PMID:7855594
| Citation |
Babbitt, PC, Mrachko, GT, Hasson, MS, Huisman, GW, Kolter, R, Ringe, D, Petsko, GA, Kenyon, GL and Gerlt, JA (1995) A functionally diverse enzyme superfamily that abstracts the alpha protons of carboxylic acids. Science 267:1159-61 |
|---|---|
| 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. |
| Links | |
| Keywords |
Amino Acid Sequence; Base Sequence; Binding Sites; Histidine/metabolism; Hydro-Lyases/chemistry; Hydro-Lyases/genetics; Hydro-Lyases/metabolism; Intramolecular Lyases; Isomerases/chemistry; Isomerases/metabolism; Lysine/metabolism; Molecular Sequence Data; Open Reading Frames; Operon; Protons; Pseudomonas putida/enzymology; Pseudomonas putida/genetics; Racemases and Epimerases/chemistry; Racemases and Epimerases/metabolism |
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