EC number:5.4.99.1
Enzyme
Download| EC Tree |
| 5. Isomerases |
| 5.4 Intramolecular transferases |
| 5.4.99 Transferring other groups |
| ID: | 5.4.99.1 |
|---|---|
| Description: | Methylaspartate mutase. |
| Alternative Name: |
Methylaspartic acid mutase. Glutamic mutase. Glutamic isomerase. Glutamate mutase. Glutamate isomerase. Beta-methylaspartate-glutamate mutase. |
| Cath: | 3.20.20.240; 3.90.970.10; 3.40.50.280; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 5.4.99.1 |
| BRENDA Enzyme Link: | BRENDA 5.4.99.1 |
| KEGG Enzyme Link: | KEGG5.4.99.1 |
| BioCyc Enzyme Link: | BioCyc 5.4.99.1 |
| ExPASy Enzyme Link: | ExPASy5.4.99.1 |
| EC2PDB Enzyme Link: | EC2PDB 5.4.99.1 |
| ExplorEnz Enzyme Link: | ExplorEnz 5.4.99.1 |
| PRIAM enzyme-specific profiles Link: | PRIAM 5.4.99.1 |
| IntEnz Enzyme Link: | IntEnz 5.4.99.1 |
| MEDLINE Enzyme Link: | MEDLINE 5.4.99.1 |
| RHEA:12857 | (2S,3S)-3-methyl-L-aspartate = L-glutamate |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[CH3;+0:3])-[C;H0;+0:4](=[*:5])-[*:6]>>[*:1]-[CH2;+0:2]-[CH2;+0:3]-[C;H0;+0:4](=[*:5])-[*:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Adenosylcobalamin-dependent glutamate mutase from Clostridium tetanomorphum. Overexpression in Escherichia coli, purification, and characterization of the recombinant enzyme. | Holloway DE, Marsh EN | 1994 Aug 12 | 8051138 |
| Characterization of the coenzyme-B12-dependent glutamate mutase from Clostridium cochlearium produced in Escherichia coli. | Zelder O, Beatrix B, Leutbecher U, Buckel W | 1994 Dec 1 | 7880251 |
| Electronic structure studies of the adenosylcobalamin cofactor in glutamate mutase. | Brooks AJ, Fox CC, Marsh EN, Vlasie M, Banerjee R, Brunold TC | 2005 Nov 22 | 16285720 |
| Glutamate mutase from Clostridium cochlearium. Purification, cobamide content and stereospecific inhibitors. | Leutbecher U, Böcher R, Linder D, Buckel W | 1992 Apr 15 | 1315276 |
| The role of the active site glutamate in the rearrangement of glutamate to 3-methylaspartate catalyzed by adenosylcobalamin-dependent glutamate mutase. | Madhavapeddi P, Marsh EN | 2001 Dec | 11755393 |
| Radical Shuttling in a Protein: Ribose Pseudorotation Controls Alkyl-Radical Transfer in the Coenzyme B(12) Dependent Enzyme Glutamate Mutase This work was supported by the Österreichische Akademie der Wissenschaften (APART fellowship 614), the Österreichische Fonds zur Förderung der wissenschaftlichen Forschung (FWF-project 11599), and the European Commission (TMR project number ERB 4061 PL 95-0307). Crystallographic data were collected at the EMBL-beamline BW7B at DESY in Hamburg, Germany. We thank the beamline scientists for their assistance, and Ingrid Dreveny, Günter Gartler, Gerwald Jogl, and Oliver Sauer for their help during data collection. This research emerged from a collaboration with Prof. W. Buckel (Marburg) who supplied us with clones of the glutamate mutase proteins. | Gruber K, Reitzer R, Kratky C | 2001 Sep 17 | 11592143 |
| Adenosylcobalamin-dependent isomerases: new insights into structure and mechanism. | Marsh EN, Drennan CL | 2001 Oct | 11578922 |
| Interconversion of (S)-glutamate and (2S,3S)-3-methylaspartate: a distinctive B(12)-dependent carbon-skeleton rearrangement. | Wetmore SD, Smith DM, Golding BT, Radom L | 2001 Aug 22 | 11506551 |
| Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights. | Reitzer R, Gruber K, Jogl G, Wagner UG, Bothe H, Buckel W, Kratky C | 1999 Aug 15 | 10467146 |