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 an efficient strategy, involving enzymatic conversion from <i>trans</i>-<i>p</i>-hydroxycinnamic acids to generate valued-added canonical and non-canoni...

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Autores principales:	Fei Peng, Habibu Aliyu, André Delavault, Ulrike Engel, Jens Rudat
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	β-tyrosine β-amino acid phenylalanine aminomutase lignin valorization computational enzyme design Rosetta enzyme design Chemical technology TP1-1185 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/c9f80b42850d4b7f8c8c59c77d075a49
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spelling	oai:doaj.org-article:c9f80b42850d4b7f8c8c59c77d075a492021-11-25T17:05:43ZComputational-Designed Enzyme for β-Tyrosine Production in Lignin Valorization10.3390/catal111113102073-4344https://doaj.org/article/c9f80b42850d4b7f8c8c59c77d075a492021-10-01T00:00:00Zhttps://www.mdpi.com/2073-4344/11/11/1310https://doaj.org/toc/2073-4344Lignin is an underutilized sustainable source of aromatic compounds. To valorize the low-value lignin monomers, we proposed an efficient strategy, involving enzymatic conversion from <i>trans</i>-<i>p</i>-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 (<i>R</i>)-β-selective phenylalanine aminomutase from <i>Taxus chinensis</i> (TchPAM) was successfully mutated to accept β-tyrosine as the substrate, as well as to generate the (<i>R</i>)-β-tyrosine with excellent enantiopurity (ee > 99%) as the unique product from <i>trans</i>-<i>p</i>-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 (<i>R</i>)-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. Combining the upstream lignin depolymerization and downstream production, a sustainable value chain based on lignin is enabled. In summary, we report a β-tyrosine synthesis process from a monolignol component, offering a new way for lignin valorization by biocatalyst modification.Fei PengHabibu AliyuAndré DelavaultUlrike EngelJens RudatMDPI AGarticleβ-tyrosineβ-amino acidphenylalanine aminomutaselignin valorizationcomputational enzyme designRosetta enzyme designChemical technologyTP1-1185ChemistryQD1-999ENCatalysts, Vol 11, Iss 1310, p 1310 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	β-tyrosine β-amino acid phenylalanine aminomutase lignin valorization computational enzyme design Rosetta enzyme design Chemical technology TP1-1185 Chemistry QD1-999
spellingShingle	β-tyrosine β-amino acid phenylalanine aminomutase lignin valorization computational enzyme design Rosetta enzyme design Chemical technology TP1-1185 Chemistry QD1-999 Fei Peng Habibu Aliyu André Delavault Ulrike Engel Jens Rudat Computational-Designed Enzyme for β-Tyrosine Production in Lignin Valorization
description	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 <i>trans</i>-<i>p</i>-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 (<i>R</i>)-β-selective phenylalanine aminomutase from <i>Taxus chinensis</i> (TchPAM) was successfully mutated to accept β-tyrosine as the substrate, as well as to generate the (<i>R</i>)-β-tyrosine with excellent enantiopurity (ee > 99%) as the unique product from <i>trans</i>-<i>p</i>-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 (<i>R</i>)-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. Combining the upstream lignin depolymerization and downstream production, a sustainable value chain based on lignin is enabled. In summary, we report a β-tyrosine synthesis process from a monolignol component, offering a new way for lignin valorization by biocatalyst modification.
format	article
author	Fei Peng Habibu Aliyu André Delavault Ulrike Engel Jens Rudat
author_facet	Fei Peng Habibu Aliyu André Delavault Ulrike Engel Jens Rudat
author_sort	Fei Peng
title	Computational-Designed Enzyme for β-Tyrosine Production in Lignin Valorization
title_short	Computational-Designed Enzyme for β-Tyrosine Production in Lignin Valorization
title_full	Computational-Designed Enzyme for β-Tyrosine Production in Lignin Valorization
title_fullStr	Computational-Designed Enzyme for β-Tyrosine Production in Lignin Valorization
title_full_unstemmed	Computational-Designed Enzyme for β-Tyrosine Production in Lignin Valorization
title_sort	computational-designed enzyme for β-tyrosine production in lignin valorization
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/c9f80b42850d4b7f8c8c59c77d075a49
work_keys_str_mv	AT feipeng computationaldesignedenzymeforbtyrosineproductioninligninvalorization AT habibualiyu computationaldesignedenzymeforbtyrosineproductioninligninvalorization AT andredelavault computationaldesignedenzymeforbtyrosineproductioninligninvalorization AT ulrikeengel computationaldesignedenzymeforbtyrosineproductioninligninvalorization AT jensrudat computationaldesignedenzymeforbtyrosineproductioninligninvalorization
_version_	1718412741112233984

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

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