4.4.1.11: methionine gamma-lyase
This is an abbreviated version!
For detailed information about methionine gamma-lyase, go to the full flat file.
Word Map on EC 4.4.1.11
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4.4.1.11
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lipase
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monoacylglycerol
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endocannabinoids
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cannabinoids
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lectin
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putida
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c-type
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2-arachidonoylglycerol
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pyridoxal
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medicine
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monoglyceride
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orthotopic
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galactose-type
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galnac
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selenomethionine
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anandamide
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freundii
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2-arachidonoyl
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citrobacter
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alpha-ketobutyrate
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methylselenol
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meibomian
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methionine-dependent
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mercaptan
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beta-lyase
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5'-phosphate-dependent
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dc-sign
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s-substituted
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synthesis
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nutrition
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environmental protection
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analysis
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drug development
- 4.4.1.11
- lipase
- monoacylglycerol
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endocannabinoids
- cannabinoids
- lectin
- putida
-
c-type
- 2-arachidonoylglycerol
- pyridoxal
- medicine
- monoglyceride
-
orthotopic
-
galactose-type
- galnac
- selenomethionine
- anandamide
- freundii
-
2-arachidonoyl
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citrobacter
- alpha-ketobutyrate
- methylselenol
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meibomian
-
methionine-dependent
- mercaptan
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beta-lyase
-
5'-phosphate-dependent
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dc-sign
-
s-substituted
- synthesis
- nutrition
- environmental protection
- analysis
- drug development
Reaction
Synonyms
CalE6, EhMGL1, EhMGL2, fer1MgL2, Fn1419, L-methionase, L-methioninase, L-methionine gamma-lyase, L-methionine gamma-lyase 1, L-methionine-alpha-deamino-gamma-mercaptomethane lyase, L-methionine-alpha-deamino-gamma-mercaptomethane-lyase, L-methionine-gamma-lyase, lyase, methionine, MdeA, MegL, METase, methioninase, methionine alpha,gamma-lyase, methionine dethiomethylase, methionine gamma-lyase, methionine lyase, methionine-gamma-lyase, MGL, MGL1, MGL2, rMETase, sav7062, TvMGL1, TvMGL2, YtjE
ECTree
4.4.1.11 methionine gamma-lyaseAdvanced search results
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results (Crystallization
Crystallization on EC 4.4.1.11 - methionine gamma-lyase
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor-diffusion method
computational model of the enzyme and the external aldimine intermediate, based on the crystal structures of methionine gamma-lyase from Clostridium sporogenes and Citrobacter freundii. The catalytic reaction can be divided into the formation of external aldimine intermediate from the internal aldimine intermediate, and a second step, when the external aldimine intermediate converts to the aminocrotonate intermediate, which contains complex asynchronous and concerted proton transfer processes
enzyme in complex with gamma-(L-1-amino-3-methylthiopropylphosphinic acid), beta-(S-ethyl-L-cysteine), and L-norleucine, soaking of holoenzyme crystals in a cryoprotective solution containing 35% PEG monomethyl ether 2000, 50 mM Tris-HCl, pH 8.5, 0.2 mM pyridoxal 5'-phosphate, 25 mM DTT, with addition of the respective ligand, 6.8 mM of beta-(S-ethyl-L-cysteine), 40 mM L-norleucine, or 48 mM gamma-(L-1-amino-3-methylthiopropylphosphinic acid), during different time intervals of 5-120 min, 1-2 weeks, X-ray diffraction structure determination and anaysis at 1.45-1.84 A resolution, molecular replacement
mutant C115H, in complex with inhibitor L-norleucine, to 1.45 A resolution. The inhibotor binds both noncovalently and covalently at the active site, corresponding to the intermediates of the gamma- and beta-elimination reactions, Michaelis complex and the external aldimine
purified recombinant enzyme in complex with inhibitor glycine, crystals are obtained using a method without the presence of ammonium sulfate, complexing with glycine by soaking of holoenzyme crystals in a cryoprotective mother liquid solution to which glycine is added stepwise from 5 mM to 20 mM during 20 min,, 1-2 weeks, X-ray diffraction structure determination and analysis at 2.45 A resolution, molecular replacement
structure of mutant Y58F, to 1.96 A resolution. The mutation does not result in essential changes of the conformation of the active site
to 1.65 A resolution. Absence of an aldimine bond between the active site Lys210 and pyridoxal 5'-phosphate in crystals, grown in monomethyl ether polyethylene glycol 2000 in the presence of ammonium sulfate
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hanging-drop vapor-diffusion method
computational model of the enzyme and the external aldimine intermediate, based on the crystal structures of methionine gamma-lyase from Clostridium sporogenes and Citrobacter freundii. The catalytic reaction can be divided into the formation of external aldimine intermediate from the internal aldimine intermediate, and a second step, when the external aldimine intermediate converts to the aminocrotonate intermediate, which contains complex asynchronous and concerted proton transfer processes
sitting drop vapour diffusion method, using 1.8 M ammonium sulfate, 0.1 M cacodylate buffer pH 6.2, 0.1 M lithium citrate, and 0.01 M betaine
in complex with 2-(N-morpholino)ethanesulfonic acid, to 2.1 A resolution. The ligand induces rotation of residue Tyr100, which stacks with PLP
to 2.0 A resolution. Active site resiudes are G105 and V322
1.8 A resolution. Residues Y59 and R61 of neighbouring subunits contact the phosphate group of pyridoxal 5-phosphate. Residues K240, D241 and R61 of one partner monomer and Y114 and C116 of the other form a hydrogen-bond network in the active site
hanging-drop vapor diffusion, protein solution containing 10-20 mg/ml protein in 20 mM sodium phosphate, pH 7.2, 0.5 mM pyridoxal 5'-phosphate and 0.5% 2-mercaptoethanol is equilibrated against a reservoir solution consisting of 15% polyethylene glycol 6000, 250 mM NaCl, 200 mM MES-NaOH, pH 6.5, 0.5 mM pyridoxal 5'-phosphate and 0.5% 2-mercaptoethanol, crystals grow at room temperatur within 1 week, crystals diffract to 1.7 A
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in mutant C116H a loop structure (Ala51-Asn64) in the adjacent subunit of the catalytic dimer cannot approach the cofactor pyridoxal 5'-phosphate because His116 disrupts the interaction of Asp241 with Lys240, and the liberated side chain of Lys240 causes steric hindrance with this loop
purified recombinant wild-type and mutant C116H enzymes, the latter complexed with L-methionine or L-homocysteine, sitting drop vapour diffusion method, mixing of 500 nl of 20 mg/ml protein 10 mM HEPES-NaOH, pH 7.4, with 500 nl of reservoir solution containing 200 mM MES-NaOH, pH 6.2, with 12.5% w/v PEG6000, 250 mm ammonium sulfate, 0.5 mM pyridoxal 5'-phosphate, and 0.5% v/v 2-mercaptoethanol, and equilibration against 0.1 ml of reservoir solution, 20°C, for ligand binding soaking of crystals in reservoir solution containing 50 mM amino acid, method optimization, X-ray diffraction structure determination and analysis at 2.1-2.6 A resolution, molecular replacement
sitting-drop vapor diffusion, 1.25 M ammonium sulfate in 100 mM MES-HCl, pH 6.0 as reservoir solution, protein solution consists of 10-20 mg/ml METase in 120 mM sodium chloride, 10 mM sodium phosphate, pH 7.2, crystals diffract to at least 2.68 A
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