InterPro domain: IPR013342

Mandelate racemase 5.1.2.2 (MR) and muconate lactonising enzyme 5.5.1.1 (MLE) are two bacterial enzymes involved in aromatic acid catabolism. They catalyse mechanistically distinct reactions yet they are related at the level of their primary, quaternary (homooctamer) and tertiary structures [ 1 , 2 ].A number of other proteins also seem to be evolutionary related to these twoenzymes. These include, various plasmid-encoded chloromuconate cycloisomerases 5.5.1.7 , Escherichia coli protein rspA [ 3 ], E. coli bifunctional DGOA protein, a number of D-galactonate dehydratases and D-mannonate dehydratases, and a hypothetical protein from Streptomyces ambofaciens [ 4 ].

This entry represents the C-terminal region of these proteins.

1. Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous. Nature 347, 692-4
2. On the origin of enzymatic species. Trends Biochem. Sci. 18, 372-6
3. Sensing starvation: a homoserine lactone--dependent signaling pathway in Escherichia coli. Science 265, 537-9
4. Analysis of genome instability in Streptomyces ambofaciens. J. Gen. Microbiol. 139, 2559-67