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Literature summary for 1.1.1.292 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
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Ensifer adhaerens

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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
G206I kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 1.4fold lower than wild type value Ensifer adhaerens
H180A kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 61.9fold lower than wild type value Ensifer adhaerens
K94G kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 137fold lower than wild type value Ensifer adhaerens
S10G kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 1.3fold higher than wild type value Ensifer adhaerens
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
S176A kcat/Km for reaction with 1,5-anhydro-D-fructose and NADPH is 1001fold lower than wild type value Ensifer adhaerens
S33D no activity Ensifer adhaerens
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]

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

Organism

Organism UniProt Comment Textmining
Ensifer adhaerens Q2I8V6 i.e. Ensifer adhaerens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,5-anhydro-D-fructose + NADH + H+
-
 Ensifer adhaerens 1,5-anhydro-D-mannitol + NAD+
-
 r
1,5-anhydro-D-fructose + NADPH + H+
-
 Ensifer adhaerens 1,5-anhydro-D-mannitol + NADP+
-
 ?

Synonyms

Synonyms Comment Organism
1,5-anhydro-D-fructose reductase
-
 Ensifer adhaerens

Turnover Number [1/s]

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

Cofactor

Cofactor Comment Organism Structure
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
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