EC number:5.3.3.6
| ID: | 5.3.3.6 |
|---|---|
| Description: | Methylitaconate Delta-isomerase. |
| 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 5.3.3.6 |
| BRENDA Enzyme Link: | BRENDA 5.3.3.6 |
| KEGG Enzyme Link: | KEGG5.3.3.6 |
| BioCyc Enzyme Link: | BioCyc 5.3.3.6 |
| ExPASy Enzyme Link: | ExPASy5.3.3.6 |
| EC2PDB Enzyme Link: | EC2PDB 5.3.3.6 |
| ExplorEnz Enzyme Link: | ExplorEnz 5.3.3.6 |
| PRIAM enzyme-specific profiles Link: | PRIAM 5.3.3.6 |
| IntEnz Enzyme Link: | IntEnz 5.3.3.6 |
| MEDLINE Enzyme Link: | MEDLINE 5.3.3.6 |
| RHEA:23480 | 2-methylene-3-methylsuccinate = dimethylmaleate |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[C;H0;+0:4](-[*:5])=[CH2;+0:6]>>[*:1]-[C;H0;+0:2](-[*:3])=[C;H0;+0:4](-[*:5])-[CH3;+0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Assay and purification of the adenosylcobalamin-dependent 2-methyleneglutarate mutase from Clostridium barkeri. | Michel C, Hartrampf G, Buckel W | 1989 Sep 1 | 2776761 |
| Nicotinic acid metabolism. VI. Purification and properties of alpha-methyleneglutarate mutase (B 12-dependent) and methylitaconate isomerase. | Kung HF, Stadtman TC | 1971 May 25 | 5574401 |
| Crystal structure and putative mechanism of 3-methylitaconate-delta-isomerase from Eubacterium barkeri. | Velarde M, Macieira S, Hilberg M, Bröker G, Tu SM, Golding BT, Pierik AJ, Buckel W, Messerschmidt A | 2009 Aug 21 | 19559030 |