3 '-O-methyltransferase mutant and application thereof

By directed transformation and metabolic engineering optimization of 3′-O-methyltransferase from rice-derived 3′-O-methyltransferase, the tryptophan position 284 of the mutated rice flavonoid 3′-O-methyltransferase is alanine, and overexpressing the S-adenosine-L-methionine synthase gene, the problems of high production cost and low extraction rate of methylated flavonoid compounds in the prior art are solved, and the efficient production of methylated flavonoid compounds is achieved.

CN120485148APending Publication Date: 2025-08-15SHAANXI UNIV OF SCI & TECH
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Patent Information

Application Number
CN202510631741.8
Authority / Receiving Office
CN · China
Patent Type
Applications(China)
Current Assignee / Owner
Filing Date
2022-10-31
Publication Date
2025-08-15

AI Technical Summary

Technical Problem

The prior art produces high cost, unfriendly environment, low extraction rate and complex process, making it difficult to meet market demand.

Method used

The key amino acid sites of flavonoid 3′-O-methyltransferase were determined through semi-rational design of enzyme engineering strategies. The tryptophan at the 284th position of 3′-O-methyltransferase from mutant rice origin was alanine, which combined with overexpressing the S-adenosine-L-methionine synthase gene, optimized metabolic pathways and improved catalytic performance and yield.

Benefits of technology

The yield of methylated flavonoids has been significantly improved, the catalytic efficiency has been improved, the substrate affinity has been enhanced, and the yield of synthetic methylated flavonoids has been increased by more than 3.5 times.

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Abstract

The invention relates to a 3 '-O-methyltransferase mutant and application thereof. The 3 '-O-methyltransferase mutant is obtained by mutating tryptophan W at the 284th position of wild type plant oxygen methyltransferase derived from rice into alanine A, the amino acid sequence of the wild type plant oxygen methyltransferase is as shown in SEQ ID NO: 1, and the amino acid sequence of the 3'-O-methyltransferase mutant is as shown in SEQ ID NO: 2. According to the application, a key amino acid site of the catalytic activity of the flavonoid 3 '-O-methyltransferase is determined through a semi-rationally designed enzyme engineering strategy, a dominant mutant is obtained, and the dominant effect of oriented modification on the synthesis of methylated flavonoid compounds by catalyzing flavonoid compounds through the flavonoid 3'-O-methyltransferase is defined; the obtained 3 '-O-methyltransferase mutant has excellent catalytic performance, and meanwhile, the yield of methylated flavonoid compounds is further increased by optimizing and strengthening a metabolic pathway.
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