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1.
Int J Mol Sci ; 24(21)2023 Oct 25.
Artículo en Inglés | MEDLINE | ID: mdl-37958559

RESUMEN

Tyrosine aminotransferase (TAT, E.C. 2.6.1.5) is a pyridoxal phosphate-dependent aminotransferase that is widely found in living organisms. It catalyzes the transfer of the amino group on tyrosine to α-ketoglutarate to produce 4-hydroxyphenylpyruvic acid (4-HPP) and is the first enzyme for tyrosine degradation. Three SmTATs have been identified in the genome of Salvia miltiorrhiza (a model medicinal plant), but their information is very limited. Here, the expression profiles of the three SmTAT genes (SmTAT1, SmTAT2, and SmTAT3) were studied. All three genes expressed in different tissues and responded to methyl jasmonate stimuli. SmTAT proteins are localized in the cytoplasm. The recombinant SmTATs were subjected to in vitro biochemical properties. All three recombinant enzymes had TAT activities and SmTAT1 had the highest catalytic activity for tyrosine, followed by SmTAT3. Also, SmTAT1 preferred the direction of tyrosine deamination to 4-HPP, while SmTAT2 preferred transamination of 4-HPP to tyrosine. In parallel, transient overexpression of SmTATs in tobacco leaves revealed that all three SmTAT proteins catalyzed tyrosine to 4-HPP in vivo, with SmTAT1 exhibiting the highest enzymatic activity. Overall, our results lay a foundation for the production of tyrosine-derived secondary metabolites via metabolic engineering or synthetic biology in the future.


Asunto(s)
Salvia miltiorrhiza , Tirosina Transaminasa , Tirosina Transaminasa/genética , Tirosina Transaminasa/metabolismo , Salvia miltiorrhiza/metabolismo , Transaminasas/genética , Transaminasas/metabolismo , Tirosina/genética , Tirosina/metabolismo , Regulación de la Expresión Génica de las Plantas , Proteínas de Plantas/genética , Proteínas de Plantas/metabolismo
2.
ACS Appl Bio Mater ; 2024 Jul 20.
Artículo en Inglés | MEDLINE | ID: mdl-39031088

RESUMEN

Dietary oils─rich in omega-3, -6, and -9 fatty acids─exhibit critical impacts on health parameters such as cardiovascular function, bodily inflammation, and neurological development. There has emerged a need for low-cost, accessible method to assess dietary oil consumption and its health implications. Existing methods typically require specialized, complex equipment and extensive sample preparation steps, rendering them unsuitable for home use. Addressing this gap, herein, we study passive wireless, biocompatible biosensors that can be used to monitor dietary oils directly from foods either prepared or cooked in oil. This design uses broad-coupled split ring resonators interceded with porous silk fibroin biopolymer (requiring only food-safe materials, such as aluminum foil and biopolymer). These porous biopolymer films absorb oils at rates proportional to their viscosity/fatty acid composition and whose response can be measured wirelessly without any microelectronic components touching food. The engineering and mechanism of such sensors are explored, alongside their ability to measure the oil presence and fatty acid content directly from foods. Its simplicity, portability, and inexpensiveness are ideal for emerging needs in precision nutrition─such sensors may empower individuals to make informed dietary decisions based on direct-from-food measurements.

3.
Plant Sci ; 327: 111565, 2023 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-36526028

RESUMEN

Jasmonic acid (JA), as an important plant hormone, can induce the synthesis of phenolic acids in Salvia miltiorrhiza Bunge, a model medicinal plant, but the specific mechanism remains to be further elucidated. JA-responsive SmMYB111 positively regulates the biosynthesis of salvianolic acid B (SalB), but the molecular mechanism is unclear. Here, we found that SmMYB111 directly binds to the promoters of SmTAT1 and SmCYP98A14 and activates their transcription. Yeast two hybrid and bimolecular fluorescent complementation assay indicated that SmMYB111 interacts with SmJAZ4. Furthermore, we systematically characterized the function of SmJAZ4, which was highly expressed in flowers and roots and located in the nucleus and cell membrane. The contents of phenolic acids in the SmJAZ4-overexpressed transgenic plantlets and SmJAZ4-overexpressed transgenic hairy roots decreased significantly. SmJAZ4 interacts with SmMYC2 or SmMYB111 to repress their transcriptional activation activity on target enzyme genes of the biosynthesis pathway of phenolic acids. Overall, the molecular mechanism of SmJAZ4-SmMYC2/SmMYB111 module participating in JA signaling regulation of SalB biosynthesis was elucidated, which give a clue for the molecular regulation of phenolic acids biosynthesis in S. miltiorrhiza.


Asunto(s)
Salvia miltiorrhiza , Salvia miltiorrhiza/genética , Salvia miltiorrhiza/metabolismo , Proteínas de Plantas/genética , Proteínas de Plantas/metabolismo , Hidroxibenzoatos/metabolismo , Raíces de Plantas/metabolismo , Regulación de la Expresión Génica de las Plantas
4.
RSC Adv ; 11(23): 13722-13730, 2021 Apr 13.
Artículo en Inglés | MEDLINE | ID: mdl-35423954

RESUMEN

Quinolines and quinoline-containing macromolecules are renowned for their valuable biological activities and excellent materials properties. Herein, we validate a general strategy for the synthesis of chloro-containing quinoline, benzoquinoline and polybenzoquinoline variants via the aza-Diels-Alder reaction. The described findings could be ultimately implemented in other synthetic pathways and may open new opportunities for analogous quinoline-derived materials.

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