Methylaspartate mutase

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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 $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] 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.

[edit] References

IUBMB entry for 5.4.99.1
BRENDA references for 5.4.99.1 (Recommended.)
PubMed references for 5.4.99.1
PubMed Central references for 5.4.99.1
Google Scholar references for 5.4.99.1
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: 521–528. doi:10.1073/pnas.45.4.521.