EC Number   |
Application |
Reference |
|---|
    4.1.1.72 | agriculture |
plants with enzymic activity show enhanced cold tolerance, role as a protective mechanism for growth of plants under sub optimal temperatures |
648373 |
| 4.1.1.72 | medicine |
in patients with maple syrup urine disease, mutations such as R114W-alpha or R220W-alpha cause a strongly reduced binding of thiamin diphosphate, rendering the enzyme inactive |
648374 |
| 4.1.1.72 | medicine |
naturally occuring mutations cause an impaired assembly of enzyme in patients with maple syrup urine disease |
349091 |
| 4.1.1.72 | synthesis |
comparison of relevant properties for isobutanol production of Saccharomyces cerevisiae Aro10 and Lactococcus lactis KivD and KdcA genes. Activity in cell extracts reveals a superior Vmax/Km ratio of KdcA for alpha-ketoisovalerate and a wide range of linear and branched-chain 2-oxo acids. KdcA also shows the highest activity with pyruvate which, in engineered strains, can contribute to formation of ethanol as a by-product. During oxygen-limited incubation in the presence of glucose, strains expressing kdcA or kivD show a ca. twofold higher in vivo rate of conversion of alpha-ketoisovalerate into isobutanol than an Aro10-expressing strain. Cell extracts from cultures grown on different nitrogen sources reveal increased activity of constitutively expressed KdcA after growth on both valine and phenylalanine, while KivD and Aro10 activity is only increased after growth on phenylalanine |
-, 735821 |
| 4.1.1.72 | synthesis |
expression of branched-chain 2-oxoacid decarboxylase gene from Lactococcus lactis subsp. lactis CICC 6246 and alcohol dehydrogenase gene from Zymomonas mobilis CICC 41465 in Escherichia coli. Upon incubation in LB medium, much more 3-methyl-1-butanol (104 mg/l) than isobutanol (24 mg/l) is produced. In 5 g/l glucose-containing medium, 156 and 161 mg/l isobutanol and 3-methyl-1-butanol, respectively, is produced |
-, 748348 |
| 4.1.1.72 | synthesis |
the enzyme is able to catalyze carboligation reactions with an exceptionally broad substrate range, a feature that makes KdcA a potentially valuable biocatalyst for C-C bond formation, in particular for the enzymatic synthesis of diversely substituted 2-hydroxyketones with high enantioselectivity |
677319 |
| 4.1.1.72 | synthesis |
use of the enzyme for catalytic asymmetric synthesis of (R)-phenylacetylcarbinol derivatives |
747569 |
