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. 2021 Sep 30;12:713795. doi: 10.3389/fpls.2021.713795

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Copyright © 2021 Li, Xu, Zheng, Zhang and Cai.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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LlTYDC enzyme activity assays of recombinant LlTYDC. (A) SDS-PAGE gel image of LlTYDC expression in E. coli. The recombinant GST-tagged protein was purified from the culture lysates by affinity chromatography. 1: loading sample, 2: Flow through, 3: elution fractions, 4: wash through. M, molecular weight marker. (B) LC-MS/MS analysis of the enzyme assay of GST vector using tyrosine as a substrate. (C) LC-MS/MS analysis of the tyramine standard. (D) LC-MS/MS analysis of the enzyme assay of LlTYDC using tyrosine as a substrate. The reaction product tyramine was detected in an assay using recombinant LlTYDC. The identity was confirmed by MS/MS fragmentation of tyrosine (E) and tyramine (F). The red line segment indicated the ion fragmentation pattern and the arrow indicated the retention time.