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http://purl.uniprot.org/citations/28497697http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28497697http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28497697http://www.w3.org/2000/01/rdf-schema#comment"Eukaryotic biochemistry is organized throughout the cell in and on membrane-bound organelles. When engineering metabolic pathways this organization is often lost, resulting in flux imbalance and a loss of kinetic advantages from enzyme colocalization and substrate channeling. Here, we develop a protein-based scaffold for colocalizing multienzyme pathways on the membranes of intracellular lipid droplets. Scaffolds based on the plant lipid droplet protein oleosin and cohesin-dockerin interaction pairs recruited upstream enzymes in yeast ester biosynthesis to the native localization of the terminal reaction step, alcohol-O-acetyltransferase (Atf1). The native localization is necessary for high activity and pathway assembly in close proximity to Atf1 increased pathway flux. Screening a library of scaffold variants further showed that pathway structure can alter catalysis and revealed an optimized scaffold and pathway expression levels that produced ethyl acetate at a rate nearly 2-fold greater than unstructured pathways. This strategy should prove useful in spatially organizing other metabolic pathways with key lipid droplet-localized and membrane-bound reaction steps."xsd:string
http://purl.uniprot.org/citations/28497697http://purl.org/dc/terms/identifier"doi:10.1021/acssynbio.7b00041"xsd:string
http://purl.uniprot.org/citations/28497697http://purl.org/dc/terms/identifier"doi:10.1021/acssynbio.7b00041"xsd:string
http://purl.uniprot.org/citations/28497697http://purl.uniprot.org/core/author"Zhu J."xsd:string
http://purl.uniprot.org/citations/28497697http://purl.uniprot.org/core/author"Zhu J."xsd:string
http://purl.uniprot.org/citations/28497697http://purl.uniprot.org/core/author"Lin J.L."xsd:string
http://purl.uniprot.org/citations/28497697http://purl.uniprot.org/core/author"Lin J.L."xsd:string
http://purl.uniprot.org/citations/28497697http://purl.uniprot.org/core/author"Wheeldon I."xsd:string
http://purl.uniprot.org/citations/28497697http://purl.uniprot.org/core/author"Wheeldon I."xsd:string
http://purl.uniprot.org/citations/28497697http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28497697http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28497697http://purl.uniprot.org/core/name"ACS Synth. Biol."xsd:string
http://purl.uniprot.org/citations/28497697http://purl.uniprot.org/core/name"ACS Synth. Biol."xsd:string
http://purl.uniprot.org/citations/28497697http://purl.uniprot.org/core/pages"1534-1544"xsd:string
http://purl.uniprot.org/citations/28497697http://purl.uniprot.org/core/pages"1534-1544"xsd:string
http://purl.uniprot.org/citations/28497697http://purl.uniprot.org/core/title"Synthetic Protein Scaffolds for Biosynthetic Pathway Colocalization on Lipid Droplet Membranes."xsd:string
http://purl.uniprot.org/citations/28497697http://purl.uniprot.org/core/title"Synthetic Protein Scaffolds for Biosynthetic Pathway Colocalization on Lipid Droplet Membranes."xsd:string
http://purl.uniprot.org/citations/28497697http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/28497697http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/28497697http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28497697
http://purl.uniprot.org/citations/28497697http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28497697
http://purl.uniprot.org/citations/28497697http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/28497697
http://purl.uniprot.org/citations/28497697http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/28497697