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(+)-alliin + H2O
allicin + pyruvate + NH3
-
-
-
?
(+)methiin + H2O
methanesulfenic acid + pyruvate + NH3
-
-
-
?
(+)propiin + H2O
propane-1-sulfenic acid + pyruvate + NH3
-
-
-
?
(+-)-alliin + H2O
allicin + pyruvate + NH3
-
-
-
?
(+-)-butiin + H2O
butane-1-sulfenic acid + pyruvate + NH3
-
-
-
?
(+-)-ethiin + H2O
ethanesulfenic acid + pyruvate + NH3
-
-
-
?
(+-)methiin + H2O
methanesulfenic acid + pyruvate + NH3
-
-
-
?
(+-)propiin + H2O
propane-1-sulfenic acid + pyruvate + NH3
-
-
-
?
1-amino-3-(methylthio)propylphosphinic acid + H2O
1-oxopropylphosphinic acid + methanethiol + NH3
-
-
-
?
2-amino-3-(N,N-dimethylamino)propionic acid
2-iminopropionic acid + ?
-
C-N-bond cleavage
-
?
alliin + H2O
allicin + pyruvic acid + NH3
-
-
-
?
beta-chloro-L-alanine + H2O
?
-
-
-
?
cystathionine + ?
?
-
-
-
-
?
DL-2-amino-3-(N-hydroxyethylamino)-propionic acid
ethanolamine + NH3 + pyruvate
-
-
-
?
DL-2-amino-3-(N-methylamino)propionic acid
methylamine + NH3 + pyruvate
-
-
-
?
DL-ethionine + H2O
?
-
-
-
-
?
DL-homocysteic acid + H2O
?
-
-
-
-
?
DL-homocysteine + 2-mercaptoethanol
H2S + S-(beta-hydroxyethyl)-L-homocysteine
gamma-replacement reaction, wild-type enzyme
-
-
?
DL-homocysteine + H2O
2-oxobutanoate + NH3 + H2S
DL-homocysteine + H2O
2-oxobutanoate + NH3 + hydrogen sulfide
-
-
-
?
DL-homocysteine + H2O
hydrogen sulfide + NH3 + 2-oxobutanoate
DL-homoserine + H2O
NH3 + 2-oxobutanoate
-
-
-
-
?
ethiin + H2O
ethanesulfenic acid + pyruvate + NH3
-
-
-
?
homocysteine + alkanethiol
S-alkylhomocysteine
-
-
corresponding
?
L-1-amino-3-methylthiopropylphosphinic acid + H2O
methanethiol + NH3 + propanoylphosphinic acid
Arg374 and Ser339 are involved in the binding of carboxyl groups of the substrate, the hydroxyl of Tyr113 is a potential acceptor of a proton from the amino groups of the amino acid
-
-
?
L-cystathionine + ?
?
-
-
-
-
?
L-cysteine
2-oxopropanoate + NH3 + H2S
-
-
-
-
?
L-cysteine + 2-mercaptoethanol
H2S + S-(beta-hydroxyethyl)-L-cysteine
beta-replacement reaction, wild-type enzyme and mutant C116H
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
L-cystine + H2O
?
assay at pH 8.0, 37°C
-
-
?
L-ethionine + H2O
ethanethiol + NH3 + 2-oxobutanoate
L-Gly(vinyl) + H2O
?
-
-
-
-
?
L-homocysteine
2-oxobutanoate + NH3 + hydrogen sulfide
L-homocysteine + H2O
hydrogen sulfide + NH3 + 2-oxobutanoate
L-homocysteine + H2O
sulfide + NH3 + 2-oxobutanoate
L-homoserine
NH3 + 2-oxobutanoate
-
-
-
?
L-methionine
methanethiol + NH3 + 2-oxobutanoate
L-methionine + 2-butylthiol
S-2-butylhomocysteine
-
-
-
?
L-methionine + 2-mercaptoethanol
methanethiol + S-(beta-hydroxyethyl)-L-homocysteine
gamma-replacement reaction, wild-type enzyme
-
-
?
L-methionine + 2-propylthiol
S-2-propylhomocysteine
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
L-methionine sulfone + H2O
? + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine sulfoxide
?
-
-
-
-
?
L-methionine sulfoxide + H2O
?
L-selenodjenkolate
pyruvate + NH3 + H2Se + formaldehyde
-
-
-
?
L-selenomethionine + H2O
?
-
-
-
-
?
methiin + H2O
methanesulfenic acid + pyruvate + NH3
-
-
-
?
O-acetyl-DL-homoserine + H2O
NH3 + 2-oxobutanoate + acetate
-
-
-
-
?
O-acetyl-L-homoserine
?
-
-
-
?
O-acetyl-L-homoserine + H2O
2-oxobutanoate + NH3 + acetate
-
-
-
?
O-acetyl-L-homoserine + H2O
?
-
-
-
-
?
O-acetyl-L-serine + H2O
2-oxopropanoate + NH3 + acetate
O-methyl-L-serine + H2O
?
-
-
-
-
?
O-succinyl-L-homoserine + H2O
?
weak activity
-
-
?
S-benzyl-L-cysteine + H2O
?
S-benzyl-L-cysteine + H2O
thiobenzyl alcohol + NH3 + 2-oxopropanoate
S-butyl-L-cysteine + H2O
butanethiol + NH3 + 2-oxopropanoate
-
-
-
?
S-ethyl-L-cysteine
?
-
-
-
?
S-ethyl-L-cysteine + H2O
?
S-ethyl-L-cysteine + H2O
ethanethiol + NH3 + 2-oxopropanoate
S-ethyl-L-cysteine + H2O
ethanethiol + NH3 + pyruvate
Arg374 and Ser339 are involved in the binding of carboxyl groups of the substrate, the hydroxyl of Tyr113 is a potential acceptor of a proton from the amino groups of the amino acid. Formation of external aldimine, conformational changes in the active center enable the Tyr58 hydroxyl group to occupy a position favorable for protonation of the leaving group
-
-
?
S-ethyl-L-homocysteine + H2O
?
S-ethyl-L-homocysteine + H2O
ethanethiol + NH3 + 2-oxobutanoate
S-methyl-L-cysteine
?
-
-
-
?
S-methyl-L-cysteine + 2-mercaptoethanol
?
-
-
-
?
S-methyl-L-cysteine + H2O
?
-
-
-
-
?
S-methyl-L-cysteine + H2O
methanethiol + NH3 + 2-oxopropanoate
S-methyl-L-cysteine + H2O
pyruvate + NH3 + CH3SH
S-methylcysteine + H2O
?
