Abstract
The strategy that nature has used to evolve new catalytic activities from pre-existing enzymes (i.e. retention of substrate binding or of catalytic mechanism) has been controversial. Recent work supports a strategy in which a partial reaction, catalyzed by a progenitor, is retained, and the active-site architecture is modified to allow the intermediate generated to be directed to different products.
Publication types
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Amidohydrolases / chemistry*
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Amidohydrolases / classification
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Amidohydrolases / genetics
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Bacterial Proteins*
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Biological Evolution*
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Catalysis*
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Enoyl-CoA Hydratase / chemistry*
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Enoyl-CoA Hydratase / classification
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Enoyl-CoA Hydratase / genetics
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Glutathione Transferase / chemistry
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Glutathione Transferase / classification
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Glutathione Transferase / genetics
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Lactoylglutathione Lyase / chemistry
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Lactoylglutathione Lyase / classification
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Lactoylglutathione Lyase / genetics
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Metalloproteins / chemistry
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Metalloproteins / classification
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Metalloproteins / genetics
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Oxygenases / chemistry
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Oxygenases / classification
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Oxygenases / genetics
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Phosphopyruvate Hydratase / chemistry*
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Phosphopyruvate Hydratase / classification
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Phosphopyruvate Hydratase / genetics
Substances
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Bacterial Proteins
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Metalloproteins
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Oxygenases
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Glutathione Transferase
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Amidohydrolases
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Phosphopyruvate Hydratase
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Enoyl-CoA Hydratase
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Lactoylglutathione Lyase