التفاصيل البيبلوغرافية
| العنوان: |
Functional characterization of a catalytically promiscuous tryptophan decarboxylase from camptothecin-producing Camptotheca acuminata |
| المؤلفون: |
Chong Qiao, Fei Chen, Zhan Liu, Tianfang Huang, Wei Li, Guolin Zhang, Yinggang Luo |
| المصدر: |
Frontiers in Plant Science, Vol 13 (2022) |
| بيانات النشر: |
Frontiers Media S.A., 2022. |
| سنة النشر: |
2022 |
| المجموعة: |
LCC:Plant culture |
| مصطلحات موضوعية: |
tryptophan decarboxylase, promiscuity, tryptamine, decarboxylation, Camptotheca acuminata, Plant culture, SB1-1110 |
| الوصف: |
Tryptophan decarboxylases (TDCs) are a group of pyridoxal 5′-phosphate-dependent enzymes involved in the enzymatic conversion of tryptophan into tryptamine, a critical biogenic amine. We herein mined and cloned a TDC-encoding gene, CaTDC3, from camptothecin-producing plant Camptotheca acuminata. The intact CaTDC3 was heterologously overexpressed in Escherichia coli and the recombinant CaTDC3 was purified to homogeneity. High-performance liquid chromatography (HPLC)-diode array detector (DAD) and high resolution mass spectrometry (HRMS) data analyses of the CaTDC3-catalyzed reaction mixture confirmed the catalytically decarboxylative activity of CaTDC3. CaTDC3 shows strict stereoselectivity for L-tryptophan. Homology modeling and molecular docking implied CaTDC3’s recognition of L-tryptophan derivatives and analogs. Substrate scope investigations revealed that the appropriate substituent groups on the indole ring, i.e., hydroxylated and halogenated L-tryptophans, could be recognized by CaTDC3 and the decarboxylation reactions generated the corresponding tryptamines. The Cβ -methyl-L-tryptophans were decarboxylated by CaTDC3 efficiently. 1-Thio-L-tryptophan, the NH group of the indole ring replaced by an S atom, could be decarboxylated by CaTDC3. CaTDC3 catalyzed the decarboxylation of 7-aza-L-tryptophan, an N displacement of the C on the aromatic ring, to afford 7-aza-tryptamine. L-Kynurenine, an L-tryptophan degradation product, could be decarboxylated by CaTDC3. The present works uncover a catalytically promiscuous TDC and the TDC is a versatile decarboxylase in synthetic biology for specialized pharmaceutically important substances. |
| نوع الوثيقة: |
article |
| وصف الملف: |
electronic resource |
| اللغة: |
English |
| تدمد: |
1664-462X |
| Relation: |
https://www.frontiersin.org/articles/10.3389/fpls.2022.987348/full; https://doaj.org/toc/1664-462X |
| DOI: |
10.3389/fpls.2022.987348 |
| URL الوصول: |
https://doaj.org/article/5110cb4b363b4959855b9d4a2afb97cf |
| رقم الانضمام: |
edsdoj.5110cb4b363b4959855b9d4a2afb97cf |
| قاعدة البيانات: |
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