L-Methionine γ-Lyase, Pseudomonas putida recombinant protein
L-Methionine-α-deamino-γ-mercaptomethane-Lyase, Methioninase, METase, MGL, mdeA
|Calculated MW||47.1 kDa (1-398 aa, NT Poly-His Tag)|
|Other Names||L-Methionine-α-deamino-γ-mercaptomethane-Lyase, Methioninase, METase, MGL, mdeA|
|Gene Source||Pseudomonas putida|
|Results||≥ 0.5 U/mg.|
|Sequence||1-398 aa, NT Poly-His Tag|
|Application Notes||Briefly spin down and reconstitute in water or phosphate buffer.|
|Storage||–20°C; Lyophilized from 10 mg/ml in 20 mM potassium phosphate, 150 mM NaCl, pH 8.3.|
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Provided below are standard protocols that you may find useful for product applications.
Methionine gamma-lyase (EC 220.127.116.11) from Pseudomonas putida is a PLP-dependent enzyme which plays a central role in sulfur amino acid metabolism. METase catalyzes the α, γ-elimination of methionine to α-ketobutyrate, methanethiol, and ammonia. METase also catalyzes the α, γ-elimination of other sulfur containing amino acids, such as homocysteine, cysteine. Because of its ability to deplete methionine, METase has been considered as a viable component of cancer therapeutics against methionine-dependent tumor cells. METase has also been utilized to design drug targets for the infectious diseases caused by parasitic protozoa and anaerobic periodontal bacteria.
Inoue H.,et al.J. Biochem. 117:1120-1125(1995).
Inoue H.,et al.J. Bacteriol. 179:3956-3962(1997).
Nakayama T.,et al.Biochemistry 27:1587-1591(1988).
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