A Completely De Novo ATPase from Combinatorial Protein Design

A Completely De Novo ATPase from Combinatorial Protein Design

Our understanding of biological chemistry is shaped by the observation that all life comes from other lifeas Pasteur put it, omne vivum ex vivo. A key step in expanding our biochemical vocabulary is to recapitulate biogenic catalysis using non-natural sequences that did not arise from common ancest...

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Veröffentlicht in:Journal of the American Chemical Society 2020-09, Vol.142 (36), p.15230-15234
Hauptverfasser: Wang, Michael S, Hecht, Michael H
Format: Artikel
Sprache:eng
Schlagworte:
Adenosine Triphosphatases - chemical synthesis
Adenosine Triphosphatases - chemistry
Adenosine Triphosphatases - metabolism
Adenosine Triphosphate - chemistry
Adenosine Triphosphate - metabolism
Combinatorial Chemistry Techniques
Hydrolysis
Magnesium - pharmacology
Models, Molecular
Molecular Structure
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Zusammenfassung:Our understanding of biological chemistry is shaped by the observation that all life comes from other lifeas Pasteur put it, omne vivum ex vivo. A key step in expanding our biochemical vocabulary is to recapitulate biogenic catalysis using non-natural sequences that did not arise from common ancestry. Here we describe an enzyme designed completely de novo that hydrolyzes ATP. This protein was designed to lack β-sheet structure and is competitively inhibited by magnesium, two traits that are unlike natural ATPases.
ISSN:0002-7863
1520-5126
DOI:10.1021/jacs.0c02954