In enzymology, a methylaspartate mutase (EC 5.4.99.1) is an enzyme that catalyzes the chemical reaction
| methylaspartate mutase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.4.99.1 | ||||||||
| CAS no. | 9032-97-7 | ||||||||
| 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 | ||||||||
| |||||||||
- L-threo-3-methylaspartate L-glutamate
Hence, this enzyme has one substrate, L-threo-3-methylaspartate, and one product, L-glutamate.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is L-threo-3-methylaspartate carboxy-aminomethylmutase. Other names in common use include glutamate mutase, glutamic mutase, glutamic isomerase, glutamic acid mutase, glutamic acid isomerase, methylaspartic acid mutase, beta-methylaspartate-glutamate mutase, and glutamate isomerase. This enzyme participates in c5-branched dibasic acid metabolism. It employs one cofactor, cobamide.
Structural studies edit
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1B1A, 1BE1, 1CB7, 1CCW, 1FMF, 1I9C, 1ID8, and 2PWH.
References edit
- BARKER HA, ROOZE V, SUZUKI F, IODICE AA (1964). "The Glutamate Mutase System. Assays and Properties". J. Biol. Chem. 239: 3260–6. doi:10.1016/S0021-9258(18)97713-6. PMID 14245371.
- Weissbach H, Toohey J, Barker HA (1959). "Isolation and properties of B12 coenzymes containing benzimidazole or dimethylbenzimidazole". Proc. Natl. Acad. Sci. USA. 45 (4): 521–528. Bibcode:1959PNAS...45..521W. doi:10.1073/pnas.45.4.521. PMC 222591. PMID 16590408.
