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 |
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 |
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 |
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 |
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 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.1.1.263 | gel filtration | Ensifer adhaerens |
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+ | - |
? |
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 |
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 |
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 |