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Merck
CN

M4545

L-Methionine γ-lyase from Pseudomonas putida

lyophilized powder, pkg of ≥1.0 units/vial

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About This Item

CAS Number:
EC Number:
EC Number:
255-916-5
UNSPSC Code:
12352204
MDL number:
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form

lyophilized powder

packaging

pkg of ≥1.0 units/vial

storage temp.

−20°C

Other Notes

One unit will release 1.0 μmol of α-ketobutyrate from L-methionine per min at pH 8.0 at 37 °C.

Storage Class

13 - Non Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Regulatory Information

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[Perspectives of developing enzyme-based antitumor drugs].
V S Pokrovskiĭ et al.
Voprosy onkologii, 57(2), 155-164 (2011-08-04)
Wei Fu et al.
Sheng wu yi xue gong cheng xue za zhi = Journal of biomedical engineering = Shengwu yixue gongchengxue zazhi, 28(4), 839-842 (2011-09-23)
Methionine-dependent increase in tumor cells is a specific metabolic defect. This metabolic defect is also a target for selective treatment of cancer. Studies found that the methionine gamma-lyase (methioninase, L-methionine gamma-lyase) can specificly split the methionine of extracellular and intracellular
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
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

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