-
-
-
-
?
S-propyl-L-cysteine + H2O
propanethiol + NH3 + 2-oxopropanoate
-
-
-
?
Se-methylselenocysteine
?
selenoethionine + H2O
ethylselenol + NH3 + 2-oxobutanoate
-
-
-
?
selenomethionine + H2O
methylselenol + NH3 + 2-oxobutanoate
trifluoromethionine + H2O
?
-
-
-
-
?
trifluoromethionine + H2O
trifluoromethanethiol + NH3 + 2-oxobutanoate
-
-
-
?
DL-homocysteine + H2O
2-oxobutanoate + NH3 + H2S
-
-
-
-
?
DL-homocysteine + H2O
2-oxobutanoate + NH3 + H2S
112% of activity with L-methionine
-
?
DL-homocysteine + H2O
2-oxobutanoate + NH3 + H2S
294% of EhMGL1 activity with L-methionine
-
?
DL-homocysteine + H2O
?
-
-
-
-
?
DL-homocysteine + H2O
?
-
-
-
-
?
DL-homocysteine + H2O
?
-
-
-
-
?
DL-homocysteine + H2O
?
-
-
-
-
?
DL-homocysteine + H2O
?
-
-
-
-
?
DL-homocysteine + H2O
?
-
-
-
-
?
DL-homocysteine + H2O
?
-
-
-
-
?
DL-homocysteine + H2O
?
-
-
-
-
?
DL-homocysteine + H2O
hydrogen sulfide + NH3 + 2-oxobutanoate
-
-
-
-
?
DL-homocysteine + H2O
hydrogen sulfide + NH3 + 2-oxobutanoate
-
-
-
?
DL-homocysteine + H2O
hydrogen sulfide + NH3 + 2-oxobutanoate
-
-
-
?
DL-homocysteine + H2O
hydrogen sulfide + NH3 + 2-oxobutanoate
-
-
-
?
DL-homocysteine + H2O
hydrogen sulfide + NH3 + 2-oxobutanoate
-
-
-
?
DL-homocysteine + H2O
hydrogen sulfide + NH3 + 2-oxobutanoate
highest substrate specificity for DL-homocysteine
-
-
?
ethionine
?
-
-
-
?
L-cystathionine + H2O
?
assay at pH 8.0, 37°C
-
-
?
L-cystathionine + H2O
?
-
-
-
-
?
L-cystathionine + H2O
?
-
-
-
-
?
L-cysteine
?
-
-
-
?
L-cysteine + H2O
?
-
-
-
-
?
L-cysteine + H2O
?
assay at pH 8.0, 37°C
-
-
?
L-cysteine + H2O
?
-
-
-
-
?
L-cysteine + H2O
?
-
-
-
-
?
L-cysteine + H2O
?
-
-
-
-
?
L-cysteine + H2O
?
-
-
-
-
?
L-cysteine + H2O
?
-
-
-
-
?
L-cysteine + H2O
?
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
160% of EhMGL1 activity with L-methionine
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
20% of activity with L-methionine
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
-
-
-
?
L-ethionine + H2O
?
-
-
-
-
?
L-ethionine + H2O
?
-
-
-
-
?
L-ethionine + H2O
?
-
-
-
-
?
L-ethionine + H2O
?
-
-
-
-
?
L-ethionine + H2O
?
-
-
-
-
?
L-ethionine + H2O
?
-
-
-
-
?
L-ethionine + H2O
?
-
-
-
-
?
L-ethionine + H2O
ethanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-ethionine + H2O
ethanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-ethionine + H2O
ethanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-ethionine + H2O
ethanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-ethionine + H2O
ethanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-ethionine + H2O
ethanethiol + NH3 + 2-oxobutanoate
-
60% of activity with L-methinine
-
?
L-homocysteine
2-oxobutanoate + NH3 + hydrogen sulfide
-
-
methionine gamma-lyase catalyzes the decomposition of homocysteine to hydrogen sulfide which forms fluorescent CdS nanoparticles in the presence of Cd(NO3)2. Hydrogen sulfide dissociates to yield S2? anions which readily interact with Cd2+ forming fluorescent CdS nanocrystals, assay method development and evaluation, overview
-
?
L-homocysteine
2-oxobutanoate + NH3 + hydrogen sulfide
-
-
methionine gamma-lyase catalyzes the decomposition of homocysteine to hydrogen sulfide which forms fluorescent CdS nanoparticles in the presence of Cd(NO3)2. Hydrogen sulfide dissociates to yield S2? anions which readily interact with Cd2+ forming fluorescent CdS nanocrystals, assay method development and evaluation, overview
-
?
L-homocysteine + H2O
?
-
-
-
-
?
L-homocysteine + H2O
?
-
-
-
-
?
L-homocysteine + H2O
hydrogen sulfide + NH3 + 2-oxobutanoate
-
-
-
-
?
L-homocysteine + H2O
hydrogen sulfide + NH3 + 2-oxobutanoate
-
-
-
-
?
L-homocysteine + H2O
sulfide + NH3 + 2-oxobutanoate
-
-
-
?
L-homocysteine + H2O
sulfide + NH3 + 2-oxobutanoate
-
-
-
?
L-homoserine + H2O
?
-
-
-
-
?
L-homoserine + H2O
?
-
-
-
-
?
L-homoserine + H2O
?
-
-
-
-
?
L-methionine
?
-
bacterial metabolism of methionine
-
-
?
L-methionine
?
-
bacterial metabolism of methionine
-
-
?
L-methionine
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
?
-
-
-
-
?
L-methionine + H2O
?
-
-
-
-
?
L-methionine + H2O
?
-
-
-
-
?
L-methionine + H2O
?
-
-
-
-
?
L-methionine + H2O
?
-
-
-
-
?
L-methionine + H2O
?
assay at pH 8.0, 37°C
-
-
?
L-methionine + H2O
?
-
-
-
-
?
L-methionine + H2O
?
-
-
-
-
?
L-methionine + H2O
?
-
-
-
-
?
L-methionine + H2O
?
-
-
-
-
?
L-methionine + H2O
?
-
-
-
-
?
L-methionine + H2O
?
-
-
-
-
?
L-methionine + H2O
?
-
-
-
-
?
L-methionine + H2O
?
-
-
-
-
?
L-methionine + H2O
?
