| Literature DB >> 7855594 |
P C Babbitt1, G T Mrachko, M S Hasson, G W Huisman, R Kolter, D Ringe, G A Petsko, G L Kenyon, J A Gerlt.
Abstract
Mandelate racemase and muconate lactonizing enzyme are structurally homologous but catalyze different reactions, each initiated by proton abstraction from carbon. The structural similarity to mandelate racemase of a previously unidentified gene product was used to deduce its function as a galactonate dehydratase. In this enzyme superfamily that has evolved to catalyze proton abstraction from carbon, three variations of homologous active site architectures are now represented: lysine and histidine bases in the active site of mandelate racemase, only a lysine base in the active site of muconate lactonizing enzyme, and only a histidine base in the active site of galactonate dehydratase. This discovery supports the hypothesis that new enzymatic activities evolve by recruitment of a protein catalyzing the same type of chemical reaction.Entities:
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Year: 1995 PMID: 7855594 DOI: 10.1126/science.7855594
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728