Methylaspartate ammonia-lyase
In enzymology, a methylaspartate ammonia-lyase (EC 4.3.1.2) is an enzyme that catalyzes the chemical reaction
- L-threo-3-methylaspartate mesaconate + NH3
| methylaspartate ammonia-lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifiers | |||||||||
| EC number | 4.3.1.2 | ||||||||
| CAS number | 9033-26-5 | ||||||||
| 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 | ||||||||
| |||||||||
Hence, this enzyme has one substrate, L-threo-3-methylaspartate, and two products, mesaconate and NH3.
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-threo-3-methylaspartate ammonia-lyase (mesaconate-forming). Other names in common use include beta-methylaspartase, 3-methylaspartase, and L-threo-3-methylaspartate ammonia-lyase. This enzyme participates in c5-branched dibasic acid metabolism and nitrogen metabolism. It employs one cofactor, cobamide.
Structural studies
Several structures of this enzyme have been deposited in the Protein Data Bank (linked in the infobox) which show it possesses a TIM barrel domain.
References
- Levy, C. W.; Buckley, P. A.; Sedelnikova, S.; Kato, Y.; Asano, Y.; Rice, D. W.; Baker, P. J. (2002). "Insights into Enzyme Evolution Revealed by the Structure of Methylaspartate Ammonia Lyase". Structure. 10 (1): 105–13. doi:10.1016/S0969-2126(01)00696-7. PMID 11796115.
- BARKER HA, SMYTH RD, WAWSZKIEWICZ EJ, LEE MN, WILSON RM (1958). "Enzymic preparation and characterization of an alpha-L-beta-methylaspartic acid". Arch. Biochem. Biophys. 78 (2): 468–76. doi:10.1016/0003-9861(58)90371-0. PMID 13618029.
- Bright HJ; Ingraham LL (1960). "The preparation of crystalline beta-methylaspartase". Biochim. Biophys. Acta. 44: 586–588. doi:10.1016/0006-3002(60)91612-7.