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
-
endocannabinoids
- cannabinoids
- lectin
- putida
-
c-type
- 2-arachidonoylglycerol
- pyridoxal
- medicine
- monoglyceride
-
orthotopic
-
galactose-type
- galnac
- selenomethionine
- anandamide
- freundii
-
2-arachidonoyl
-
citrobacter
- alpha-ketobutyrate
- methylselenol
-
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
results (
results (Engineering
Engineering on EC 4.4.1.11 - methionine gamma-lyase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A366Y
mutant of the C-terminal flexible loop at the active site entry channel
C115A
mutation leads to a decrease of the catalytic efficiency in the gamma-elimination reaction of the physiological substrate by more than an order of magnitude
C115H
P357I
mutant of the C-terminal flexible loop at the active site entry channel
P360Q
mutant of the C-terminal flexible loop at the active site entry channel
V358Y
mutant exhibits a 1.9fold increase in the catalytic rate and a 3fold increase in Km value, catalytic efficiency is similar to wild type MGL. The cytotoxic activity towards a panel of cancer and nonmalignant cell lines is lower than that of wild-type
Y58F
mutation leads to a decrease of catalytic efficiencies in both gamma- and beta-elimination reactions of about two orders of magnitude and to a change of rate the limiting step of the physiological reaction
C110G
decrease in kcat values for both L-methionine and L-cysteine
Y108F
almost 100% reduction in alpha-gamma-elimination of both L-methionine and homocysteine
Y111F
about 80% reduction in alpha-gamma-elimination of both L-methionine and homocysteine
C116A
the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme
C116D
the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme
C116E
the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme
C116F
the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme
C116G
the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme
C116H
C116H/Y114F
site-directed mutagenesis, almost inactive mutant in gamma- and beta-elimination reactions of amino acids with 2-mercaptoethanol, no activity with L-methionine
C116I
the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme
C116K
the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme
C116L
the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme
C116M
the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme
C116N
the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme
C116P
the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme
C116Q
the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme
C116R
the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme
C116S
C116T
C116V
the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme
C116W
the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme
C116Y
the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme
D241E
site-directed mutagenesis, the mutant shows reduced activity in the elimination reaction compared to the wild-type enzyme
D241H
site-directed mutagenesis, the mutant shows reduced activity in the elimination reaction compared to the wild-type enzyme
D241I
site-directed mutagenesis, the mutant shows reduced activity in the elimination reaction compared to the wild-type enzyme
D241K
site-directed mutagenesis, the mutant shows reduced activity in the elimination reaction compared to the wild-type enzyme
D241M
site-directed mutagenesis, the mutant shows reduced activity in the elimination reaction compared to the wild-type enzyme
D241N
site-directed mutagenesis, the mutant shows reduced activity in the elimination reaction compared to the wild-type enzyme
D241R
site-directed mutagenesis, the mutant shows reduced activity in the elimination reaction compared to the wild-type enzyme
D241T
site-directed mutagenesis, the mutant shows reduced activity in the elimination reaction compared to the wild-type enzyme
K240D
site-directed mutagenesis, the mutant shows reduced activity in the elimination reaction compared to the wild-type enzyme
K240E
site-directed mutagenesis, the mutant shows reduced activity in the elimination reaction compared to the wild-type enzyme
K240H
site-directed mutagenesis, the mutant shows reduced activity in the elimination reaction compared to the wild-type enzyme
K240M
site-directed mutagenesis, the mutant shows reduced activity in the elimination reaction compared to the wild-type enzyme
K240R
site-directed mutagenesis, the mutant shows reduced activity in the elimination reaction compared to the wild-type enzyme
additional information
C115H
mutant cleaves S-alk(en)yl-L-cysteine sulfoxides more effectively than the wild type, reaction of EC 4.4.1.4
C115H
mutant is inactive in the gamma-elimination reaction of methionine while fully active in the gamma-elimination reaction of O-acetyl-L-homoserine and in the beta-elimination reaction of S-alk(en)yl-substituted cysteines
C115H
mutation leads to loss of activity in the gamma-elimination reaction of the physiological substrate. The catalytic efficiency in the beta-elimination reaction of S-substituted L-cysteine sulfoxides is increased by about an order of magnitude compared to the wild type
C116H
the mutant possesses little catalytic activity and shows marked increase in activity toward L-cysteine and a decrease in that toward L-methionine
C116H
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increase of enzyme activity toward cysteine, decrease of enzyme activity toward methionine
C116H
site-directed mutagenesis, the H-bond network of the mutant is broken affecting catalytic residue Tyr114, the mutant acquires a beta-elimination activity, and shows high conformational changes upon substrate binding, implicating an altered substrate specificity, highly increased for L-cysteine and reduced for L-methionine, compared to the wild-type enzyme
C116H
mutation renders the enzyme inactive towards L-methionine, but activity is restored when the substrate is homocysteine due to substrate-assisted catalysis
C116S
the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme
C116T
the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme
additional information
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overexpression in Escherichia coli allows growth on L-methionine as sole nitrogen source and confers a high rate of methanethiol emission. Knock-out of gene significantly increases leaf methionine content and leaf and root S-methylmethionine content in Arabidopsis plants
additional information
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knockout mutations, increase of S-methylmethionine and methionine accumulation in leaves under sulfate-limiting growth conditions, increase of free methionine in flowers and seeds under normal growth conditions
additional information
delta-mgl knock-out mutant, results in a 62% decrease in thiol-producing activity and a 97% decrease in total volatile sulfur compounds production
additional information
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delta-mgl knock-out mutant, results in a 62% decrease in thiol-producing activity and a 97% decrease in total volatile sulfur compounds production
additional information
site-saturation mutagenesis at residues of the C-terminal flexible loop at the active site entry channel, P357, V358, P360 and A366
additional information
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site-saturation mutagenesis at residues of the C-terminal flexible loop at the active site entry channel, P357, V358, P360 and A366
additional information
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fusion protein consisting of an amino-terminal fragment of urokinase linked to the amino terminus of the enzyme, greater inhibitory effect on proliferation of cancer cell lines
additional information
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gene silencing by siRNA, amino acid profiling of transgenic lines, overview
