Biosynthesis of a Therapeutically Important Nicotinamide Mononucleotide through a Phosphoribosyl Pyrophosphate Synthetase 1 and 2 Engineered Strain of Escherichia coli

2021 ◽  
Author(s):  
Anoth Maharjan ◽  
Mamata Singhvi ◽  
Beom Soo Kim
Keyword(s):  
Escherichia Coli ◽  
Phosphoribosyl Pyrophosphate ◽  
Nicotinamide Mononucleotide ◽  
Phosphoribosyl Pyrophosphate Synthetase ◽  
Engineered Strain

scholarly journals Creating enzymes and self-sufficient cells for biosynthesis of the non-natural cofactor nicotinamide cytosine dinucleotide

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Xueying Wang ◽  
Yanbin Feng ◽  
Xiaojia Guo ◽  
Qian Wang ◽  
Siyang Ning ◽  
...  
Keyword(s):  
Biological Sciences ◽  
Escherichia Coli ◽  
Nicotinamide Adenine Dinucleotide ◽  
Chemical Biology ◽  
Reduced Form ◽  
Redox Transformations ◽  
Nicotinamide Mononucleotide ◽  
Self Sufficiency ◽  
Binding Pockets ◽  
Pathway Regulation

AbstractNicotinamide adenine dinucleotide (NAD) and its reduced form are indispensable cofactors in life. Diverse NAD mimics have been developed for applications in chemical and biological sciences. Nicotinamide cytosine dinucleotide (NCD) has emerged as a non-natural cofactor to mediate redox transformations, while cells are fed with chemically synthesized NCD. Here, we create NCD synthetase (NcdS) by reprograming the substrate binding pockets of nicotinic acid mononucleotide (NaMN) adenylyltransferase to favor cytidine triphosphate and nicotinamide mononucleotide over their regular substrates ATP and NaMN, respectively. Overexpression of NcdS alone in the model host Escherichia coli facilitated intracellular production of NCD, and higher NCD levels up to 5.0 mM were achieved upon further pathway regulation. Finally, the non-natural cofactor self-sufficiency was confirmed by mediating an NCD-linked metabolic circuit to convert L-malate into D-lactate. NcdS together with NCD-linked enzymes offer unique tools and opportunities for intriguing studies in chemical biology and synthetic biology.

5-Phosphoribosyl pyrophosphate synthetase from Ehrlich ascites tumor cells

Biochemistry ◽  
1969 ◽  
Vol 8 (4) ◽  
pp. 1608-1614 ◽  
Author(s):  
P. C. L. Wong ◽  
Andrew W. Murray
Keyword(s):  
Tumor Cells ◽  
Ehrlich Ascites Tumor ◽  
Ehrlich Ascites Tumor Cells ◽  
Ascites Tumor ◽  
Phosphoribosyl Pyrophosphate ◽  
Ehrlich Ascites ◽  
Phosphoribosyl Pyrophosphate Synthetase

scholarly journals Identification of the Escherichia coliNicotinic Acid Mononucleotide Adenylyltransferase Gene

2000 ◽  
Vol 182 (15) ◽  
pp. 4372-4374 ◽  
Author(s):  
Ryan A. Mehl ◽  
Cynthia Kinsland ◽  
Tadhg P. Begley
Keyword(s):  
Escherichia Coli ◽  
Product Inhibition ◽  
Biosynthetic Enzyme ◽  
Nicotinamide Mononucleotide

ABSTRACT The gene (ybeN) coding for nicotinate mononucleotide adenylyltransferase, an NAD(P) biosynthetic enzyme, has been identified and overexpressed in Escherichia coli. This enzyme catalyzes the reversible adenylation of nicotinate mononucleotide and shows product inhibition. The rate of adenylation of nicotinate mononucleotide is at least 20 times faster than the rate of adenylation of nicotinamide mononucleotide.

scholarly journals 87 NAD SYNTHESIS BY ERYTHROCYTES IN PHOSPHORIBOSYL -PYROPHOSPHATE SYNTHETASE (PPRPs) SUPERACTIVITY

1988 ◽  
Vol 24 (1) ◽  
pp. 125-125
Author(s):  
Vanna Micheli ◽  
H Anne Simmonds
Keyword(s):  
Phosphoribosyl Pyrophosphate ◽  
Nad Synthesis ◽  
Phosphoribosyl Pyrophosphate Synthetase

A direct, stimulating effect of cyclic GMP on purified phosphoribosyl pyrophosphate synthetase and its antagonism by cyclic AMP

Cell ◽  
1974 ◽  
Vol 2 (4) ◽  
pp. 241-245 ◽  
Author(s):  
Christopher D. Green ◽  
David W. Martin
Keyword(s):  
Cyclic Amp ◽  
Cyclic Gmp ◽  
Phosphoribosyl Pyrophosphate ◽  
Phosphoribosyl Pyrophosphate Synthetase

scholarly journals Biodegradation of p-nitrophenol by engineered strain

AMB Express ◽  
2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Jing Xu ◽  
Bo Wang ◽  
Wen-hui Zhang ◽  
Fu-Jian Zhang ◽  
Yong-dong Deng ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Health Risks ◽  
Aromatic Hydrocarbons ◽  
Environmental Pollutant ◽  
Toxic Substances ◽  
High Tolerance ◽  
Rapid Degradation ◽  
Degradation Ability ◽  
Engineered Strain ◽  
Functional Strain

Abstractp-Nitrophenol (PNP) is an important environmental pollutant and can causes significant environmental and health risks. Compared with the traditional methods, biodegradation is a useful one to completely remove the harmful pollutants from the environment. Here, an engineered strain was first constructed by introducing PNP biodegradation pathway via the hydroquinone (HQ) pathway into Escherichia coli. In the engineered strain BL-PNP, PNP was completely degraded to β-ketoadipate and subsequently enter the metabolites of multiple anabolic pathways. The high tolerance and rapid degradation ability to PNP enable the engineered strain to have the potential to degrade toxic substances. The engineered strain created in this study can be used as a functional strain for bioremediation of PNP and potential toxic intermediates, and the method of assembling aromatic hydrocarbons metabolic pathway can be used to eradicate nitroaromatic pollutants in the environment.

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