-
 1,5-Anhydro-D-fructose mutant D176A in the presence of NADPH Ensifer adhaerens
1.1.1.292 0.02
-
 NADPH pH 6.5, mutant enzyme A13G Ensifer adhaerens
1.1.1.292 0.06
-
 NADPH pH 6.5 recombinant wild-type enzyme Ensifer adhaerens
1.1.1.292 0.06
-
 NADPH pH 6.5, mutant enzyme G206I Ensifer adhaerens
1.1.1.292 0.1
-
 NADPH pH 6.5, native wild-type enzyme Ensifer adhaerens
1.1.1.292 0.2
-
 NADPH pH 6.5, mutant enzyme K94G Ensifer adhaerens
1.1.1.292 0.27
-
 NADPH pH 6.5, mutant enzyme S10G Ensifer adhaerens
1.1.1.292 0.38
-
 NADPH pH 6.5, mutant enzyme S10G/A13G Ensifer adhaerens
1.1.1.292 1
-
 NADPH pH 6.5, mutant enzyme S33D/A13G Ensifer adhaerens
1.1.1.292 1.1
-
 NADH pH 6.5, mutant enzyme A13G Ensifer adhaerens
1.1.1.292 1.1
-
 NADH pH 6.5, mutant enzyme S33D/A13G Ensifer adhaerens
1.1.1.292 1.1
-
 NADH mutant enzyme A13G/S33D, at pH 6.5 and 30°C Ensifer adhaerens
1.1.1.292 1.2
-
 NADH pH 6.5, mutant enzyme S10G/A13G Ensifer adhaerens
1.1.1.292 1.2
-
 NADH mutant enzyme A13G/S10G, at pH 6.5 and 30°C Ensifer adhaerens
1.1.1.292 3.2
-
 1,5-Anhydro-D-fructose pH 6.5, mutant enzyme S33D/A13G, cofactor: NADH Ensifer adhaerens
1.1.1.292 3.5
-
 1,5-Anhydro-D-fructose pH 6.5, mutant enzyme S10G, cofactor: NADPH Ensifer adhaerens
1.1.1.292 6.4
-
 1,5-Anhydro-D-fructose pH 6.5 recombinant wild-type enzyme, cofactor: NADPH Ensifer adhaerens
1.1.1.292 7.1
-
 1,5-Anhydro-D-fructose pH 6.5, mutant enzyme S10G/A13G, cofactor: NADPH Ensifer adhaerens
1.1.1.292 8.3
-
 1,5-Anhydro-D-fructose pH 6.5, mutant enzyme G206I, cofactor: NADPH Ensifer adhaerens
1.1.1.292 8.3
-
 1,5-Anhydro-D-fructose pH 6.5, native wild-type enzyme, cofactor: NADPH Ensifer adhaerens
1.1.1.292 8.5
-
 1,5-Anhydro-D-fructose pH 6.5, mutant enzyme A13G, cofactor: NADPH Ensifer adhaerens
1.1.1.292 8.9
-
 1,5-Anhydro-D-fructose pH 8.0, mutant enzyme H180A, cofactor: NADPH Ensifer adhaerens
1.1.1.292 11.1
-
 1,5-Anhydro-D-fructose pH 6.5, mutant enzyme A13G, cofactor: NADH Ensifer adhaerens
1.1.1.292 20.2
-
 1,5-Anhydro-D-fructose pH 6.5, mutant enzyme S33D/A13G, cofactor: NADPH Ensifer adhaerens
1.1.1.292 22.5
-
 1,5-Anhydro-D-fructose pH 6.5, mutant enzyme K94G, cofactor: NADPH Ensifer adhaerens
1.1.1.292 39
-
 1,5-Anhydro-D-fructose pH 6.5, mutant enzyme S10G/A13G, cofactor: NADH Ensifer adhaerens
1.1.1.292 49
-
 1,5-Anhydro-D-fructose pH 7.5, mutant enzyme D176A, cofactor: NADPH Ensifer adhaerens

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.263 Ensifer adhaerens
-
-
-
1.1.1.263 Ensifer adhaerens S-30.7.5
-
-
-
1.1.1.292 Ensifer adhaerens Q2I8V6 i.e. Ensifer adhaerens
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.263 gel filtration Ensifer adhaerens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.263 1,5-anhydro-D-fructose + NADH
-
 Ensifer adhaerens 1,5-anhydro-D-mannitol + NAD+
-
 ?
1.1.1.263 1,5-anhydro-D-fructose + NADH
-
 Ensifer adhaerens S-30.7.5 1,5-anhydro-D-mannitol + NAD+
-
 ?
