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.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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)
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
X Xu et al.
Journal of dental research, 89(11), 1304-1308 (2010-09-23)
Epigallocatechin gallate (EGCg), the main antimicrobial tea catechin, has been reported to inhibit growth and virulence factors of oral pathogens in vitro. Although the mechanism is unclear, the potential of EGCg in reducing halitosis caused by volatile sulfur compounds (VSCs)
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
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