L-Methionine y-Lase Polyclonal Antibody
Purified Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB |
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Primary Accession | P13254 |
Reactivity | Human, Mouse |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 42627 Da |
Other Names | Methionine gamma-lyase, L-methioninase, mdeA |
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Target/Specificity | L-Methionine y-Lase |
Formulation | 100 µg (0.5 mg/ml) of antibody in PBS pH 7.2, 0.01 % BSA, 0.03 % ProClin®, and 50 % glycerol. |
Handling | The antibody solution should be gently mixed before use. |
Background Descriptions | |
Precautions | L-Methionine y-Lase Polyclonal Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | mdeA {ECO:0000312|EMBL:BAA20553.1} |
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Function | Catalyzes the alpha,gamma-elimination of L-methionine to produce methanethiol, 2-oxobutanoate and ammonia (PubMed:8586629, PubMed:6742420). Is involved in L-methionine catabolism (PubMed:9190812). In fact, shows a multicatalytic function since it also catalyzes gamma-replacement of L-methionine with thiol compounds, alpha,gamma-elimination and gamma-replacement reactions of L- homocysteine and its S-substituted derivatives, O-substituted-L- homoserines and DL-selenomethionine, and, to a lesser extent, alpha,beta-elimination and beta-replacement reactions of L-cysteine, S- methyl-L-cysteine, and O-acetyl-L-serine (PubMed:6742420, PubMed:22785484). Also catalyzes deamination and gamma-addition reactions of L-vinylglycine (PubMed:6742420). Thus, the enzyme is able to cleave C-S, C-Se, and C-O bonds of sulfur, selenium, and oxygen amino acids, respectively (PubMed:6742420, PubMed:22785484). |
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Provided below are standard protocols that you may find useful for product applications.
Background
Methionine gamma-lyase 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.
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