   4.1.1.63 | synthesis |
engineering of Pseudomonas putida KT2440 to produce muconate from either aromatic molecules or sugars. Coexpression of protocatechuate decarboxylase and associated proteins reduces protocatechuate accumulation and enhances muconate production relative to strains expressing the protocatechuate decarboxylase alone. In bioreactor experiments, coexpression increases the specific productivity of muconate from the lignin monomer p-coumarate by 50% and results in a titer of >15 g/l. In strains engineered to produce muconate from glucose, coexpression more than triples the titer, yield, productivity, and specific productivity, with the best strain producing 4.92±0.48 g/l muconate |
-, 748563 |
| 4.1.1.63 | synthesis |
production of the 4-hydroxybenzoate, protocatechuate, and catechol in Escherichia coli. To enhance endogenous biosynthesis of 4-hydroxybenzoate, native chorismate pyruvate lyase ubiC is overexpressed. 4-Hydroxybenzoate is converted to protocatechuate by hydroxylase pobA from Pseudomonas aeruginosa. Catechol is produced by the additional coexpression of protocatechuate decarboxylase from Enterobacter cloacae. Systematic expression of appropriate pathway elements in phenylalanine overproducing Escherichia coli enables initial titers of 32, 110, and 81 mg/l for 4-hydroxybenzoate, protocatechuate, and catechol, respectively. Disruption of chorismate mutase/prephenate dehydratase (pheA) to preserve endogenous chorismate then allows maximum titers of 277, 454, and 451 mg/l, respectively, at glucose yields of 5.8, 9.7, and 14.3% of their respective theoretical maxima |
749197 |