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
part of the methanethiol produced can react with an activated form of serine to produce S-methylcysteine. Product 2-oxobutanoate enters the papthway of Ile synthesis in plastids, part of the methanethiol produced can react with an activated form of serine to produce S-methylcysteine
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
gamma-elimination reaction
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
gamma-elimination reaction
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
gamma-elimination reaction, initial aldimine, quinonoid, and ketimine intermediates of the gamma-elimination reaction, possible concerted mechanisms of reversible ketimine formation and pro-(R)-Calpha-proton exchange, overview
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
gamma-elimination reaction
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
gamma-elimination reaction
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
181% of EhMGL1 activity with L-methionine
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
gamma-elimination reaction
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
ir
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
ir
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
gamma-elimination reaction
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine sulfone
?
-
-
-
-
?
L-methionine sulfone
?
-
-
-
?
L-methionine sulfoxide + H2O
?
-
gamma-elimination reaction
-
-
?
L-methionine sulfoxide + H2O
?
-
gamma-elimination reaction
-
-
?
L-methionine sulfoxide + H2O
?
-
gamma-elimination reaction
-
-
?
L-methionine sulfoxide + H2O
?
-
gamma-elimination reaction
-
-
?
L-vinylglycine
?
-
-
-
-
?
O-acetyl-L-serine + H2O
2-oxopropanoate + NH3 + acetate
-
-
-
?
O-acetyl-L-serine + H2O
2-oxopropanoate + NH3 + acetate
-
-
-
?
O-acetyl-L-serine + H2O
2-oxopropanoate + NH3 + acetate
11% of activity with L-methionine
-
?
O-acetyl-L-serine + H2O
2-oxopropanoate + NH3 + acetate
34% of EhMGL1 activity with L-methionine
-
?
O-acetyl-L-serine + H2O
2-oxopropanoate + NH3 + acetate
weak activity
-
-
?
S-benzyl-L-cysteine + H2O
?
-
beta-elimination reaction
-
-
?
S-benzyl-L-cysteine + H2O
?
-
beta-elimination reaction
-
-
?
S-benzyl-L-cysteine + H2O
?
-
beta-elimination reaction
-
-
?
S-benzyl-L-cysteine + H2O
?
-
beta-elimination reaction
-
-
?
S-benzyl-L-cysteine + H2O
thiobenzyl alcohol + NH3 + 2-oxopropanoate
-
-
-
-
?
S-benzyl-L-cysteine + H2O
thiobenzyl alcohol + NH3 + 2-oxopropanoate
-
-
-
?
S-benzyl-L-cysteine + H2O
thiobenzyl alcohol + NH3 + 2-oxopropanoate
-
-
-
-
?
S-benzyl-L-cysteine + H2O
thiobenzyl alcohol + NH3 + 2-oxopropanoate
-
-
-
?
S-ethyl-L-cysteine + H2O
?
-
beta-elimination reaction
-
-
?
S-ethyl-L-cysteine + H2O
?
-
beta-elimination reaction
-
-
?
S-ethyl-L-cysteine + H2O
?
-
beta-elimination reaction
-
-
?
S-ethyl-L-cysteine + H2O
?
-
beta-elimination reaction
-
-
?
S-ethyl-L-cysteine + H2O
ethanethiol + NH3 + 2-oxopropanoate
-
-
-
-
?
S-ethyl-L-cysteine + H2O
ethanethiol + NH3 + 2-oxopropanoate
-
-
-
?
S-ethyl-L-cysteine + H2O
ethanethiol + NH3 + 2-oxopropanoate
-
-
-
-
?
S-ethyl-L-cysteine + H2O
ethanethiol + NH3 + 2-oxopropanoate
-
-
-
?
S-ethyl-L-cysteine + H2O
ethanethiol + NH3 + 2-oxopropanoate
-
-
-
-
?
S-ethyl-L-cysteine + H2O
ethanethiol + NH3 + 2-oxopropanoate
weak activity
-
-
?
S-ethyl-L-homocysteine + H2O
?
-
gamma-elimination reaction
-
-
?
S-ethyl-L-homocysteine + H2O
?
-
gamma-elimination reaction
-
-
?
S-ethyl-L-homocysteine + H2O
?
-
gamma-elimination reaction
-
-
?
S-ethyl-L-homocysteine + H2O
?
-
gamma-elimination reaction
-
-
?
S-ethyl-L-homocysteine + H2O
ethanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
S-ethyl-L-homocysteine + H2O
ethanethiol + NH3 + 2-oxobutanoate
-
-
-
?
S-methyl-L-cysteine + H2O
methanethiol + NH3 + 2-oxopropanoate
-
-
-
-
?
S-methyl-L-cysteine + H2O
methanethiol + NH3 + 2-oxopropanoate
-
-
-
?
S-methyl-L-cysteine + H2O
methanethiol + NH3 + 2-oxopropanoate
-
-
-
-
?
S-methyl-L-cysteine + H2O
methanethiol + NH3 + 2-oxopropanoate
-
-
-
?
S-methyl-L-cysteine + H2O
methanethiol + NH3 + 2-oxopropanoate
weak activity
-
-
?
S-methyl-L-cysteine + H2O
pyruvate + NH3 + CH3SH
-
-
-
-
?
S-methyl-L-cysteine + H2O
pyruvate + NH3 + CH3SH
-
-
-
-
?
S-methyl-L-cysteine + H2O
pyruvate + NH3 + CH3SH
-
-
-
ir
Se-methylselenocysteine
?
-
-
-
-
?
Se-methylselenocysteine
?
-
-
-
?
selenomethionine + H2O
methylselenol + NH3 + 2-oxobutanoate
-
-
-
-
?
selenomethionine + H2O
methylselenol + NH3 + 2-oxobutanoate
-
-
-
?
L-methionine
?
additional information
-
bacterial metabolism of methionine
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
multicatalytic: alpha,gamma-elimination and gamma-replacement reactions of L-methionine and its analogs, alpha, beta-elimination and beta-replacement of L-cysteine and its analogs, deamination and gamma-addition of vinylglycine and deuterium labelling at alpha and beta position of L-methionine and other straight-chain L-amino acids
-
?
additional information
?
-
-
no substrate: L-cysteine
-
-
?
additional information
?
-
-
determination of rate constants of the enzyme-catalyzed exchange of Calpha and Cbeta-protons with deuterium, as well as the kinetic isotope effect of the deuterium label in the Calpha-position of inhibitors on the rate of exchange of their beta-protons. Neither stereoselectivity in the beta-proton exchange nor noticeable isotope effect on the exchange rates of beta-protons is found
-
-
?
additional information
?
-
-
substrate specificty, overview. In addition to the physiological reaction, the enzyme catalyzes the beta-elimination reaction of L-cysteine and its S-substituted derivatives, yielding the corresponding mercaptans, pyruvic acid, and ammonia
-
-
?
additional information
?
