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
存储类别
11 - Combustible Solids
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
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
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
[Perspectives of developing enzyme-based antitumor drugs].
V S Pokrovskiĭ et al.
Voprosy onkologii, 57(2), 155-164 (2011-08-04)
E A Morozova et al.
Biochemistry. Biokhimiia, 75(10), 1272-1280 (2010-12-21)
Kinetic parameters of Citrobacter freundii methionine γ-lyase were determined with substrates in γ-elimination reactions as well as the inhibition of the enzyme in the γ-elimination of L-methionine by amino acids with different structure. The data indicate an important contribution of
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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