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Merck
CN

M2570

L-Methionine γ-Lyase

≥0.2 unit/mg solid

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About This Item

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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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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