PMID:9818186
| Citation |
Gerlt, JA and Babbitt, PC (1998) Mechanistically diverse enzyme superfamilies: the importance of chemistry in the evolution of catalysis. Curr Opin Chem Biol 2:607-12 |
|---|---|
| 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. |
| Links | |
| Keywords |
Amidohydrolases/chemistry; Amidohydrolases/classification; Amidohydrolases/genetics; Bacterial Proteins; Biological Evolution; Catalysis; Enoyl-CoA Hydratase/chemistry; Enoyl-CoA Hydratase/classification; Enoyl-CoA Hydratase/genetics; Glutathione Transferase/chemistry; Glutathione Transferase/classification; Glutathione Transferase/genetics; Lactoylglutathione Lyase/chemistry; Lactoylglutathione Lyase/classification; Lactoylglutathione Lyase/genetics; Metalloproteins/chemistry; Metalloproteins/classification; Metalloproteins/genetics; Oxygenases/chemistry; Oxygenases/classification; Oxygenases/genetics; Phosphopyruvate Hydratase/chemistry; Phosphopyruvate Hydratase/classification; Phosphopyruvate Hydratase/genetics |
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