By a News Reporter-Staff News Editor at Biotech Week -- A new study on Proteobacteria is now available. According to news reporting out of Logan, Utah, by NewsRx editors, research stated, "Phenylalanine ammonia-lyase (PAL) is an important enzyme that links primary metabolism to secondary metabolism. Its efficiency is often a critical factor that affects the overall flux of a related metabolic pathway, the titer of the final products, and the efficacy of PAL-based therapies."
Our news journalists obtained a quote from the research from Utah State University, "Thus, PAL is a common target for metabolic engineering, and it is of significant interest to screen efficient PALs for industrial and medical applications. In this study, a novel and efficient visible reporter assay for screening of PAL efficiency in Escherichia coli was established based on a plant type III polyketide biosynthetic pathway. The candidate PALs were co-expressed with a 4-coumarate:CoA ligase 4CL1 from Arabidopsis thaliana and curcuminoid synthase (CUS) from Oryza sativa in E. coli BL21(DE3) to form a dicinnamoylmethane biosynthetic pathway. Taking advantage of the yellow color of the product, a microplate-based assay was designed to measure the titer of dicinnamoylmethane, which was validated by HPLC analysis. The different titers of the product reflect the overall performance (expression level and enzymatic activity) of the individual PALs in E. coli. Using this system, we have screened three PALs (PAL1, PAL3, and PAL4) from Trifolium pratense, among which PAL1 showed the best performance in E. coli. The engineered E. coli strain containing PAL1, 4CL1, and CUS led to the production of dicinnamoylmethane at a high level of 0.36 g/l."
According to the news editors, the research concluded: "Supplement of 2-fluoro-phenylalanine yielded two fluorinated dicinnamoylmethane derivatives, 6,6'-difluoro-dicinnamoylmethane and 6-fluoro-dicinnamoylmethane, of which the latter is a new curcuminoid."
For more information on this research see: Design and application of an in vivo reporter assay for phenylalanine ammonia-lyase. Applied Microbiology and Biotechnology, 2013;97(17):7877-7885. Applied Microbiology and Biotechnology can be contacted at: Springer, 233 Spring St, New York, NY 10013, USA. (Springer - www.springer.com; Applied Microbiology and Biotechnology - www.springerlink.com/content/0175-7598/)
Our news journalists report that additional information may be obtained by contacting S.Y. Wang, Utah State University, Dept. of Biol Engn, Logan, UT 84322, United States. Additional authors for this research include S.W. Zhang, T. Zhou, J. Zeng and J.X. Zhan (see also Proteobacteria).
Keywords for this news article include: Utah, Logan, Escherichia, United States, Phenylalanine, Ammonia Lyases, Enterobacteriaceae, Nitrogen Compounds, Gammaproteobacteria, Aromatic Amino Acids, Enzymes and Coenzymes, Essential Amino Acids, Carbon-Nitrogen Lyases, North and Central America
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