Methylaspartate ammonia-lyase

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 and Ingraham LL (1960). "The preparation of crystalline beta-methylaspartase". Biochim. Biophys. Acta 44: 586–588. doi:10.1016/0006-3002(60)91612-7.

Carbon-nitrogen lyases (EC 4.3)

4.3.1: ammonia-lyases	Histidine ammonia-lyase Formiminotransferase cyclodeaminase Serine dehydratase

4.3.2: amidine-lyases	Argininosuccinate lyase Adenylosuccinate lyase

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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