EC Number   |
Protein Variants |
Reference |
|---|
    1.1.1.14 | D364A |
the mutant exhibits abolished energy efficiency compared to the wild type enzyme |
740006 |
| 1.1.1.14 | D55N |
mutation located at the NAD+ binding cleft, changes cofactor specificity frm NADH to NADPH |
-, 736022 |
| 1.1.1.14 | E154C |
purified preparations of mutant contain 0.1-0.4 atoms of Zn2+ per subunit and exhibit a constant catalytic Zn2+ centre activity of 1.19 per s, mutant does not require exogenous Zn2+ for stability. Mutant retains less than 1% of wild-type catalytic efficiency and displays similar primary and solvent deuterium effects as wild-type |
684974 |
| 1.1.1.14 | H302A |
the mutant exhibits abolished energy efficiency compared to the wild type enzyme |
740006 |
| 1.1.1.14 | M366A |
the mutant exhibits abolished energy efficiency compared to the wild type enzyme |
740006 |
| 1.1.1.14 | more |
construction of disruption mutants of genes sldA or sldB, the mutants are inactive, the sldB mutation leads to a higher enzyme expression and accumulation of unprocessed SldA |
-, 655022 |
| 1.1.1.14 | more |
construction of gene disruption mutants of genes sldA and sldB, the mutants are inactive, the sldB mutation leads to a higher enzyme expression and accumulation of unprocessed SldA, co-expression of sldB is required for enzyme activity in vivo |
-, 654867 |
| 1.1.1.14 | more |
in vitro bioreduction of 2-hydroxyacetophenone (2-HAP) is catalyzed by GoSCR coupled with glucose dehydrogenase (GDH) from Bacillus subtilis for cofactor regeneration. The two coexpressed enantiocomplementary carbonyl reductases, BDHA (2, 3-butanediol dehydrogenase from Bacillus subtilis) and GoSCR are used for asymmetric reduction of 2-hydroxyacetophenone (2-HAP) to (R)-1-phenyl-1,2-ethanediol ((R)-PED) or (S)-1-phenyl-1,2-ethanediol ((S)-PED) with excellent stereochemical selectivity, method optimization, overview. Products (R)-PED and (S)-PED are obtained with 99% yield, over 99% enantiomeric excess and 18.0 g/l/h volumetric productivity. The reaction is carried out in 5 ml sodium phosphate buffer (pH 7.0, 100 mM) at 30°C, containing 10 U/ml BDHA (cell free extract of Escherichia coli (BDHA)), 15 U/ml GoSCR (cell free extract of Escherichia coli (GoSCR)), 10 U/ml GDH (cell free extract of Escherichia coli (GDH)), 50-200 mM 2-HAP (with 10% DMSO as cosolvent), 60-250 mM D-glucose. Strong tolerance of BDHA and GoSCR against high substrate concentration |
-, 761565 |
| 1.1.1.14 | more |
substitution of the substrate-binding loop by the loop-region of the galactitol dehydrogenase from Rhodobacter sphaeroides (PDH-158). The substrate scope of this chimera basically represents the average of both wild-type enzymes, with an increase in thermal stability. The amino acid positions Q157 and N161 in the PDH-loop variant seem to have an essential role, variants containing mutations at these sites exhibit decreased enzyme activities. Variants containing mutations V97A or N99L do not lead to a significant activity loss |
-, 736022 |
| 1.1.1.14 | Y110F |
mutation in hydrogen onding network, complete loss of activity and destabilization of protein into tetramers, dimers and monomers compared to only tetramers for wild-type |
686021 |
