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High-throughput sel...
High-throughput selection of (new) enzymes : phage display-mediated isolation of alkyl halide hydrolases from a library of active-site mutated epoxide hydrolases
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- Blazic, Marija (författare)
- Uppsala universitet,Biokemi
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- Gautier, Candice (författare)
- Uppsala universitet,Biokemi
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- Norberg, Thomas, 1948- (författare)
- Uppsala universitet,Institutionen för kemi - BMC
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- Widersten, Mikael (författare)
- Uppsala universitet,Biokemi
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(creator_code:org_t)
- 2024
- 2024
- Engelska.
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Ingår i: Faraday discussions. - : Royal Society of Chemistry. - 1359-6640 .- 1364-5498.
- Relaterad länk:
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https://doi.org/10.1...
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https://uu.diva-port... (primary) (Raw object)
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Epoxide hydrolase StEH1, from potato, is similar in overall structural fold and catalytic mechanism to haloalkane dehalogenase DhlA from Xanthobacter autotrophicus. StEH1 displays low (promiscuous) hydrolytic activity with (2-chloro)- and (2-bromo)ethanebenzene producing 2-phenylethanol. To investigate possibilities to amplify these very low dehalogenase activities, StEH1 was subjected to targeted randomized mutagenesis at five active-site amino acid residues and the resulting protein library was challenged for reactivity towards a bait chloride substrate. Enzymes catalyzing the first half-reaction of a hydrolytic cycle were isolated following monovalent phage display of the mutated proteins. Several StEH1 derived enzymes were identified with enhanced dehalogenase activities.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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