-
enzyme additionally catalyzes the beta-elimination reaction of (+-)-S-alk(en)yl-L-cysteine sulfoxides to yield thiosulfinate, reaction of EC 4.4.1.4. It can decompose both diastereomers equally
-
-
?
additional information
?
-
-
enzyme additionally catalyzes the beta-elimination reaction of (+-)-S-alk(en)yl-L-cysteine sulfoxides to yield thiosulfinate, reaction of EC 4.4.1.4. It can decompose both diastereomers equally
-
-
?
additional information
?
-
enzyme catalyzes the exchange of both Calpha-protons of glycine with high stereospecificity for pro-R-proton. The reaction mechanism includes ketimine intermediate formation
-
-
?
additional information
?
-
-
enzyme catalyzes the exchange of both Calpha-protons of glycine with high stereospecificity for pro-R-proton. The reaction mechanism includes ketimine intermediate formation
-
-
?
additional information
?
-
-
substrate specificty, overview. In addition to the physiological reaction, the enzyme catalyzes the beta-elimination reaction of L-cysteine and its S-substituted derivatives, yielding the corresponding mercaptans, pyruvic acid, and ammonia
-
-
?
additional information
?
-
-
substrate specificty, overview. In addition to the physiological reaction, the enzyme catalyzes the beta-elimination reaction of L-cysteine and its S-substituted derivatives, yielding the corresponding mercaptans, pyruvic acid, and ammonia
-
-
?
additional information
?
-
under normal conditions, isoform ehMGL1 is involved in degradation of L-methionine
-
-
?
additional information
?
-
under normal conditions, isoform ehMGL1 is involved in degradation of L-methionine
-
-
?
additional information
?
-
-
under normal conditions, isoform ehMGL1 is involved in degradation of L-methionine
-
-
?
additional information
?
-
under normal conditions, isoform ehMGL2 is not involved degradation of L-methionine
-
-
?
additional information
?
-
under normal conditions, isoform ehMGL2 is not involved degradation of L-methionine
-
-
?
additional information
?
-
-
under normal conditions, isoform ehMGL2 is not involved degradation of L-methionine
-
-
?
additional information
?
-
-
using whole-cell lysate of Ferroplasma acidarmanus fer1, pyridoxal 5'-phosphate-dependent and L-methionine-dependent production of alpha-keto compounds and thiol groups is demonstrated, thus indicating the presence of methionine gamma-lyase in this acidophilic archaeon
-
-
?
additional information
?
-
-
using whole-cell lysate of Ferroplasma acidarmanus fer1, pyridoxal 5'-phosphate-dependent and L-methionine-dependent production of alpha-keto compounds and thiol groups is demonstrated, thus indicating the presence of methionine gamma-lyase in this acidophilic archaeon
-
-
?
additional information
?
-
additional information
-
-
-
?
additional information
?
-
-
substrate specificty, overview. In addition to the physiological reaction, the enzyme catalyzes the beta-elimination reaction of L-cysteine and its S-substituted derivatives, yielding the corresponding mercaptans, pyruvic acid, and ammonia
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
beta-exchange between cysteine and alkanethiols, exchange reaction between substituents of gamma-carbon of homocysteine and alkanethiols, forming corresponding S-alkylhomocysteine
-
?
additional information
?
-
-
not: D-methionine, 2-oxo-4-methylthiobutanoate, non-sulfur-containing amino acids
-
?
additional information
?
-
-
multicatalytic: alpha,gamma-elimination and gamma-replacement reactions of L-methionine and its analogs, alpha, beta-elimination and beta-replacement of L-cysteine and its analogs, deamination and gamma-addition of vinylglycine and deuterium labelling at alpha and beta position of L-methionine and other straight-chain L-amino acids
-
?
additional information
?
-
no activity with O-phospho-L-serine
-
-
?
additional information
?
-
-
no activity with O-phospho-L-serine
-
-
?
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1.25
1-amino-3-(methylthio)propylphosphinic acid
-
30°C
18.2
2-amino-3-(N,N-dimethylamino)propionic acid
-
-
12.3
DL-2-amino-3(N-hydroxyethyl)propionic acid
-
-
2.3
DL-amino-3-(N-methylamino)propionic acid
-
-
1.2
L-1-amino-3-methylthiopropylphosphinic acid
pH and temperature not specified in the publication
6.7
L-Gly(vinyl)
-
30°C, pH 8.0
1.78 - 6.43
L-homocysteine
4 - 38
L-methionine sulfone
6.2 - 33.51
L-methionine sulfoxide
2.3
L-selenodjenkolate
-
-
6.7 - 7.22
L-Vinylglycine
5.82
O-acetyl-DL-homoserine
-
pH 8.0, 30°C
2.22 - 6
O-acetyl-L-homoserine
2.88 - 52.33
O-acetyl-L-serine
2.8
O-methyl-L-serine
-
-
0.18 - 2.75
S-Benzyl-L-cysteine
0.17 - 8.19
S-ethyl-L-cysteine
0.278 - 8.11
S-ethyl-L-homocysteine
0.4 - 2.62
S-methyl-L-cysteine
0.77
S-methylcysteine
-
-
0.13
Se-methyl-L-selenocysteine
-
-
0.1 - 5.45
trifluoromethionine
additional information
L-methionine
0.44
alliin
