scholarly journals Correction to: Amorpha-4,11-diene synthase: a key enzyme in artemisinin biosynthesis and engineering

aBIOTECH ◽  
2021 ◽  
Author(s):  
Jin Quan Huang ◽  
Xin Fang
Keyword(s):  
Key Enzyme ◽  
Artemisinin Biosynthesis

Cyclization Mechanism of Amorpha-4,11-diene Synthase, a Key Enzyme in Artemisinin Biosynthesis

2006 ◽  
Vol 69 (5) ◽  
pp. 758-762 ◽  
Author(s):  
Soon-Hee Kim ◽  
Keon Heo ◽  
Yung-Jin Chang ◽  
Si-Hyung Park ◽  
Sang-Ki Rhee ◽  
...  
Keyword(s):  
Key Enzyme ◽  
Artemisinin Biosynthesis

scholarly journals SUB-CLONING OF GENES ENCODINGCYTHOCHROME P450 MONOOXYGENASE (CYP71AVI) INTOEXPRESSION VECTOR IN ESCHERICHIA COLI

2017 ◽  
Vol 10 (14) ◽  
pp. 69
Author(s):  
Imam Adi Wicaksono ◽  
Tresna Lestari ◽  
Evi Umayah Ulfa ◽  
Catur Riani ◽  
Elfahmi Elfahmi
Keyword(s):  
Escherichia Coli ◽  
Restriction Site ◽  
Restriction Analysis ◽  
Sequencing Analysis ◽  
Gene Encoding ◽  
P450 Monooxygenase ◽  
Recombinant Vector ◽  
Sds Page ◽  
Key Enzyme ◽  
Artemisinin Biosynthesis

Objective: Cytochrome P450 monooxygenase (CYP71AVI) is a key enzyme involved in the artemisinin biosynthesis pathway.In this research, sub-cloning gene encoding CYP71AVI into pETDUET1 vector in Escherichia coli has been done and then the expression products characterized with SDS-PAGE.Methods: Gene construction started with sub-cloning of cyp71avi gene from pJexpress401_cyp into pETDUET1 through restriction site NdeI and XhoI to get pETDUET1_cyp. Overproduction of CYP71AVI at temperature 37 °C has conducted by IPTG induction.Results: Confirmation of the recombinant vector pETDUET1_cyp was done by migration, restriction site and sequencing analysis. The result of pETDUET1_cyp restriction analysis with XhoI restriction enzyme showed one DNA band with experimental size 6585 bp.The CYP71AVI protein has been produced and characterized with SDS-PAGE method. Based on experimental calculation from SDS-PAGE analysis obtained molecular weight of CYP71AVI band was 57.55 kDa.Conclusion: Construction of gene encoding CYP71AVI into pETDUET1 as the co-expression vector in Escherichia colihas been succesfully and confirmed by migration, restriction site and sequencing analysis. The result of overproduction showed protein bands on SDS-PAGE analysis indicated as CYP71AVI. 

scholarly journals Overexpression ofAaWRKY1Leads to an Enhanced Content of Artemisinin inArtemisia annua

2016 ◽  
Vol 2016 ◽  
pp. 1-9 ◽  
Author(s):  
Weimin Jiang ◽  
Xueqing Fu ◽  
Qifang Pan ◽  
Yueli Tang ◽  
Qian Shen ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Transgenic Plants ◽  
Biosynthetic Pathway ◽  
High Expression ◽  
35S Promoter ◽  
Key Enzymes ◽  
Key Enzyme ◽  
Effective Component ◽  
Artemisinin Biosynthesis ◽  
Insight Into

Artemisinin is an effective component of drugs against malaria. The regulation of artemisinin biosynthesis is at the forefront of artemisinin research. Previous studies showed that AaWRKY1 can regulate the expression ofADS, which is the first key enzyme in artemisinin biosynthetic pathway. In this study,AaWRKY1was cloned, and it activated ADSpro and CYPpro in tobacco using dual-LUC assay. To further study the function of AaWRKY1, pCAMBIA2300-AaWRKY1 construct under 35S promoter was generated. Transgenic plants containingAaWRKY1were obtained, and four independent lines with high expression ofAaWRKY1were analyzed. The expression ofADSandCYP, the key enzymes in artemisinin biosynthetic pathway, was dramatically increased inAaWRKY1-overexpressingA. annuaplants. Furthermore, the artemisinin yield increased significantly inAaWRKY1-overexpressingA. annuaplants. These results showed that AaWRKY1 increased the content of artemisinin by regulating the expression of bothADSandCYP. It provides a new insight into the mechanism of regulation on artemisinin biosynthesis via transcription factors in the future.

