| methylaspartate ammonia-lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Identifiers | |||||||||
| EC no. | 4.3.1.2 | ||||||||
| CAS no. | 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 | ||||||||
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The enzyme methylaspartate ammonia-lyase (EC 4.3.1.2) catalyzes the chemical reaction
- L-threo-3-methylaspartate mesaconate + 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 β-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 α-L-β-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 β-methylaspartase". Biochim. Biophys. Acta. 44: 586–588. doi:10.1016/0006-3002(60)91612-7.
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