EC Number   |
Application |
Reference |
|---|
   1.3.1.31 | biotechnology |
enoate reductase(ER)-functionalized poplar powder(FPP) and glucose-6-phosphate dehydrogenase(GDH)-FPP enable the continuous conversion of 4-(4-methoxyphenyl)-3-buten-2-one with NAD+ recycling. The immobilization strategy is simple and inexpensive and exploits a method for the immobilization and application of enoate reductase and its cofactor recycling system |
763356 |
| 1.3.1.31 | synthesis |
2-methylsuccinic acid is a C5 branched-chain dicarboxylate that serves as an attractive synthon for the synthesis of polymers with extensive applications in coatings, cosmetic solvents and bioplastics. A promising platform for 2-methylsuccinic acid bioproduction is established. Over-expression of codon-optimized citramalate synthase variant CimA from Methanococcus jannaschii, endogenous isopropylmalate isomerase EcLeuCD and enoate reductase YqjM from Bacillus subtilis allows the production of 2-methylsuccinic acid in Escherichia coli. Incorporation of the enzyme (KpnER) into the 2-methylsuccinic acid biosynthetic pathway leads to 2-methylsuccinic acid production improvement to a titer of 0.96 g/l in aerobic condition |
-, 763423 |
| 1.3.1.31 | synthesis |
Bacillus sp. FM18civ1 can be useful for resolving a racemic mixture of carvone. Biotransformation of (4R)-(-)-carvone with Mentha pulegium leaves |
-, 763774 |
| 1.3.1.31 | synthesis |
hydrogenation activity of enoate reductases can potentially replace the chemical hydrogenation step in current synthetic protocols creating a completely bio-based pathway for the greener production of adipic acid or other biochemicals e.g. 3-phenylpropanoic acid from renewable feedstocks |
762904 |
| 1.3.1.31 | synthesis |
hydrogenation activity of enoate reductases can potentially replace the chemical hydrogenation step in current synthetic protocols creating a completely bio-based pathway for the greener production of adipic acid or other biochemicals e.g. 3-phenylpropanoic acid from renewable feedstocks. High oxygen tolerance and thermostability make the enzyme useful for in vivo and in vitro applications to overcome the limitations of chemical catalysts |
762904 |
