Heavy Enzymes and the Rational Redesign of Protein Catalysts
Abstract: An unsolved mystery in biology concerns the link between enzyme catalysis and protein motions. Comparison between isotopically labelled “heavy” dihydrofolate reductases and their natural‐abundance counterparts has suggested that the coupling of protein motions to the chemistry of the catalysed reaction is minimised in the case of hydride transfer. In alcohol dehydrogenases, unnatural, bulky substrates that induce additional electrostatic rearrangements of the active site enhance coupled motions. This finding could provide a new route to engineering enzymes with altered substrate specificity, because amino acid residues responsible for dynamic coupling with a given substrate present as hotspots for mutagenesis. Detailed understanding of the biophysics of enzyme catalysis based on insights gained from analysis of “heavy” enzymes might eventually allow routine engineering of enzymes to catalyse reactions of choice.
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Erschienen in
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Heavy Enzymes and the Rational Redesign of Protein Catalysts ; volume:20 ; number:22 ; year:2019 ; pages:2807-2812 ; extent:6
ChemBioChem ; 20, Heft 22 (2019), 2807-2812 (gesamt 6)
- Urheber
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Scott, Alan F.
Luk, Louis Y.‐P.
Tuñón, Iñaki
Moliner, Vicent
Allemann, Rudolf K.
- DOI
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10.1002/cbic.201900134
- URN
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urn:nbn:de:101:1-2022071408155486675993
- Rechteinformation
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
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15.08.2025, 07:34 MESZ
Datenpartner
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Scott, Alan F.
- Luk, Louis Y.‐P.
- Tuñón, Iñaki
- Moliner, Vicent
- Allemann, Rudolf K.
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