Purification and Properties of Crystalline Anaerobes , atrobacter sp . Strain YG - 05043 - Methylaspartase from Two Facultative and Morganella morganii Strain YG - 0601

3-Methylaspartase (3-methylaspartate ammonia-lyase, EC 4.3.1.2) from two facultatiye anaerobes from soil, atrobacter sp. strain YG-0504 and Morganetla morganii strain YG-0601, were purified and crystallized from their crude extracts. Both of the Citrobacter and Mbrganetld enzymes appeared to be a dimer of subunits of M; 40,OOO and 44,OOO, respectively. The enzymes had similar enzymological properties: optimum pH for the deamination reaction of (2S,3S)-3-methylaspartic acid, substrate specificity, inhibitor, diyalent and monoyalent cation requirement, and N-terminal amino acid sequence homology. Howeyer, some differences were detected in pH and temperature stability, optimum pH for the amination reaction of mesaconic acid, optimum temperature, specific activity, and stability during electrophoresis. Both enzymes had similar enzymological properties to the known 3-methylaspartase from an obligate anaerobic bacterium, (;lbstridium tetanomorphum Hl, except kinetic onstants and substrate specificities.