PMID:9772162
| Citation |
Hubbard, BK, Koch, M, Palmer, DR, Babbitt, PC and Gerlt, JA (1998) Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli. Biochemistry 37:14369-75 |
|---|---|
| Abstract |
The genes encoding the enzymes in the (D)-glucarate/galactarate catabolic pathway have been identified in the Escherichia coli genome. These encode, in three transcriptional units, (D)-glucarate dehydratase (GlucD), galactarate dehydratase, 5-keto-4-deoxy-(D)-glucarate aldolase, tartronate semialdehyde reductase, a glycerate kinase that generates 2-phosphoglycerate as product, and two hexaric acid transporters. We also have identified a gene proximal to that encoding GlucD that encodes a protein that is 72% identical in primary sequence to GlucD (GlucD-related protein or GlucDRP). However, whereas GlucD catalyzes the efficient dehydration of both (D)-glucarate and (L)-idarate as well as their epimerization, GlucDRP is significantly impaired in both reactions. Perhaps GlucDRP is an example of gene duplication and evolution in progress in the E. coli chromosome. |
| Links |
PubMed Online version:10.1021/bi981124f |
| Keywords |
Alcohol Oxidoreductases/chemistry; Alcohol Oxidoreductases/genetics; Aldehyde-Lyases/chemistry; Aldehyde-Lyases/genetics; Aldehyde-Lyases/isolation & purification; Amino Acid Sequence; Enzyme Activation; Escherichia coli/enzymology; Escherichia coli Proteins; Evolution, Molecular; Glucaric Acid/chemistry; Glucaric Acid/metabolism; Hydro-Lyases/chemistry; Hydro-Lyases/genetics; Hydro-Lyases/isolation & purification; Molecular Sequence Data; Operon; Phosphopyruvate Hydratase/chemistry; Phosphotransferases (Alcohol Group Acceptor)/chemistry; Phosphotransferases (Alcohol Group Acceptor)/genetics; Sequence Homology, Amino Acid; Sugar Acids/chemistry; Sugar Acids/metabolism |
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