Methylaspartate ammonia-lyase
| 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
[edit]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
[edit]- ^ 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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