mutant C115H, pH 8.0, 30°C
1.75
alliin
mutant C115A, pH 8.0, 30°C
3.6
cysteine
-
recombinant, MGL2 C116G
8.5
cysteine
-
recombinant MGL1
9.7
cysteine
-
recombinant MGL1, C113G
22.3
cysteine
-
recombinant MGL2
0.2
DL-homocysteine
pH 8.0, 37°C, recombinant mutant Y114F/C116H
0.24
DL-homocysteine
mutant enzyme C116S, at 37°C
0.6
DL-homocysteine
pH 8.0, 37°C, recombinant mutant K240R
0.8
DL-homocysteine
pH 8.0, 37°C, recombinant mutant K240N
0.97
DL-homocysteine
recombinant enzyme
0.97
DL-homocysteine
-
pH 8.0, 30°C
1
DL-homocysteine
-
30°C, pH 8.0
1.1
DL-homocysteine
wild-type
1.1
DL-homocysteine
pH 8.0, 37°C, recombinant wild-type enzyme
1.4
DL-homocysteine
pH 8.0, 37°C, recombinant mutant C166H
1.4
DL-homocysteine
pH 8.0, 37°C, recombinant mutant K240M
1.47
DL-homocysteine
wild-type ehMGL2, pH 7.0, 37°C
1.61
DL-homocysteine
mutant enzyme C116A, at 37°C
1.8
DL-homocysteine
mutant enzyme C116H, at 37°C
1.82
DL-homocysteine
wild type enzyme, at 37°C
1.87
DL-homocysteine
36°C, pH 6.8, recombinant EhMGL2
3.03
DL-homocysteine
wild-type ehMGL1, pH 7.0, 37°C
3.4
DL-homocysteine
36°C, pH 6.8, recombinant EhMGL1
3.46
DL-homocysteine
mutant Y58F, pH 8.0, 30°C
6
DL-homocysteine
pH 8.0, 37°C, recombinant mutant K240I
56.5
DL-homoserine
-
pH 8.0, 30°C
56.5
DL-homoserine
-
30°C, pH 8.0
0.457
ethiin
mutant C115H, pH 8.0, 30°C
5.48
ethiin
mutant C115A, pH 8.0, 30°C
0.12
L-cysteine
mutant enzyme C116S, at 37°C
0.16
L-cysteine
recombinant enzyme
0.16
L-cysteine
-
30°C, pH 8.0
0.18
L-cysteine
wild-type
0.18
L-cysteine
pH 7.6, 37°C
0.2
L-cysteine
pH 8.0, 37°C
0.2
L-cysteine
pH 8.0, 37°C, recombinant wild-type enzyme
0.2
L-cysteine
pH 8.0, 37°C, recombinant mutant Y114F/C116H
0.3
L-cysteine
pH 8.0, 37°C, recombinant mutant C166H
0.3
L-cysteine
pH 8.0, 37°C, recombinant mutants K240R and K240M
0.32
L-cysteine
pH 7.6, 37°C
0.34
L-cysteine
mutant C110G, pH 7.0, 37°C
0.39
L-cysteine
mutant enzyme C116A, at 37°C
0.46
L-cysteine
mutant C110S, pH 7.0, 37°C
0.53
L-cysteine
wild type enzyme, at 37°C
0.63
L-cysteine
pH 7.6, 37°C
0.63
L-cysteine
mutant enzyme C116H, at 37°C
0.64
L-cysteine
wild-type ehMGL1, pH 7.0, 37°C
1
L-cysteine
pH 8.0, 37°C, recombinant mutants K240I and K240N
1.01
L-cysteine
mutant Y108F, pH 7.0, 37°C
1.7
L-cysteine
wild-type ehMGL2, pH 7.0, 37°C
0.2
L-ethionine
-
-
0.2
L-ethionine
-
37°C, pH 8.0
0.27
L-ethionine
-
37°C, pH 8.0
0.54
L-ethionine
recombinant enzyme
0.56
L-ethionine
wild-type
6.2
L-ethionine
-
recombinant MGL2, C116G
12.2
L-ethionine
-
recombinant MGL1
15.2
L-ethionine
-
recombinant MGL1, C113G
37.2
L-ethionine
-
recombinant MGL2
1.78
L-homocysteine
pH 8.0, 37°C
30
L-homoserine
-
-
30
L-homoserine
-
37°C, pH 8.0
0.0013
L-methionine
-
-
0.04
L-methionine
pH 8.0, 37°C, recombinant mutant K240R
0.11
L-methionine
mutant enzyme C116S, at 37°C
0.19
L-methionine
mutant C110G, pH 7.0, 37°C
0.3
L-methionine
mutant C115A, pH 8.0, 30°C
0.432
L-methionine
-
pH 8.0, 30°C, recombinant enzyme
0.5
L-methionine
pH 8.0, 37°C, recombinant wild-type enzyme
0.61
L-methionine
wild-type ehMGL1, pH 7.0, 37°C
0.7
L-methionine
wild-type
0.7
L-methionine
recombinant enzyme
0.7
L-methionine
-
pH 8.0, 30°C
0.7
L-methionine
-
30°C, pH 8.0
0.72
L-methionine
mutant C110S, pH 7.0, 37°C
0.8
L-methionine
wild-type, pH 7.2, 30°C
0.9
L-methionine
-
37°C, pH 8.0
0.92
L-methionine
wild type enzyme, at 37°C
0.94
L-methionine
36°C, pH 6.8, recombinant EhMGL1
0.947
L-methionine
-
pH 8.0, 30°C, recombinant enzyme
1.2
L-methionine
pH 7.5, 37°C
1.42
L-methionine
mutant enzyme C116H, at 37°C
1.6
L-methionine
pH 8.0, 37°C
1.6
L-methionine
mutant P360Q, pH 7.2, 30°C
1.7
L-methionine
-
37°C, pH 8.0
1.77
L-methionine
-
pH 8.0, 30°C, recombinant enzyme
1.9
L-methionine
36°C, pH 6.8, recombinant EhMGL2
2.3
L-methionine
pH 8.0, 37°C, recombinant mutant C166H
2.7
L-methionine
mutant V358Y, pH 7.2, 30°C
2.85
L-methionine
mutant enzyme C116A, at 37°C
3.58
L-methionine
wild-type ehMGL2, pH 7.0, 37°C
3.7
L-methionine
mutant P357I, pH 7.2, 30°C
4.8
L-methionine
pH 8.0, 37°C, recombinant mutant K240I
5.5
L-methionine
mutant A366Y, pH 7.2, 30°C
5.7
L-methionine
pH 8.0, 37°C, recombinant mutant K240M
9.8
L-methionine
pH 8.0, 37°C, recombinant mutant K240N
10.6
L-methionine
-
pH 7.2, 30°C
15.12
L-methionine
mutant C113S, pH 7.0, 37°C
19.65
L-methionine
mutant Y58F, pH 8.0, 30°C
98
L-methionine
pH 8.0, 23°C
4
L-methionine sulfone
-
pH 8.0, 30°C
8.22
L-methionine sulfone
-
37°C, pH 8.0
38
L-methionine sulfone
pH 7.5, 37°C
6.2
L-methionine sulfoxide
-
pH 8.0, 30°C
7.07
L-methionine sulfoxide
-
pH 8.0, 30°C, recombinant enzyme
12.22
L-methionine sulfoxide
-
pH 8.0, 30°C, recombinant enzyme
33.51
L-methionine sulfoxide
-
pH 8.0, 30°C, recombinant enzyme
6.7
L-Vinylglycine
-
pH 8.0, 30°C
7.22
L-Vinylglycine
-
37°C, pH 8.0
0.57
methiin
mutant C115H, pH 8.0, 30°C
0.63
methiin
mutant C115A, pH 8.0, 30°C
2.22
O-acetyl-L-homoserine
