The enzyme methylaspartate ammonia-lyase (EC 4.3.1.2) catalyzes the chemical reaction
L-threo-3-methylaspartate ⇌ {\displaystyle \rightleftharpoons } mesaconate + NH3 It thus degrades L-threo-3-methylaspartate into mesaconate and ammonia. 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
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.


