Literature summary for 1.1.3.46 extracted from

Chen, Y.; Wu, P.; Ko, L.; Kao, T.; Liu, L.; Zhang, Y.; Yuan, J.
High-yielding protocatechuic acid synthesis from l -tyrosine in Escherichia coli (2020), ACS Sust. Chem. Eng., 8, 14949-14954 .

No PubMed abstract available

Search for more literature for 1.1.3.46

Application

Application	Comment	Organism
synthesis	whole-cell bioconversion of L-tyrosine into protocatechuic acid using artificial enzymatic cascades engineered in Escherichia coli. The first biocatalytic route comprises L-amino acid deaminase (LAAD) from Proteus mirabilis, hydroxymandelate synthase (HmaS) from Amycolatopsis orientalis, two-component flavin-dependent monooxygenase (HpaBC) from Escherichia coli, hydroxymandelate oxidase (HMO) from Streptomyces coelicolor, benzoylformate decarboxylase (BFD) from Pseudomonas putida, and aldehyde dehydrogenase (ALDH) from Saccharomyces cerevisiae. Combining LAAD/HmaS/HpaBC results in efficient synthesis of 3,4-dihydroxymandelate, which can be further converted to protocatechuic acid by HMO/BFD/ALDH to a final conversion of 64.4%. The recombinant E. coli catalyzes >99% conversion of L-tyrosine into 4-hydroxybenzoate within 12 h, further incorporation of 4-hydroxybenzoate hydroxylase PobA results in complete conversion of 4-hydroxybenzoate into protocatechuic acid, reaching >99% conversion	Streptomyces coelicolor

Organism

Organism	UniProt	Comment	Textmining
Streptomyces coelicolor	-	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)