EC number:5.4.99.4
Enzyme
Download| EC Tree |
| 5. Isomerases |
| 5.4 Intramolecular transferases |
| 5.4.99 Transferring other groups |
| ID: | 5.4.99.4 |
|---|---|
| Description: | 2-methyleneglutarate mutase. |
| Alternative Name: |
Alpha-methyleneglutarate mutase. |
| Cath: | 1.10.1040.10; 1.10.150.120; 3.20.20.140; 3.30.365.10; 3.30.390.50; 3.30.465.10; 3.40.50.720; 2.30.40.10; 3.40.50.12340; 3.10.20.30; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 5.4.99.4 |
| BRENDA Enzyme Link: | BRENDA 5.4.99.4 |
| KEGG Enzyme Link: | KEGG5.4.99.4 |
| BioCyc Enzyme Link: | BioCyc 5.4.99.4 |
| ExPASy Enzyme Link: | ExPASy5.4.99.4 |
| EC2PDB Enzyme Link: | EC2PDB 5.4.99.4 |
| ExplorEnz Enzyme Link: | ExplorEnz 5.4.99.4 |
| PRIAM enzyme-specific profiles Link: | PRIAM 5.4.99.4 |
| IntEnz Enzyme Link: | IntEnz 5.4.99.4 |
| MEDLINE Enzyme Link: | MEDLINE 5.4.99.4 |
| RHEA:13793 | 2-methyleneglutarate = 2-methylene-3-methylsuccinate |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[*:3])-[CH2;+0:4]-[CH2;+0:5]-[*:6]>>[*:1]-[C;H0;+0:2](=[*:3])-[CH;+0:5](-[*:6])-[CH3;+0:4] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| On the role of two different cobalt(II) species in coenzyme B12-dependent 2-methyleneglutarate mutase from Clostridium barkeri. | Zelder O, Buckel W | 1993 Jan | 8382495 |
| Cloning, sequencing and expression of the gene encoding the coenzyme B12-dependent 2-methyleneglutarate mutase from Clostridium barkeri in Escherichia coli. | Beatrix B, Zelder O, Linder D, Buckel W | 1994 Apr 1 | 8168499 |
| On the steric course of the adenosylcobalamin-dependent 2-methyleneglutarate mutase reaction in Clostridium barkeri. | Hartrampf G, Buckel W | 1986 Apr 15 | 3699016 |
| Assay and purification of the adenosylcobalamin-dependent 2-methyleneglutarate mutase from Clostridium barkeri. | Michel C, Hartrampf G, Buckel W | 1989 Sep 1 | 2776761 |
| Searching for intermediates in the carbon skeleton rearrangement of 2-methyleneglutarate to (R)-3-methylitaconate catalyzed by coenzyme B12-dependent 2-methyleneglutarate mutase from Eubacterium barkeri. | Pierik AJ, Ciceri D, Lopez RF, Kroll F, Bröker G, Beatrix B, Buckel W, Golding BT | 2005 Aug 9 | 16060663 |