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Tryptophan Synthase: Biocatalyst Extraordinaire
Tryptophan synthase (TrpS) has emerged as a paragon of noncanonical amino acid (ncAA) synthesis and is an ideal biocatalyst for synthetic and biological applications. TrpS catalyzes an irreversible, C−C bond‐forming reaction between indole and serine to make l‐tryptophan; native TrpS complexes posse...
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Published in: | Chembiochem : a European journal of chemical biology 2021-01, Vol.22 (1), p.5-16 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Tryptophan synthase (TrpS) has emerged as a paragon of noncanonical amino acid (ncAA) synthesis and is an ideal biocatalyst for synthetic and biological applications. TrpS catalyzes an irreversible, C−C bond‐forming reaction between indole and serine to make l‐tryptophan; native TrpS complexes possess fairly broad specificity for indole analogues, but are difficult to engineer to extend substrate scope or to confer other useful properties due to allosteric constraints and their heterodimeric structure. Directed evolution freed the catalytically relevant TrpS β‐subunit (TrpB) from allosteric regulation by its TrpA partner and has enabled dramatic expansion of the enzyme's substrate scope. This review examines the long and storied career of TrpS from the perspective of its application in ncAA synthesis and biocatalytic cascades.
Multifunctional: Tryptophan synthase (TrpS) natively catalyzes the formation of tryptophan but also possesses remarkable promiscuous activity for synthesizing a wide range of noncanonical amino acids (ncAAs). This review looks at TrpS as a ncAA synthase, from the characterization of its broad substrate scope via efforts to expand its non‐natural chemistry to applications in synthesizing diverse natural and xenobiotic compounds. |
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ISSN: | 1439-4227 1439-7633 |
DOI: | 10.1002/cbic.202000379 |