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L-Methionine γ-Lyase, Pseudomonas putida recombinant protein
L-Methionine-α-deamino-γ-mercaptomethane-Lyase, Methioninase, METase, MGL, mdeA
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P13254 |
|---|---|
| Calculated MW | 47.1 kDa (1-398 aa, NT Poly-His Tag) |
| Gene Symbol | mdeA |
|---|---|
| Other Names | L-Methionine-α-deamino-γ-mercaptomethane-Lyase, Methioninase, METase, MGL, mdeA |
| Gene Source | Pseudomonas putida |
| Source | E. coli |
| Assay&Purity | SDS-PAGE; ≥90% |
| Assay2&Purity2 | HPLC; |
| Recombinant | Yes |
| Results | ≥ 0.5 U/mg. |
| Sequence | 1-398 aa, NT Poly-His Tag |
| Target/Specificity | L-Methionine γ-Lyase |
| Application Notes | Briefly spin down and reconstitute in water or phosphate buffer. |
| Format | Lyophilized |
| 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.
Background
Methionine gamma-lyase (EC 4.4.1.11) 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.
References
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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