|PROSITE documentation PDOC00706|
Mandelate racemase (EC 220.127.116.11) (MR) and muconate lactonizing enzyme (EC 18.104.22.168) (MLE) are two bacterial enzymes involved in aromatic acid catabolism. They catalyze 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 two enzymes. These are:
We developed two signature patterns for these enzymes; both contain conserved acidic residues. The second pattern contains an aspartate and a glutamate which are ligands for either a magnesium ion (in MR) or a manganese ion (in MLE).Last update:
December 2001 / Patterns and text revised.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Neidhart D.J., Kenyon G.L., Gerlt J.A., Petsko G.A.|
|Title||Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous.|
|2||Authors||Petsko G.A., Kenyon G.L., Gerlt J.A., Ringe D., Kozarich J.W.|
|Title||On the origin of enzymatic species.|
|Source||Trends Biochem. Sci. 18:372-376(1993).|
|3||Authors||Huisman G.W., Kolter R.|
|Title||Sensing starvation: a homoserine lactone--dependent signaling pathway in Escherichia coli.|
|4||Authors||Schneider D., Aigle B., Leblond P., Simonet J.M., Decaris B.|
|Title||Analysis of genome instability in Streptomyces ambofaciens.|
|Source||J. Gen. Microbiol. 139:2559-2567(1993).|