1.1.1.263 1,5-anhydro-D-fructose + NADPH
-
 Ensifer adhaerens 1,5-anhydro-D-mannitol + NADP+
-
 ir
1.1.1.263 1,5-anhydro-D-fructose + NADPH
-
 Ensifer adhaerens S-30.7.5 1,5-anhydro-D-mannitol + NADP+
-
 ir
1.1.1.292 1,5-anhydro-D-fructose + NADH + H+
-
 Ensifer adhaerens 1,5-anhydro-D-mannitol + NAD+
-
 r
1.1.1.292 1,5-anhydro-D-fructose + NADPH + H+
-
 Ensifer adhaerens 1,5-anhydro-D-mannitol + NADP+
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.263 1,4-AF-reductase
-
 Ensifer adhaerens
1.1.1.263 AFR
-
 Ensifer adhaerens
1.1.1.263 NADP(H)-dependent 1,5-anhydro-D-fructose reductase
-
 Ensifer adhaerens
1.1.1.263 NADPH-dependent anhydrofructose reductase
-
 Ensifer adhaerens
1.1.1.292 1,5-anhydro-D-fructose reductase
-
 Ensifer adhaerens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.263 1.3
-
 1,5-Anhydro-D-fructose mutant D176A in the presence of NADPH Ensifer adhaerens
1.1.1.263 3.7
-
 1,5-Anhydro-D-fructose mutant H108A in the presence of NADPH Ensifer adhaerens
1.1.1.263 4.2
-
 1,5-Anhydro-D-fructose mutant K94G in the presence of NADPH Ensifer adhaerens
1.1.1.263 5.5
-
 1,5-Anhydro-D-fructose mutant A13G/S10G in the presence of NADH Ensifer adhaerens
1.1.1.263 6.3
-
 1,5-Anhydro-D-fructose mutant A13G/S33D in the presence of NADPH Ensifer adhaerens
1.1.1.263 12.4
-
 1,5-Anhydro-D-fructose mutant A13G in the presence of NADH Ensifer adhaerens
1.1.1.263 13.5
-
 1,5-Anhydro-D-fructose mutant S33D in the presence of NADH Ensifer adhaerens
1.1.1.263 119
-
 1,5-Anhydro-D-fructose mutant S10G in the presence of NADPH Ensifer adhaerens
1.1.1.263 145
-
 1,5-Anhydro-D-fructose recombinant wild type enzyme in the presence of NADPH Ensifer adhaerens
1.1.1.263 156
-
 1,5-Anhydro-D-fructose mutant G206I in the presence of NADPH Ensifer adhaerens
1.1.1.263 216
-
 1,5-Anhydro-D-fructose native wild type enzyme in the presence of NADPH Ensifer adhaerens
1.1.1.263 369
-
 1,5-Anhydro-D-fructose mutant A13G/S10Gin the presence of NADPH Ensifer adhaerens
1.1.1.263 405
-
 1,5-Anhydro-D-fructose mutant A13G in the presence of NADPH Ensifer adhaerens
1.1.1.292 1.3
-
 1,5-Anhydro-D-fructose pH 7.5, mutant enzyme D176A, cofactor: NADPH Ensifer adhaerens
1.1.1.292 3.7
-
 1,5-Anhydro-D-fructose pH 8.0, mutant enzyme H180A, cofactor: NADPH Ensifer adhaerens
1.1.1.292 4.2
-
 1,5-Anhydro-D-fructose pH 6.5, mutant enzyme K94G, cofactor: NADPH Ensifer adhaerens
1.1.1.292 5.5
-
 1,5-Anhydro-D-fructose pH 6.5, mutant enzyme S10G/A13G, cofactor: NADH Ensifer adhaerens
1.1.1.292 6.3
-
 1,5-Anhydro-D-fructose pH 6.5, mutant enzyme S33D/A13G, cofactor: NADPH Ensifer adhaerens
1.1.1.292 12.4
-
 1,5-Anhydro-D-fructose pH 6.5, mutant enzyme A13G, cofactor: NADH Ensifer adhaerens
1.1.1.292 13.5
-
 1,5-Anhydro-D-fructose pH 6.5, mutant enzyme S33D/A13G, cofactor: NADH Ensifer adhaerens
1.1.1.292 119
-
 1,5-Anhydro-D-fructose pH 6.5, mutant enzyme S10G, cofactor: NADPH Ensifer adhaerens
1.1.1.292 145
-
 1,5-Anhydro-D-fructose pH 6.5 recombinant wild-type enzyme, cofactor: NADPH Ensifer adhaerens
1.1.1.292 156
-
 1,5-Anhydro-D-fructose pH 6.5, mutant enzyme G206I, cofactor: NADPH Ensifer adhaerens
1.1.1.292 216
-
 1,5-Anhydro-D-fructose pH 6.5, native wild-type enzyme, cofactor: NADPH Ensifer adhaerens
1.1.1.292 369
-
 1,5-Anhydro-D-fructose pH 6.5, mutant enzyme S10G/A13G, cofactor: NADPH Ensifer adhaerens
1.1.1.292 405
-
 1,5-Anhydro-D-fructose pH 6.5, mutant enzyme A13G, cofactor: NADPH Ensifer adhaerens

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.263 NAD(P)H
-
 Ensifer adhaerens
1.1.1.292 NADH wild-type enzyme and mutant enzymes S10G, S33D, K94G, D176A, H180A and G206I shows no activity with NADH. Mutant enzymes A13G, S10G/A13G and S33D/A13G are active with NADH Ensifer adhaerens
1.1.1.292 NADPH the N-terminal domain displays a Rossman fold and contains the cofactor binding site. The intact crystals contain the oxidized cofactor NADP+ Ensifer adhaerens