Chorismate mutase, AroQ class, eukaryotic type
Short name | Chorismate_mutase_AroQ_euk |
Overlapping homologous superfamilies |
Description
References
1.Crystal structures of the monofunctional chorismate mutase from Bacillus subtilis and its complex with a transition state analog. Chook YM, Ke H, Lipscomb WN. Proc. Natl. Acad. Sci. U.S.A. 90, 8600-3, (1993). View articlePMID: 8378335
2.Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase. Helmstaedt K, Krappmann S, Braus GH. Microbiol. Mol. Biol. Rev. 65, 404-21, table of contents, (2001). View articlePMID: 11528003
3.A small, thermostable, and monofunctional chorismate mutase from the archaeon Methanococcus jannaschii. MacBeath G, Kast P, Hilvert D. Biochemistry 37, 10062-73, (1998). View articlePMID: 9665711
4.Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures. Strater N, Schnappauf G, Braus G, Lipscomb WN. Structure 5, 1437-52, (1997). View articlePMID: 9384560
5.The aroQ-encoded monofunctional chorismate mutase (CM-F) protein is a periplasmic enzyme in Erwinia herbicola. Xia T, Song J, Zhao G, Aldrich H, Jensen RA. J. Bacteriol. 175, 4729-37, (1993). View articlePMID: 8335631
GO terms
biological process
molecular function
cellular component
- None
Cross References
Contributing Member Database Entries
- PROSITE profiles:PS51169
- PIRSF:PIRSF017318
- PANTHER:PTHR21145
- NCBIfam:TIGR01802