-
37°C, pH 8.0
2.46
O-acetyl-L-homoserine
mutant C115H, pH 8.0, 30°C
6
O-acetyl-L-homoserine
mutant C115A, pH 8.0, 30°C
2.88
O-acetyl-L-serine
mutant C115A, pH 8.0, 30°C
3.68
O-acetyl-L-serine
mutant C115H, pH 8.0, 30°C
6.28
O-acetyl-L-serine
wild-type ehMGL1, pH 7.0, 37°C
52.33
O-acetyl-L-serine
wild-type ehMGL2, pH 7.0, 37°C
0.18
S-Benzyl-L-cysteine
recombinant enzyme
0.18
S-Benzyl-L-cysteine
-
30°C, pH 8.0
0.19
S-Benzyl-L-cysteine
wild-type
0.348
S-Benzyl-L-cysteine
-
pH 8.0, 30°C, recombinant enzyme
0.766
S-Benzyl-L-cysteine
-
pH 8.0, 30°C, recombinant enzyme
1.47
S-Benzyl-L-cysteine
-
pH 8.0, 30°C, recombinant enzyme
2.75
S-Benzyl-L-cysteine
mutant Y58F, pH 8.0, 30°C
0.17
S-ethyl-L-cysteine
recombinant enzyme
0.17
S-ethyl-L-cysteine
-
30°C, pH 8.0
0.17
S-ethyl-L-cysteine
pH and temperature not specified in the publication
0.26
S-ethyl-L-cysteine
mutant C115A, pH 8.0, 30°C
0.358
S-ethyl-L-cysteine
-
pH 8.0, 30°C, recombinant enzyme
0.48
S-ethyl-L-cysteine
-
37°C, pH 8.0
0.49
S-ethyl-L-cysteine
wild-type
0.72
S-ethyl-L-cysteine
-
pH 8.0, 30°C, recombinant enzyme
0.93
S-ethyl-L-cysteine
mutant C115H, pH 8.0, 30°C
2.17
S-ethyl-L-cysteine
-
pH 8.0, 30°C, recombinant enzyme
8.19
S-ethyl-L-cysteine
mutant Y58F, pH 8.0, 30°C
0.278
S-ethyl-L-homocysteine
-
pH 8.0, 30°C, recombinant enzyme
0.5
S-ethyl-L-homocysteine
-
30°C, pH 8.0
0.545
S-ethyl-L-homocysteine
-
pH 8.0, 30°C, recombinant enzyme
0.93
S-ethyl-L-homocysteine
-
pH 8.0, 30°C, recombinant enzyme
8.11
S-ethyl-L-homocysteine
mutant Y58F, pH 8.0, 30°C
0.4
S-methyl-L-cysteine
-
37°C, pH 8.0
0.4
S-methyl-L-cysteine
pH 8.0, 37°C, recombinant mutant Y114F/C116H
0.61
S-methyl-L-cysteine
-
-
0.61
S-methyl-L-cysteine
wild-type
0.69
S-methyl-L-cysteine
-
-
0.7
S-methyl-L-cysteine
pH 8.0, 37°C, recombinant wild-type enzyme
0.71
S-methyl-L-cysteine
recombinant enzyme
0.71
S-methyl-L-cysteine
-
30°C, pH 8.0
0.77
S-methyl-L-cysteine
-
-
0.8
S-methyl-L-cysteine
mutant C115A, pH 8.0, 30°C
1.4
S-methyl-L-cysteine
-
-
2.1
S-methyl-L-cysteine
pH 8.0, 37°C, recombinant mutant C166H
2.62
S-methyl-L-cysteine
mutant C115H, pH 8.0, 30°C
0.1
trifluoromethionine
-
-
0.1
trifluoromethionine
wild-type ehMGL1, pH 7.0, 37°C
0.29
trifluoromethionine
mutant Y111F, pH 7.0, 37°C
0.57
trifluoromethionine
mutant Y108F, pH 7.0, 37°C
0.83
trifluoromethionine
mutant R55A, pH 7.0, 37°C
0.92
trifluoromethionine
wild-type ehMGL2, pH 7.0, 37°C
1.62
trifluoromethionine
mutant R58A, pH 7.0, 37°C
5.45
trifluoromethionine
mutant C113S, pH 7.0, 37°C
additional information
L-methionine
-
values between 0.8 to 1.7, depending on publications
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
values for native and cyanylated enzyme
-
additional information
additional information
steady-state kinetics
-
additional information
additional information
-
steady-state kinetics for beta- and gamma-elimination reactions, overview
-
additional information
additional information
-
steady-state kinetics for beta- and gamma-elimination reactions, overview
-
additional information
additional information
-
steady-state kinetics for beta- and gamma-elimination reactions, overview
-
additional information
additional information
-
steady-state kinetics for beta- and gamma-elimination reactions, overview
-
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445-467
2010
Achromobacter starkeyi, Aeromonas sp., Aspergillus flavipes, Aspergillus sp., Citrobacter freundii, Citrobacter intermedius, Cladosporium cladosporioides, Clostridium sporogenes, Entamoeba histolytica, Lactococcus lactis, no activity in mammalia, Pseudomonas putida, Treponema denticola, Trichomonas vaginalis, Brevibacterium linens BL2, Aspergillus sp. Rs-1a
brenda
Faleev, N.G.; Alferov, K.V.; Tsvetikova, M.A.; Morozova, E.A.; Revtovich, S.V.; Khurs, E.N.; Vorobev, M.M.; Phillips, R.S.; Demidkina, T.V.; Khomutov, R.M.
Methionine gamma-lyase: mechanistic deductions from the kinetic pH-effects. The role of the ionic state of a substrate in the enzymatic activity
Biochim. Biophys. Acta
1794
1414-1420
2009
Citrobacter freundii
brenda
Sato, D.; Kobayashi, S.; Yasui, H.; Shibata, N.; Toru, T.; Yamamoto, M.; Tokoro, G.; Ali, V.; Soga, T.; Takeuchi, T.; Suematsu, M.; Nozaki, T.
Cytotoxic effect of amide derivatives of trifluoromethionine against the enteric protozoan parasite Entamoeba histolytica
Int. J. Antimicrob. Agents
35
56-61
2010
Entamoeba histolytica
brenda
Sato, D.; Nozaki, T.
Methionine gamma-lyase: the unique reaction mechanism, physiological roles, and therapeutic applications against infectious diseases and cancers
IUBMB Life
61
1019-1028
2009
Arabidopsis thaliana, Porphyromonas gingivalis, Brevibacterium linens, Entamoeba histolytica, Fusobacterium nucleatum, Prevotella denticola, Pseudomonas putida, Trichomonas vaginalis (O15564), Trichomonas vaginalis (O15565)
brenda
El-Sayed, A.S.
