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Computational-designed enzyme for β-tyrosine production in lignin valorization

Peng, Fei; Aliyu, Habibu; Delavault, André; Engel, Ulrike; Rudat, Jens

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

Verlagsausgabe §
DOI: 10.5445/IR/1000139732
Veröffentlicht am 12.11.2021
Cover der Publikation
Zugehörige Institution(en) am KIT Institut für Bio- und Lebensmitteltechnik (BLT)
Publikationstyp Zeitschriftenaufsatz
Publikationsjahr 2021
Sprache Englisch
Identifikator ISSN: 2073-4344
KITopen-ID: 1000139732
Erschienen in Catalysts
Verlag MDPI
Band 11
Heft 11
Seiten 1310
Schlagwörter β-tyrosine; β-amino acid; phenylalanine aminomutase; lignin valorization; computational enzyme design; Rosetta enzyme design
Nachgewiesen in Scopus
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