MRE: a web tool to suggest foreign enzymes for the biosynthesis pathway design with competing endogenous reactions in mind
KAUST DepartmentComputational Bioscience Research Center (CBRC)
Computer Science Program
Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division
KAUST Grant NumberURF/1/1976-04
Online Publication Date2016-04-29
Print Publication Date2016-07-08
Permanent link to this recordhttp://hdl.handle.net/10754/619768
MetadataShow full item record
AbstractTo rationally design a productive heterologous biosynthesis system, it is essential to consider the suitability of foreign reactions for the specific endogenous metabolic infrastructure of a host. We developed a novel web server, called MRE, which, for a given pair of starting and desired compounds in a given chassis organism, ranks biosynthesis routes from the perspective of the integration of new reactions into the endogenous metabolic system. For each promising heterologous biosynthesis pathway, MRE suggests actual enzymes for foreign metabolic reactions and generates information on competing endogenous reactions for the consumption of metabolites. These unique, chassis-centered features distinguish MRE from existing pathway design tools and allow synthetic biologists to evaluate the design of their biosynthesis systems from a different angle. By using biosynthesis of a range of high-value natural products as a case study, we show that MRE is an effective tool to guide the design and optimization of heterologous biosynthesis pathways. The URL of MRE is http://www.cbrc.kaust.edu.sa/mre/.
CitationMRE: a web tool to suggest foreign enzymes for the biosynthesis pathway design with competing endogenous reactions in mind 2016, 44 (W1):W217 Nucleic Acids Research
SponsorsKing Abdullah University of Science and Technology (KAUST) Office of Sponsored Research (OSR) [URF/1/1976-04]. Funding for open access charge: King Abdullah University of Science and Technology (KAUST) Office of Sponsored Research (OSR) [URF/1/1976-04]. Conflict of interest statement. None declared.
PublisherOxford University Press (OUP)
JournalNucleic Acids Research
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