Cloning, characterization, and enzymatic identification of a new tryptophan decarboxylase from <i>Ophiorrhiza pumila</i>

You, Dawei; Feng, Yue; Wang, Can; Sun, Chengtao; Wang, Yao; Zhao, Degang; Kai, Guoyin

doi:10.1002/bab.1935

Cited by 17 publications

(11 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…L-tryptophan decarboxylase (TDC) is a cytosolic type-II aromatic l -amino acid decarboxylase [ [53] , [54] , [55] , [56] , [57] ]. It catalyzes the final step in the microbial pathway of serotonin synthesis.…”

Section: Synthesis and Modification Pathways Of Melatonin In Microorganismsmentioning

confidence: 99%

Melatonin biosynthesis pathways in nature and its production in engineered microorganisms

Xie

Ding

Bai

et al. 2022

Synthetic and Systems Biotechnology

View full text Add to dashboard Cite

Melatonin is a biogenic amine that can be found in plants, animals and microorganism. The metabolic pathway of melatonin is different in various organisms, and biosynthetic endogenous melatonin acts as a molecular signal and antioxidant protection against external stress. Microbial synthesis pathways of melatonin are similar to those of animals but different from those of plants. At present, the method of using microorganism fermentation to produce melatonin is gradually prevailing, and exploring the biosynthetic pathway of melatonin to modify microorganism is becoming the mainstream, which has more advantages than traditional chemical synthesis. Here, we review recent advances in the synthesis, optimization of melatonin pathway. l -tryptophan is one of the two crucial precursors for the synthesis of melatonin, which can be produced through a four-step reaction. Enzymes involved in melatonin synthesis have low specificity and catalytic efficiency. Site-directed mutation, directed evolution or promotion of cofactor synthesis can enhance enzyme activity and increase the metabolic flow to promote microbial melatonin production. On the whole, the status and bottleneck of melatonin biosynthesis can be improved to a higher level, providing an effective reference for future microbial modification.

show abstract

Section: Synthesis and Modification Pathways Of Melatonin In Microorganismsmentioning

confidence: 99%

Melatonin biosynthesis pathways in nature and its production in engineered microorganisms

Xie

Ding

Bai

et al. 2022

Synthetic and Systems Biotechnology

View full text Add to dashboard Cite

show abstract

“…O. pumila has been considered to be a valuable alternative source of camptothecin (CPT), which is widely used to treat various cancers, such as colorectal, ovarian and lung cancer [ 9 , 10 ]. Studies refer to the biosynthesis process of CPT in O. pumila are decumulating [ 8 , 11 , 12 ], but the function of O. pumila compounds in cancer have rarely been explored. Previously, we reported that treatment with O. pumila extract (OPE) suppresses the proliferation and migration of liver cancer cells, indicating an anti-cancer activity of OPE in hepatocarcinoma [ 13 ].…”

Section: Introductionmentioning

confidence: 99%

In vitro and in vivo anti-lymphoma effects of Ophiorrhiza pumila extract

Fan

Liao

Chen

et al. 2022

Aging

View full text Add to dashboard Cite

Background: Current therapeutic strategies on patients with lymphomas remains limited. Previously we found the suppressive effect of Ophiorrhiza pumila (OPE) on hepatocarcinoma. In present study, the effect of OPE on lymphoma in vitro and in vivo were investigated. Methods: CCK-8 assay was applied to detect the effect of OPE on cell proliferation. Flow cytometry was used to analyze the effect of OPE on cell cycle distribution and apoptosis. Xenograft mouse model was conducted to determine the anti-tumor activity of OPE. TNUEL assay was performed to detect the apoptosis in tumor tissues. Western blot and immuno-histochemistry were used to determine protein expression. Results: In vitro tests indicate that OPE suppressed A20 cell proliferation in a dose- and time-dependent manner. OPE treatment induced cell cycle arrest at S phase and elevated apoptosis in A20 cells. OPE displayed a significant inhibition in tumor growth in a mouse xenograft model. OPE promoted apoptosis of tumor cell in the mouse model Cleaved caspase 3 expression and Bax/Bcl2 ratio were also enhanced. In addition, OPE suppressed A20 cell viability partially by reducing phosphorylation of EGFR. Conclusions: Our data showed that OPE suppressed the proliferation of lymphoma cells and promoted apoptosis in vitro and in vivo , which might be partially mediated by inactivating EGFR signaling.

show abstract

“…Aromatic amino acid decarboxylases (AAADs) play important roles in the key step of 5-HTP conversion to 5-HT. Previously, tryptophan decarboxylase (TDC) was regarded as an enzyme that catalyses non-speci c reactions in L-trp or 5-HTP (prefer to L-trp), with the result that a one-pot cascade reaction cannot be performed and has therefore never been reported [10,11]. Dopa decarboxylase (DDC), another AAAD, is able to convert L-dopa to dopamine [12].…”

Section: Introductionmentioning

confidence: 99%

Construction of Cell Factory Capable of Efficiently Converting L-tryptophan Into 5-hydroxytryptamine

Wang

Chen

et al. 2021

Preprint

View full text Add to dashboard Cite

Background: L-Tryptophan (L-trp) derivatives such as 5-hydroxytryptophan (5-HTP) and 5-hydroxytryptamine (5-HT), N-Acetyl-5-hydroxytryptamine and melatonin are important molecules with pharmaceutical interest. Among, 5-HT is an inhibitory neurotransmitter with proven benefits for treating the symptoms of depression. At present, 5-HT depends on plant extraction and chemical synthesis, which limits its mass production and causes environmental problems. Therefore, it is necessary to develop an efficient, green and sustainable biosynthesis method to produce 5-HT.Results: Here we propose a one-pot production of 5-HT from L-trp via two enzyme cascades for the first time. First, a chassis cell that can convert L-trp into 5-HTP was constructed by heterologous expression of tryptophan hydroxylase from Schistosoma mansoni (SmTPH) and an artificial endogenous BH4 module. Then, dopa decarboxylase from Harminia axyridis (HaDDC), which can specifically catalyse 5-HTP to 5-HT, was used for 5-HT production. The cell factory, E. coli BL21(DE3)△tnaA/BH4/HaDDC-SmTPH, which contains SmTPH and HaDDC, was constructed for 5-HT synthesis. The highest concentration of 5-HT reached 414.5 ± 1.6 mg/L (with conversion rate of 43 mol%) at the optimal conditions (induced temperature, 25℃; IPTG concentration, 0.5 mM; catalysis temperature, 30℃; catalysis time, 72 h). Conclusions: This protocol provided an efficient one-pot method for converting L-trp into 5-HT production, which opens up possibilities for the practical biosynthesis of natural 5-HT at an industrial scale.

show abstract

Cloning, characterization, and enzymatic identification of a new tryptophan decarboxylase from Ophiorrhiza pumila

Cited by 17 publications

References 33 publications

Melatonin biosynthesis pathways in nature and its production in engineered microorganisms

Melatonin biosynthesis pathways in nature and its production in engineered microorganisms

In vitro and in vivo anti-lymphoma effects of Ophiorrhiza pumila extract

Construction of Cell Factory Capable of Efficiently Converting L-tryptophan Into 5-hydroxytryptamine

Contact Info

Product

Resources

About