Phenylalanine lyase mutant and preparation method of alpha-methyl amino acid

By using a phenylalanine lyase mutant to catalyze the reaction between olefinic acid substrates and amino donors, the problem of low synthesis efficiency of non-natural amino acids in existing technologies has been solved, and efficient and safe preparation of α-methyl amino acids has been achieved.

CN122012482APending Publication Date: 2026-05-12TIANJIN ASYMCHEM BIOTECHNOLOGY CO LTD +1
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Patent Information

Application Number
CN202610193881.6
Authority / Receiving Office
CN · China
Patent Type
Applications(China)
Current Assignee / Owner
Filing Date
2026-02-10
Publication Date
2026-05-12

AI Technical Summary

Technical Problem

Existing technologies make it difficult to synthesize non-natural amino acids simply and efficiently. Chemical synthesis methods suffer from low yields, the use of toxic reagents, and cumbersome processes.

Method used

Develop phenylalanine lyase mutants and obtain enzymes with specific amino acid mutations through directed evolution for use in catalyzing the reaction of enoic acid substrates and amino donors to prepare α-methyl amino acids.

Benefits of technology

This method enables the efficient preparation of α-methyl amino acids with 100% atom economy and excellent stereoselectivity, meeting the green, efficient, and safe production requirements of modern pharmaceutical industry.

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Abstract

The invention provides a phenylalanine lyase mutant and a preparation method of alpha-methyl amino acid. Wherein the phenylalanine lyase mutant comprises (a) a protein mutated on the basis of wild type phenylalanine lyase as shown in SEQ ID NO: 1, and the mutation is selected from mutation of any one or more of the following sites: N438, C288, Y304, F90, P317, S114 and the like; or (b) a protein which has more than 70% of homology with the amino acid sequence limited in (a) and has phenylalanine lyase activity. The method can solve the problem that non-natural amino acid is difficult to simply and efficiently synthesize in the prior art and is suitable for the field of enzyme catalysis.
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