M2570
L-Methionine γ-Lyase
≥0.2 unit/mg solid
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.
Application
L-Methionine γ-lyase has been used in a study to assess catabolism of volatile sulfur compound precursors by Brevibacterium linens and Geotrichum candidum. It has also been used in a study to investigate the enzymatic processing of fluorinated methionine analogs.
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.
Physical form
Supplied as a lyophilized powder containing pyridoxal-5′-phosphate and potassium phosphate
Preparation Note
Expressed in E. coli from a proprietary gene
Other Notes
One unit iwill convert 1 micromole of L-methionine to 2-ketobutyrate per minute at pH 7.0 at 37 °C.
wgk
WGK 3
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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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
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)
[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
Ignace A Moya et al.
The Biochemical journal, 438(3), 513-521 (2011-06-11)
TFM (L-trifluoromethionine), a potential prodrug, was reported to be toxic towards human pathogens that express MGL (L-methionine γ-lyase; EC 4.4.1.11), a pyridoxal phosphate-containing enzyme that converts L-methionine into α-oxobutyrate, ammonia and methyl mercaptan. It has been hypothesized that the extremely
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