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• W2903712029 startingPage "2888" @default.
• W2903712029 abstract "The development of biosensors for in vitro quantification of small molecules such as metabolites or man-made chemicals is still a major challenge. Here we show that engineered variants of the sensory PAS domain of the histidine kinase CitA of the thermophilic bacterium Geobacillus thermoleovorans represent promising alternatives to established biorecognition elements. By combining binding site grafting and rational design we constructed protein variants binding l-malate, ethylmalonate, or the aromatic compound phthalate instead of the native ligand citrate. Due to more favorable entropy contributions, the wild-type protein and its engineered variants exhibited increased (nano- to micromolar) affinities and improved enantioselectivity compared to CitA homologues of mesophilic organisms. Ligand binding was directly converted into an optical signal that was preserved after immobilization of the protein. A fluorescently labeled variant was used to quantify ethylmalonate, an urinary biomarker for ethylmalonic encephalopathy, in synthetic urine, thereby demonstrating the applicability of the sensor in complex samples." @default.
• W2903712029 created "2018-12-22" @default.
• W2903712029 creator A5044135416 @default.
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• W2903712029 creator A5070950997 @default.
• W2903712029 date "2018-12-21" @default.
• W2903712029 modified "2023-10-14" @default.
• W2903712029 title "Structure-Based Design of Versatile Biosensors for Small Molecules Based on the PAS Domain of a Thermophilic Histidine Kinase." @default.
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• W2903712029 doi "https://doi.org/10.1021/acssynbio.8b00348" @default.
• W2903712029 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30525476" @default.
• W2903712029 hasPublicationYear "2018" @default.
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