초록
<P>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 <I>p</I>-coumaryl, caffeyl, and coniferyl alcohols from <SMALL>L</SMALL>-tyrosine in <I>Escherichia coli</I> BL21 (DE3). By overexpressing the <SMALL>L</SMALL>-tyrosine ammonia lyase from <I>Flavobacterium johnsoniae</I> (FjTAL), carboxylate reductase from <I>Segniliparus rugosus</I> (SruCAR), alcohol dehydrogenase YqhD and hydroxylase HpaBC from <I>E. coli</I>, and caffeate 3-O-methyltransferase (COMT) from <I>Arabidopsis thaliana</I>, three enzyme cascades FjTAL-SruCAR-YqhD, FjTAL-SruCAR-YqhD-HpaBC, and FjTAL-SruCAR-YqhD-HpaBC-COMT were constructed to produce 1028.5 mg/L <I>p</I>-coumaryl alcohol, 1015.3 mg/L caffeyl alcohol, and 411.4 mg/L coniferyl alcohol from 1500, 1500, and 1000 mg/L <SMALL>L</SMALL>-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 <I>p</I>-coumaryl, caffeyl, and coniferyl alcohols from <SMALL>L</SMALL>-tyrosine.</P><BR>[FIG OMISSION]</BR>