Methylaspartate mutase
Oxford Dictionary of Biochemistry:
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methylaspartate mutase
EC 5.4.99.1; systematic name: l-threo-3-methylaspartate carboxy-aminomethylmutase; other name: glutamate mutase. An enzyme that catalyses the reaction:
l-threo-3-methylaspartate = l-glutamate
. This is the first step of the glutamate-fermentation pathway of the anaerobic bacteria Clostridium cochlearium, C. tetanomorphum, and others. The product, (2S,3S)-3-methylaspartate, is converted to mesaconate by the enzyme methylaspartate ammonia-lyase (EC 4.3.1.2). Methylaspartate mutase requires a cobamide coenzyme and has been studied as an example of such a reaction. The enzyme has two subunits (large and small, sometimes called E and S).
| methylaspartate ammonia-lyase, methylase, methylCpG-binding protein 2 | |
| methylate, methylated-DNA-protein-cysteine S-methyltransferase, methylation of DNA |
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Methylaspartate mutase
| methylaspartate mutase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| EC number | 5.4.99.1 | ||||||
| CAS number | 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 / EGO | ||||||
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In enzymology, a methylaspartate mutase (EC 5.4.99.1) is an enzyme that catalyzes the chemical reaction
- 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
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
- BARKER HA, ROOZE V, SUZUKI F, IODICE AA (1964). "THE GLUTAMATE MUTASE SYSTEM. ASSAYS AND PROPERTIES". J. Biol. Chem. 239: 3260–6. PMID 14245371.
- Weissbach H, Toohey J and Barker HA (1959). "Isolation and properties of B12 coenzymes containing benzimidazole or dimethylbenzimidazole". Proc. Natl. Acad. Sci. USA 45 (4): 521–528. doi:10.1073/pnas.45.4.521.
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