Molecular Cloning, Expression, and Characterization of Amorpha-4,11-diene Synthase, a Key Enzyme of Artemisinin Biosynthesis in Artemisia annua L.

2000 ◽  
Vol 381 (2) ◽  
pp. 173-180 ◽  
Author(s):  
Per Mercke ◽  
Marie Bengtsson ◽  
Harro J. Bouwmeester ◽  
Maarten A. Posthumus ◽  
Peter E. Brodelius
Keyword(s):  
Molecular Cloning ◽  
Artemisia Annua ◽  
Artemisia Annua L ◽  
Key Enzyme ◽  
Artemisinin Biosynthesis

scholarly journals Amorpha-4,11-diene synthase: a key enzyme in artemisinin biosynthesis and engineering

aBIOTECH ◽  
2021 ◽  
Author(s):  
Jing-Quan Huang ◽  
Xin Fang
Keyword(s):  
Metabolic Engineering ◽  
Synthetic Biology ◽  
Biosynthetic Pathway ◽  
Catalytic Mechanism ◽  
Artemisia Annua ◽  
New Techniques ◽  
Key Enzyme ◽  
Substrate Promiscuity ◽  
Artemisinin Biosynthesis

AbstractAmorpha-4,11-diene synthase (ADS) catalyzes the first committed step in the artemisinin biosynthetic pathway, which is the first catalytic reaction enzymatically and genetically characterized in artemisinin biosynthesis. The advent of ADS in Artemisia annua is considered crucial for the emergence of the specialized artemisinin biosynthetic pathway in the species. Microbial production of amorpha-4,11-diene is a breakthrough in metabolic engineering and synthetic biology. Recently, numerous new techniques have been used in ADS engineering; for example, assessing the substrate promiscuity of ADS to chemoenzymatically produce artemisinin. In this review, we discuss the discovery and catalytic mechanism of ADS, its application in metabolic engineering and synthetic biology, as well as the role of sesquiterpene synthases in the evolutionary origin of artemisinin.

Tryptophan-Niacin Metabolism in Rat with Puromycin Aminonucleoside-Induced Nephrosis

2006 ◽  
Vol 76 (1) ◽  
pp. 28-33 ◽  
Author(s):  
Yukari Egashira ◽  
Shin Nagaki ◽  
Hiroo Sanada
Keyword(s):  
Body Weight ◽  
Urinary Excretion ◽  
Enzyme Activities ◽  
Treated Group ◽  
Control Group ◽  
Puromycin Aminonucleoside ◽  
Low Level ◽  
Key Enzyme

We investigated the change of tryptophan-niacin metabolism in rats with puromycin aminonucleoside PAN-induced nephrosis, the mechanisms responsible for their change of urinary excretion of nicotinamide and its metabolites, and the role of the kidney in tryptophan-niacin conversion. PAN-treated rats were intraperitoneally injected once with a 1.0% (w/v) solution of PAN at a dose of 100 mg/kg body weight. The collection of 24-hour urine was conducted 8 days after PAN injection. Daily urinary excretion of nicotinamide and its metabolites, liver and blood NAD, and key enzyme activities of tryptophan-niacin metabolism were determined. In PAN-treated rats, the sum of urinary excretion of nicotinamide and its metabolites was significantly lower compared with controls. The kidneyα-amino-β-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD) activity in the PAN-treated group was significantly decreased by 50%, compared with the control group. Although kidney ACMSD activity was reduced, the conversion of tryptophan to niacin tended to be lower in the PAN-treated rats. A decrease in urinary excretion of niacin and the conversion of tryptophan to niacin in nephrotic rats may contribute to a low level of blood tryptophan. The role of kidney ACMSD activity may be minimal concerning tryptophan-niacin conversion under this experimental condition.

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