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Literature summary for 4.1.1.63 extracted from

  • Pugh, S.; McKenna, R.; Osman, M.; Thompson, B.; Nielsen, D.
    Rational engineering of a novel pathway for producing the aromatic compounds p-hydroxybenzoate, protocatechuate, and catechol in Escherichia coli (2014), Process Biochem., 49, 1843-1850 .
No PubMed abstract available

Application

Application Comment Organism
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 Enterobacter cloacae

Organism

Organism UniProt Comment Textmining
Enterobacter cloacae
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