M2570
L-Methionine γ-Lyase
≥0.2 unit/mg solid
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About This Item
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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Marie-Pierre Forquin et al.
Applied and environmental microbiology, 77(4), 1449-1459 (2010-12-21)
In this study, we combined metabolic reconstruction, growth assays, and metabolome and transcriptome analyses to obtain a global view of the sulfur metabolic network and of the response to sulfur availability in Brevibacterium aurantiacum. In agreement with the growth of
Luca Ronda et al.
Biochimica et biophysica acta, 1814(6), 834-842 (2010-07-06)
Pyridoxal 5'-phosphate (PLP) dependent methionine γ-lyase catalyzes the breakdown of L-methionine to α-ketobutyric acid, methanethiol and ammonia. This enzyme, present in anaerobic microorganisms, has biomedical interest both for its activity as antitumor agent, depleting methionine supply in methionine-dependent cancers, and
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