| 2-methyleneglutarate mutase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.4.99.4 | ||||||||
| CAS no. | 9059-10-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a 2-methyleneglutarate mutase ( EC 5.4.99.4) is an enzyme that catalyzes the chemical reaction
- 2-methyleneglutarate 2-methylene-3-methylsuccinate
Hence, this enzyme has one substrate, 2-methyleneglutarate, and one product, 2-methylene-3-methylsuccinate.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is 2-methyleneglutarate carboxy-methylenemethylmutase. This enzyme is also called alpha-methyleneglutarate mutase. This enzyme participates in c5-branched dibasic acid metabolism. It employs one cofactor, cobamide.
References
- Kung HF, Cederbaum S, Tsai L, Stadtman TC (1970). "Nicotinic acid metabolism. V. A cobamide coenzyme-dependent conversion of alpha-methyleneglutaric acid to dimethylmaleic acid". Proc. Natl. Acad. Sci. U.S.A. 65 (4): 978–84. Bibcode: 1970PNAS...65..978K. doi: 10.1073/pnas.65.4.978. PMC 283012. PMID 5266166.
- Kung HF, Stadtman TC (1971). "Nicotinic acid metabolism. VI. Purification and properties of alpha-methyleneglutarate mutase (B 12-dependent) and methylitaconate isomerase". J. Biol. Chem. 246 (10): 3378–88. doi: 10.1016/S0021-9258(18)62235-5. PMID 5574401.
| 2-methyleneglutarate mutase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.4.99.4 | ||||||||
| CAS no. | 9059-10-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a 2-methyleneglutarate mutase ( EC 5.4.99.4) is an enzyme that catalyzes the chemical reaction
- 2-methyleneglutarate 2-methylene-3-methylsuccinate
Hence, this enzyme has one substrate, 2-methyleneglutarate, and one product, 2-methylene-3-methylsuccinate.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is 2-methyleneglutarate carboxy-methylenemethylmutase. This enzyme is also called alpha-methyleneglutarate mutase. This enzyme participates in c5-branched dibasic acid metabolism. It employs one cofactor, cobamide.
References
- Kung HF, Cederbaum S, Tsai L, Stadtman TC (1970). "Nicotinic acid metabolism. V. A cobamide coenzyme-dependent conversion of alpha-methyleneglutaric acid to dimethylmaleic acid". Proc. Natl. Acad. Sci. U.S.A. 65 (4): 978–84. Bibcode: 1970PNAS...65..978K. doi: 10.1073/pnas.65.4.978. PMC 283012. PMID 5266166.
- Kung HF, Stadtman TC (1971). "Nicotinic acid metabolism. VI. Purification and properties of alpha-methyleneglutarate mutase (B 12-dependent) and methylitaconate isomerase". J. Biol. Chem. 246 (10): 3378–88. doi: 10.1016/S0021-9258(18)62235-5. PMID 5574401.