Computational-Designed Enzyme for β-Tyrosine Production in Lignin Valorization

Lignin is an underutilized sustainable source of aromatic compounds. To valorize the low-value lignin monomers, we proposed efficient strategy, involving enzymatic conversion from trans-p-hydroxycinnamic acids to generate valued-added canonical and non-canonical amino acids. Among them, β-amino are recognized as building blocks for bioactive natural products pharmaceutical ingredients due their attractive antitumor properties. Using computational enzyme design, (R)-β-selective phenylalanine aminomutase Taxus chinensis (TchPAM) was successfully mutated accept β-tyrosine substrate, well (R)-β-tyrosine with excellent enantiopurity (ee > 99%) unique product acid. Moreover, kinetic parameters were determined reaction four Y424 variants synthesis different tyrosine enantiomers. In ammonia elimination (R)-β-tyrosine, Y424N Y424C displayed a two-fold increased catalytic efficiency wild type. this work, binding pocket in active site, including Y424, K427, I431, E455, examined its influence on β-enantioselectivity family. Combining upstream depolymerization downstream production, value chain based enabled. summary, report process monolignol component, offering new way valorization by biocatalyst modification.