Methylaspartate ammonia-lyase
| methylaspartate ammonia-lyase | |||||||||
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X-ray structure of methylaspartate ammonia lyase. PDB entry 1kko
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| 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 / EGO | ||||||||
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| Search | |
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| PMC | articles |
| PubMed | articles |
| NCBI | proteins |
In enzymology, a methylaspartate ammonia-lyase (EC 4.3.1.2) is an enzyme that catalyzes the chemical reaction
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.
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.
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