IPR013342
Mandelate racemase/muconate lactonizing enzyme, C-terminal
InterPro entry
Short name | Mandelate_racemase_C |
Overlapping homologous superfamilies |
Description
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 two enzymes. 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.
References
1.Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous. Neidhart DJ, Kenyon GL, Gerlt JA, Petsko GA. Nature 347, 692-4, (1990). View articlePMID: 2215699
2.On the origin of enzymatic species. Petsko GA, Kenyon GL, Gerlt JA, Ringe D, Kozarich JW. Trends Biochem. Sci. 18, 372-6, (1993). View articlePMID: 8256284
3.Sensing starvation: a homoserine lactone--dependent signaling pathway in Escherichia coli. Huisman GW, Kolter R. Science 265, 537-9, (1994). View articlePMID: 7545940
Cross References
Contributing Member Database Entry
- SMART:SM00922