GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM: COMPLEX WITH ADENOSYLCOBALAMIN AND SUBSTRATEGLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM: COMPLEX WITH ADENOSYLCOBALAMIN AND SUBSTRATE
[GMSS_CLOCO] Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).[HAMAP-Rule:MF_00526][1][2][3] [GLME_CLOCO] Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).[4][5]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
↑Leutbecher U, Bocher R, Linder D, Buckel W. Glutamate mutase from Clostridium cochlearium. Purification, cobamide content and stereospecific inhibitors. Eur J Biochem. 1992 Apr 15;205(2):759-65. PMID:1315276
↑Zelder O, Beatrix B, Leutbecher U, Buckel W. Characterization of the coenzyme-B12-dependent glutamate mutase from Clostridium cochlearium produced in Escherichia coli. Eur J Biochem. 1994 Dec 1;226(2):577-85. PMID:7880251
↑Zelder O, Beatrix B, Buckel W. Cloning, sequencing and expression in Escherichia coli of the gene encoding component S of the coenzyme B12-dependent glutamate mutase from Clostridium cochlearium. FEMS Microbiol Lett. 1994 May 1;118(1-2):15-21. PMID:8013871
↑Zelder O, Beatrix B, Leutbecher U, Buckel W. Characterization of the coenzyme-B12-dependent glutamate mutase from Clostridium cochlearium produced in Escherichia coli. Eur J Biochem. 1994 Dec 1;226(2):577-85. PMID:7880251
↑Leutbecher U, Bocher R, Linder D, Buckel W. Glutamate mutase from Clostridium cochlearium. Purification, cobamide content and stereospecific inhibitors. Eur J Biochem. 1992 Apr 15;205(2):759-65. PMID:1315276