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Merck
CN

M2570

L-Methionine γ-Lyase

≥0.2 unit/mg solid

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UNSPSC Code:
12352204
MDL number:
EC Number:
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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

pictograms

Health hazard

signalword

Danger

hcodes

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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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
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
Timothy H Tran et al.
Acta crystallographica. Section D, Biological crystallography, 67(Pt 10), 831-838 (2011-09-21)
O-Acetylhomoserine sulfhydrylase (OAHS) is a pyridoxal 5'-phosphate (PLP) dependent sulfide-utilizing enzyme in the L-cysteine and L-methionine biosynthetic pathways of various enteric bacteria and fungi. OAHS catalyzes the conversion of O-acetylhomoserine to homocysteine using sulfide in a process known as direct sulfhydrylation.
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)

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