L-methioninase production by Aspergillus flavipes under solid-state fermentation
J. Basic Microbiol.
49
331-341
2009
Aspergillus flavipes
brenda
Palwai, N.R.; Zang, X.P.; Harrison, R.G.; Benbrook, D.; Pento, J.T.
Selective growth inhibition of cancer cells by L-methioninase-containing fusion protein targeted to the urokinase receptor
Pharmacology
84
271-275
2009
Escherichia coli BL21
brenda
Joshi, V.; Jander, G.
Arabidopsis methionine gamma-lyase is regulated according to isoleucine biosynthesis needs but plays a subordinate role to threonine deaminase
Plant Physiol.
151
367-378
2009
Arabidopsis thaliana (Q9SGU9)
brenda
Morozova, E.A.; Bazhulina, N.P.; Anufrieva, N.V.; Mamaeva, D.V.; Tkachev, Y.V.; Streltsov, S.A.; Timofeev, V.P.; Faleev, N.G.; Demidkina, T.V.
Kinetic and spectral parameters of interaction of Citrobacter freundii methionine gamma-lyase with amino acids
Biochemistry (Moscow)
75
1272-1280
2010
Citrobacter freundii
brenda
Ronda, L.; Bazhulina, N.P.; Morozova, E.A.; Revtovich, S.V.; Chekhov, V.O.; Nikulin, A.D.; Demidkina, T.V.; Mozzarelli, A.
Exploring methionine gamma-lyase structure-function relationship via microspectrophotometry and X-ray crystallography
Biochim. Biophys. Acta
1814
834-842
2011
Citrobacter freundii
brenda
Suwabe, K.; Yoshida, Y.; Nagano, K.; Yoshimura, F.
Identification of an L-methionine gamma-lyase involved in the production of hydrogen sulfide from L-cysteine in Fusobacterium nucleatum subsp. nucleatum ATCC 25586
Microbiology
157
2992-3000
2011
Treponema denticola (Q73KL7), Porphyromonas gingivalis (Q7MX71), Fusobacterium nucleatum subsp. nucleatum (Q8RDT4), Porphyromonas gingivalis W83 (Q7MX71), Treponema denticola ATCC 35405 (Q73KL7), Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847 (Q8RDT4)
brenda
Morozova, E.A.; Kulikova, V.V.; Yashin, D.V.; Anufrieva, N.V.; Anisimova, N.Y.; Revtovich, S.V.; Kotlov, M.I.; Belyi, Y.F.; Pokrovsky, V.S.; Demidkina, T.V.
Kinetic parameters and cytotoxic activity of recombinant methionine gamma-lyase from Clostridium tetani, Clostridium sporogenes, Porphyromonas gingivalis and Citrobacter freundii
Acta Naturae
5
92-98
2013
Porphyromonas gingivalis, Citrobacter freundii, Clostridium sporogenes, Clostridium tetani
brenda
Saa, L.; Mato, J.M.; Pavlov, V.
Assays for methionine beta-lyase and S-adenosyl-L-homocysteine hydrolase based on enzymatic formation of CdS quantum dots in situ
Anal. Chem.
84
8961-8965
2012
Pseudomonas putida, Pseudomonas putida ICR 3460
brenda
Revtovich, S.V.; Morozova, E.A.; Khurs, E.N.; Zakomirdina, L.N.; Nikulin, A.D.; Demidkina, T.V.; Khomutov, R.M.
Three-dimensional structures of noncovalent complexes of Citrobacter freundii methionine gamma-lyase with substrates
Biochemistry (Moscow)
76
564-570
2011
Citrobacter freundii (Q84AR1)
brenda
Revtovich, S.V.; Faleev, N.G.; Morozova, E.A.; Anufrieva, N.V.; Nikulin, A.D.; Demidkina, T.V.
Crystal structure of the external aldimine of Citrobacter freundii methionine gamma-lyase with glycine provides insight in mechanisms of two stages of physiological reaction and isotope exchange of alpha- and beta-protons of competitive inhibitors
Biochimie
101
161-167
2014
Citrobacter freundii (Q84AR1)
brenda
Fukumoto, M.; Kudou, D.; Murano, S.; Shiba, T.; Sato, D.; Tamura, T.; Harada, S.; Inagaki, K.
The role of amino acid residues in the active site of L-methionine gamma-lyase from Pseudomonas putida
Biosci. Biotechnol. Biochem.
76
1275-1284
2012
Pseudomonas putida (P13254)
brenda
Huang, T.; Joshi, V.; Jander, G.
The catabolic enzyme methionine gamma-lyase limits methionine accumulation in potato tubers
Plant Biotechnol. J.
12
883-893
2014
Solanum tuberosum
brenda
Khan, M.A.; Lopez-Munoz, M.M.; Kaspar, C.W.; Hung, K.F.
Activities of methionine-gamma-lyase in the acidophilic archaeon Ferroplasma acidarmanus strain fer1
Res. Rep. Biol.
4
11-22
2013
Ferroplasma acidarmanus, Ferroplasma acidarmanus Fer1
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brenda
Revtovich, S.; Anufrieva, N.; Morozova, E.; Kulikova, V.; Nikulin, A.; Demidkina, T.
Structure of methionine gamma-lyase from Clostridium sporogenes
Acta Crystallogr. Sect. F
72
65-71
2016
Clostridium sporogenes (J7TA22), Clostridium sporogenes, Clostridium sporogenes ATCC 15579 (J7TA22)
brenda
Foo, T.C.; Terentis, A.C.; Venkatachalam, K.V.
A continuous spectrophotometric assay and nonlinear kinetic analysis of methionine gamma-lyase catalysis
Anal. Biochem.
507
21-26
2016
Porphyromonas gingivalis (C3VMV9), Porphyromonas gingivalis
brenda
Anufrieva, N.V.; Faleev, N.G.; Morozova, E.A.; Bazhulina, N.P.; Revtovich, S.V.; Timofeev, V.P.; Tkachev, Y.V.; Nikulin, A.D.; Demidkina, T.V.
The role of active site tyrosine 58 in Citrobacter freundii methionine gamma-lyase
Biochim. Biophys. Acta
1854
1220-1228
2015
Citrobacter freundii (Q84AR1), Citrobacter freundii
brenda
Revtovich, S.V.; Morozova, E.A.; Kulikova, V.V.; Anufrieva, N.V.; Osipova, T.I.; Koval, V.S.; Nikulin, A.D.; Demidkina, T.V.
