Sridhar V, Xu M, Han Q, Sun X, Tan Y, Hoffman R M, Prasad G S
Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Acta Crystallogr D Biol Crystallogr. 2000 Dec;56(Pt 12):1665-7. doi: 10.1107/s0907444900013251.
L-Methionine-alpha-deamino-gamma-mercaptomethane lyase (rMETase) is involved in the alpha,gamma-elimination of methionine to alpha-ketobutyrate, methanethiol and ammonia. The reaction catalyzed by rMETase reduces the methionine concentration of methionine-dependent tumor cells, arresting their growth. Towards the goal of developing rMETase into an effective antitumor therapeutic and also to understand the catalytic mechanism of this enzyme, rMETase from Pseudomonas putida has been expressed, purified and crystallized. The crystals belong to space group P2(1)2(1)2 and diffract X-rays to at least 2.68 A resolution at 100 K using synchrotron radiation. The unit cell has parameters a = 152.8, b = 154.6, c = 80.8 A and contains four molecules in the asymmetric unit.
L-甲硫氨酸-α-脱氨基-γ-巯基甲烷裂解酶（rMETase）参与甲硫氨酸向α-酮丁酸、甲硫醇和氨的α,γ-消除反应。rMETase催化的反应降低了甲硫氨酸依赖性肿瘤细胞的甲硫氨酸浓度，从而抑制其生长。为了将rMETase开发成一种有效的抗肿瘤治疗药物，并了解该酶的催化机制，来自恶臭假单胞菌的rMETase已被表达、纯化和结晶。这些晶体属于空间群P2(1)2(1)2，在100 K下使用同步辐射X射线衍射至少可达2.68 Å分辨率。晶胞参数为a = 152.8、b = 154.6、c = 80.8 Å，不对称单元中包含四个分子。
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