EC Number   |
Protein Variants |
Reference |
|---|
    1.1.1.4 | D194G |
the mutant enzyme has almost lost its entire enzymatic activity |
-, 738880 |
| 1.1.1.4 | E221S the |
mutation produces a 170fold decrease in the Vm/Km with NADH because of a simultaneous 16fold increase in the Km value and an 11fold decrease in the Vm value, the mutation provides a positive effect on NADPH coenzyme specificity |
696883 |
| 1.1.1.4 | E221S/I222R |
mutant with preference for NADPH as coenzyme |
696883 |
| 1.1.1.4 | E221S/I222R/A223S |
mutant with preference for NADPH as coenzyme |
696883 |
| 1.1.1.4 | G198D/S199 V/P201E/Y218A |
mutant displays no detectable activity with NADPH as cofactor, but uses NADH with kcat/Km value of 12 per s and mM |
739571 |
| 1.1.1.4 | more |
coexpression of 2,3-BD biosynthesis pathway genes alsS, alsD, and bdhA in synthetically engineered strains Corynebacterium crenatumDELTAbutADELTAldh SD and Corynebacterium crenatumDELTAldh SDA for selective acetoin (AC) and 2,3-butanediol (2,3-BD) production. Production of AC and 2,3-BD using resting cell bioconversion with glucose as substrate, method evaluation, overview |
-, 761834 |
| 1.1.1.4 | more |
construction of a an BDH1 deletion strain, WY1DELTA1, which shows 1.37fold increased diacetyl production |
-, 761646 |
| 1.1.1.4 | more |
construction of an engineered Bacillus subtilis strain 168 in which the bdhA gene is knocked out by the cre/lox system using the lox71-zeo-lox66 resistance marker cassette. The effects of bdhA gene deletion on production of acetoin and 2,3-butanediol are evaluated. By increasing the glucose concentration, the acetoin yield is improved from 6.61 g/l to 24.6 g/l. Deletion of the gene bdhA efficiently blocks the transformation of acetoin and 2,3-butanediol during the fermentation of strain BS168D, overview |
-, 762259 |
| 1.1.1.4 | more |
expression of 4 genes encoding alpha-acetolactate synthase from Bacillus subtilis, alpha-acetolactate decarboxylase and 2,3-butanediol dehydrogenase from Bacillus amyloliquefaciens, and NADH oxidase from Lactococcus lactis in Saccharomyces cerevisiae strain YPH499 is modulated using a cocktail delta-integration strategy. The resultant strain, YPH499/dPdAdG/BD6-10, is used in a fed-batch cultivation for the production of 2,3-butanediol. The concentration, production rate, and yield obtained are 80.0 g/l, 4.00 g/l/h, and 41.7%, respectively. The cocktail delta-integration strategy leads to the upregulation of BsAlsS and BaAlsD genes in the modified strain, which results in higher production rate of 2,3-butanediol. The conversion rate of pyruvate to alpha-acetolactate, catalyzed by BsAlsS, and of alpha-acetolactate into acetoin (catalyzed by BaAlsD) must be slower compared to that of acetoin being converted to 2,3-butanediol catalyzed by BaBdhA in the control strain. The conversion of alpha-acetolactate into acetoin catalyzed by alpha-acetolactate decarboxylase might be the rate limiting step in 2,3-butanediol production in recombinant Saccharomyces cerevisiae. Method development and evaluation, overview |
-, 760716 |
| 1.1.1.4 | more |
in vitro bioreduction of 2-hydroxyacetophenone (2-HAP) is catalyzed by BDHA coupled with glucose dehydrogenase (GDH) from Bacillus subtilis for cofactor regeneration. The two coexpressed enantiocomplementary carbonyl reductases, BDHA and GoSCR (polyol dehydrogenase from Gluconobacter oxydans) 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 co-solvent), 60-250 mM D-glucose. Strong tolerance of BDHA and GoSCR against high substrate concentration |
-, 761565 |
