التفاصيل البيبلوغرافية
| العنوان: |
Data_Sheet_1_Functional characterization of a catalytically promiscuous tryptophan decarboxylase from camptothecin-producing Camptotheca acuminata.docx |
| المؤلفون: |
Chong Qiao, Fei Chen, Zhan Liu, Tianfang Huang, Wei Li, Guolin Zhang, Yinggang Luo |
| سنة النشر: |
2022 |
| المجموعة: |
Frontiers: Figshare |
| مصطلحات موضوعية: |
Botany, Plant Biology, Plant Systematics and Taxonomy, Plant Cell and Molecular Biology, Plant Developmental and Reproductive Biology, Plant Pathology, Plant Physiology, Plant Biology not elsewhere classified, tryptophan decarboxylase, promiscuity, tryptamine, decarboxylation, Camptotheca acuminata |
| 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 C β -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: |
dataset |
| اللغة: |
unknown |
| Relation: |
https://figshare.com/articles/dataset/Data_Sheet_1_Functional_characterization_of_a_catalytically_promiscuous_tryptophan_decarboxylase_from_camptothecin-producing_Camptotheca_acuminata_docx/20507136 |
| DOI: |
10.3389/fpls.2022.987348.s001 |
| الاتاحة: |
https://doi.org/10.3389/fpls.2022.987348.s001
https://figshare.com/articles/dataset/Data_Sheet_1_Functional_characterization_of_a_catalytically_promiscuous_tryptophan_decarboxylase_from_camptothecin-producing_Camptotheca_acuminata_docx/20507136 |
| Rights: |
CC BY 4.0 |
| رقم الانضمام: |
edsbas.76A32FBC |
| قاعدة البيانات: |
BASE |