Whole-Cell Bioconversion Systems for Efficient Synthesis of Monolignols from L-Tyrosine in .

Monolignols and their derivatives exhibit various pharmaceutical and physiological characteristics, such as antioxidant and anti-inflammatory properties. However, they remain difficult to synthesize. In this study, we engineered several whole-cell bioconversion systems with carboxylate reductase (CAR)-mediated pathways for efficient synthesis of -coumaryl, caffeyl, and coniferyl alcohols from l-tyrosine in BL21 (DE3). By overexpressing the l-tyrosine ammonia lyase from (FjTAL), carboxylate reductase from (SruCAR), alcohol dehydrogenase YqhD and hydroxylase HpaBC from , and caffeate 3-O-methyltransferase (COMT) from , three enzyme cascades FjTAL-SruCAR-YqhD, FjTAL-SruCAR-YqhD-HpaBC, and FjTAL-SruCAR-YqhD-HpaBC-COMT were constructed to produce 1028.5 mg/L -coumaryl alcohol, 1015.3 mg/L caffeyl alcohol, and 411.4 mg/L coniferyl alcohol from 1500, 1500, and 1000 mg/L l-tyrosine, with productivities of 257.1, 203.1, and 82.3 mg/L/h, respectively. This work provides an efficient strategy for the biosynthesis of -coumaryl, caffeyl, and coniferyl alcohols from l-tyrosine.