Crystallization and preliminary crystallographic characterization of recombinant L-methionine-alpha-deamino-gamma-mercaptomethane lyase (methioninase).
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.
Sridhar
V
V
Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Xu
M
M
Han
Q
Q
Sun
X
X
Tan
Y
Y
Hoffman
R M
RM
Prasad
G S
GS
D013437:Carbon-Sulfur Lyases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D008715:Methionine / Q000378:metabolism; D011487:Protein Conformation; D016958:Pseudomonas putida / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism
D011994:Recombinant Proteins; D008715:Methionine; D013437:Carbon-Sulfur Lyases; C021558:L-methionine gamma-lyase