recombinant
expressed in E. coli
form
lyophilized powder
specific activity
≥0.2 unit/mg solid
storage temp.
−20°C
General description
L-Methionine γ-lyase is a pyridoxal phosphate-containing enzyme that converts L-methionine to α-ketobutyrate, ammonia and methyl mercaptan. [1]
Application
Biochem/physiol Actions
L-Methionine γ-Lyase or methioninase has been shown to have anti-tumor effects by depleting methionine from methionine-dependent tumors making them more sensitive to traditional chemotherapies. [3]
Unit Definition
One unit iwill convert 1 micromole of L-methionine to 2-ketobutyrate per minute at pH 7.0 at 37 °C.
Physical form
Supplied as a lyophilized powder containing pyridoxal-5′-phosphate and potassium phosphate
Preparation Note
Expressed in E. coli from a proprietary gene
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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A S El-Sayed et al.
Journal of applied microbiology, 111(1), 54-69 (2011-04-07)
To immobilize the purified Aspergillus flavipesl-methioninase on solid carriers for continuous production of methanethiol with high purity, by the enzymatic methods. The purified l-methioninase was immobilized using different methods, and physicochemical and kinetic studies for the potent immobilized enzyme were
[Perspectives of developing enzyme-based antitumor drugs].
V S Pokrovskiĭ et al.
Voprosy onkologii, 57(2), 155-164 (2011-08-04)
Ashraf S A El-Sayed
Journal of microbiology (Seoul, Korea), 49(1), 130-140 (2011-03-04)
L-Methioninase was purified to electrophoretic homogeneity from cultures of Aspergillus flavipes using anion-exchange and gel filtration chromatography by 12.1 fold compared to the crude enzyme preparation. The purified enzyme had a molecular mass of 47 kDa under denaturing conditions and
Microdetermination of D-amino acids and D-amino acid oxidase activity with 3,methyl-2-benzothiazolone hydrazone hydrochloride.
K Soda
Analytical biochemistry, 25(1), 228-235 (1968-10-24)
Xinghua Sun et al.
Cancer research, 63(23), 8377-8383 (2003-12-18)
Recombinant methioninase (rMETase) is an enzyme active in preclinical mouse models of human cancer. The efficacy of rMETase is due to depletion of plasma methionine, an amino acid for which tumors generally have an abnormally high methionine requirement. Furthermore, transient
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