Crystal structure of mutant form Cys115His of Citrobacter freundii methionine gamma-lyase complexed with l-norleucine
Biochim. Biophys. Acta
1865
1123-1128
2017
Citrobacter freundii (Q84AR1)
brenda
Raboni, S.; Revtovich, S.; Demitri, N.; Giabbai, B.; Storici, P.; Cocconcelli, C.; Faggiano, S.; Rosini, E.; Pollegioni, L.; Galati, S.; Buschini, A.; Morozova, E.; Kulikova, V.; Nikulin, A.; Gabellieri, E.; Cioni, P.; Demidkina, T.; Mozzarelli, A.
Engineering methionine gamma-lyase from Citrobacter freundii for anticancer activity
Biochim. Biophys. Acta
1866
1260-1270
2018
Citrobacter freundii (Q84AR1), Citrobacter freundii
brenda
Morozova, E.; Kulikova, V.; Rodionov, A.; Revtovich, S.; Anufrieva, N.; Demidkina, T.
Engineered Citrobacter freundii methionine gamma-lyase effectively produces antimicrobial thiosulfinates
Biochimie
128-129
92-98
2016
Citrobacter freundii (Q84AR1), Citrobacter freundii
brenda
Kulikova, V.; Morozova, E.; Rodionov, A.; Koval, V.; Anufrieva, N.; Revtovich, S.; Demidkina, T.
Non-stereoselective decomposition of (+-)-S-alk(en)yl-l-cysteine sulfoxides to antibacterial thiosulfinates catalyzed by C115H mutant methionine gamma-lyase from Citrobacter freundii
Biochimie
151
42-44
2018
Citrobacter freundii (Q84AR1), Citrobacter freundii
brenda
Morozova, E.A.; Anufrieva, N.V.; Davydov, D.Z.; Komarova, M.V.; Dyakov, I.N.; Rodionov, A.N.; Demidkina, T.V.; Pokrovsky, V.S.
Plasma methionine depletion and pharmacokinetic properties in mice of methionine gamma-lyase from Citrobacter freundii, Clostridium tetani and Clostridium sporogenes
Biomed. Pharmacother.
88
978-984
2017
Clostridium tetani (A0A1L7H888), Clostridium tetani, Clostridium sporogenes (J7TA22), Clostridium sporogenes, Citrobacter freundii (Q84AR1), Citrobacter freundii, Clostridium sporogenes ATCC 15579 (J7TA22)
brenda
Song, H.; Xu, R.; Guo, Z.
Identification and characterization of a methionine gamma-lyase in the calicheamicin biosynthetic cluster of Micromonospora echinospora
ChemBioChem
16
100-109
2015
Micromonospora echinospora (Q8KNG3), Micromonospora echinospora
brenda
Kumar, P.; Jander, G.
Concurrent overexpression of Arabidopsis thaliana cystathionine gamma-synthase and silencing of endogenous methionine gamma-lyase enhance tuber methionine content in Solanum tuberosum
J. Agric. Food Chem.
65
2737-2742
2017
Solanum tuberosum
brenda
Kuznetsov, N.A.; Faleev, N.G.; Kuznetsova, A.A.; Morozova, E.A.; Revtovich, S.V.; Anufrieva, N.V.; Nikulin, A.D.; Fedorova, O.S.; Demidkina, T.V.
Pre-steady-state kinetic and structural analysis of interaction of methionine gamma-lyase from Citrobacter freundii with inhibitors
J. Biol. Chem.
290
671-681
2015
Citrobacter freundii (Q84AR1), Citrobacter freundii
brenda
Kudou, D.; Yasuda, E.; Hirai, Y.; Tamura, T.; Inagaki, K.
Molecular cloning and characterization of L-methionine gamma-lyase from Streptomyces avermitilis
J. Biosci. Bioeng.
120
380-383
2015
Streptomyces avermitilis (Q826W3), Streptomyces avermitilis, Streptomyces avermitilis DSM 46492 (Q826W3)
brenda
Morozova, E.A.; Kulikova, V.V.; Faggiano, S.; Raboni, S.; Gabellieri, E.; Cioni, P.; Anufrieva, N.V.; Revtovich, S.V.; Demidkina, T.; Mozzarelli, A.
Soluble and nanoporous silica gel-entrapped C. freundii methionine gamma-lyase
J. Nanosci. Nanotechnol.
18
2210-2219
2018
Citrobacter freundii (Q84AR1)
brenda
Huang, K.Y.; Hu, H.Y.; Tang, Y.L.; Xia, F.G.; Luo, X.Q.; Liu, J.Z.
High-level expression, purification and large-scale production of L-methionine gamma-lyase from Idiomarina as a novel anti-leukemic drug
Mar. Drugs
13
5492-5507
2015
Idiomarina sp.
brenda
Stephen, A.; Millhouse, E.; Sherry, L.; Aduse-Opoku, J.; Culshaw, S.; Ramage, G.; Bradshaw, D.; Burnett, G.; Allaker, R.
In vitro effect of Porphyromonas gingivalis methionine gamma lyase on biofilm composition and oral inflammatory response
PLoS ONE
11
e0169157
2016
Porphyromonas gingivalis
brenda
Sato, D.; Shiba, T.; Yunoto, S.; Furutani, K.; Fukumoto, M.; Kudou, D.; Tamura, T.; Inagaki, K.; Harada, S.
Structural and mechanistic insights into homocysteine degradation by a mutant of methionine gamma-lyase based on substrate-assisted catalysis
Protein Sci.
26
1224-1230
2017
Pseudomonas putida (P13254), Pseudomonas putida
brenda
Cao, H.; Tan, K.; Wang, F.; Bigelow, L.; Yennamalli, R.; Jedrzejczak, R.; Babnigg, G.; Bingman, C.; Joachimiak, A.; Kharel, M.; Singh, S.; Thorson, J.; Phillips, G.J.
Structural dynamics of a methionine gamma-lyase for calicheamicin biosynthesis Rotation of the conserved tyrosine stacking with pyridoxal phosphate
Struct. Dyn.
3
034702
2016
Micromonospora echinospora (Q8KNG3), Micromonospora echinospora
brenda
Lin, B.; Tian, G.; Liu, Y.
Mechanistic insights into the gamma-elimination reaction of L-methionine catalyzed by methionine gamma-lyase (MGL)
Theoret. Chem. Accounts
136
105
2017
Clostridium sporogenes (J7TA22), Citrobacter freundii (Q84AR1), Clostridium sporogenes ATCC 15579 (J7TA22)
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brenda