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Enzyme Nomenclature
Information on EC 4.4.1.11 - methionine gamma-lyase
for references in articles please use BRENDA:EC4.4.1.11
Word Map on EC 4.4.1.11
- 4.4.1.11
-
lipase
-
endocannabinoids
- monoacylglycerol
- cannabinoids
- 2-arachidonoylglycerol
-
lectin
- putida
- medicine
-
c-type
- pyridoxal
- monoglyceride
- selenomethionine
-
galactose-type
- methylselenol
-
2-arachidonoyl
- anandamide
- galnac
- freundii
- alpha-ketobutyrate
-
methionine-dependent
- mercaptan
-
beta-lyase
-
semet
-
malodor
-
s-substituted
-
dc-sign
-
5'-phosphate-dependent
-
galactose-binding
- drug development
- environmental protection
- analysis
- nutrition
- synthesis
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
4.4.1.11
-
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RECOMMENDED NAME
GeneOntology No.
methionine gamma-lyase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-methionine + H2O = methanethiol + NH3 + 2-oxobutanoate
cleavage of C-N bond in addition to C-S, C-Se and C-O bond at beta-position of amino acids by elimination and replacement reactions
-
L-methionine + H2O = methanethiol + NH3 + 2-oxobutanoate
cleavage of C-N bond in addition to C-S, C-Se and C-O bond at beta-position of amino acids by elimination and replacement reactions
-
L-methionine + H2O = methanethiol + NH3 + 2-oxobutanoate
rate determining stage of the enzymatic reaction is deamination of aminocrotonate, important contribution of the sulfur atom and methylene groups to the efficiency of binding of substrates and inhibitors
-
L-methionine + H2O = methanethiol + NH3 + 2-oxobutanoate
gamma-elimination reaction mechanism and intermediates, overview
-
L-methionine + H2O = methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination
-
-
alpha,gamma and alpha,beta-elimination; gamma-replacement; of H2S or RSH, C-S bond cleavage
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
L-methionine methanethiol-lyase (deaminating; 2-oxobutanoate-forming)
A pyridoxal-phosphate protein. The enzyme cleaves a carbon-sulfur bond, releasing methanethiol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form 2-oxobutanoate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. The enzyme is involved in L-methionine catabolism.
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CAS REGISTRY NUMBER
COMMENTARY
42616-25-1
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
expression of enzyme is induced in response to high methionine levels
-
-
black-pigmented anaerobe strongly implicated as a major pathogen in adult periodontitis, growth of Porphyromonas gingivalis is inhibited by L-trifluoromethionine
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the enzyme belongs to the subclass of cystathionine beta-lyase with type I folding of the polypeptide chain of pyridoxal 5'-phosphate-dependent enzymes
malfunction
-
in planta silencing of StMGL1 results in an increased methionine to isoleucine ratio in the free amino acid profile of potato tubers and, in some transgenic lines, elevated accumulation of free methionine. In both wild-type and transgenic tubers, the ratio of methionine to isoleucine is negatively correlated with the level of StMGL1 transcript
metabolism
physiological function
additional information
metabolism
-
the enzyme is responsible for the alpha,beta,gamma-elimination and gamma,beta-replacement in analogues of L-methionione such as L-homocysteine, through degradation to keto acids, ammonia, and H2S in anaerobic bacteria and parasitic protozoa
metabolism
-
the enzyme is responsible for the alpha,beta,gamma-elimination and gamma,beta-replacement in analogues of L-methionione such as L-homocysteine, through degradation to keto acids, ammonia, and H2S in anaerobic bacteria and parasitic protozoa
-
physiological function
-
under drought conditions and in reproductive tissue enzyme might play significant role as an alternate route to fulfill increased demand for isoleucine
physiological function
-
isoleucine biosynthesis, sulfur storage, involved in the alternative reverse-transsulfuration pathway, important roe in the resumption process
physiological function
-
involvled in pathogenicity of periodontal bacterium
physiological function
the amount of H2S produced by Fn1419 is estimated to be 1.9% of the total H2S produced from L-cysteine in Fusobacterium nucleatum ATCC 25586
physiological function
-
the pyridoxal5'-phosphate-dependent enzyme catalyzes the gamma-elimination and gamma-replacement of L-methionine and its derivatives and the reactions of beta-elimination and beta-replacement of L-cysteine and S-substituted L-cysteines. The enzyme also catalyzes the reactions of gamma-elimination and gamma-replacement of the phosphinic analogue of methionine, Met-PH. Met-PH has a high antibacterial activity, is an effective fungi cide under field conditions, and inhibits the growth of tumor cells due to transformation into a metabolically stable phosphonic analog of S-adenosylmethionine
physiological function
-
the catabolic enzyme methionine gamma-lyase limits methionine accumulation in potato tubers. In both wild-type and transgenic tubers, the ratio of methionine to isoleucine is negatively correlated with the level of StMGL1 transcript
physiological function
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847
-
the amount of H2S produced by Fn1419 is estimated to be 1.9% of the total H2S produced from L-cysteine in Fusobacterium nucleatum ATCC 25586
-
additional information
-
catalytic residues: Lys210 is the base, and Tyr113 acts as a general acid, active site structure, overview
additional information
-
general acid catalytic residue is conserved Tyr114, conserved residue Lys240 is important for substrate recognition and structural stability, conserved residue Asp241 is also important in the elimination reaction, structure-function analysis, overview
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
?
DL-2-amino-3-(N-hydroxyethylamino)-propionic acid
ethanolamine + NH3 + pyruvate
-
-
-
?
DL-2-amino-3-(N-methylamino)propionic acid
methylamine + NH3 + pyruvate
-
-
-
?
DL-homocysteine + H2O
H2S + S-(beta-hydroxyethyl)-L-homocysteine
-
gamma-replacement reaction, wild-type enzyme
-
-
?
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-cysteine + H2O
H2S + S-(beta-hydroxyethyl)-L-cysteine
-
beta-replacement reaction, wild-type enzyme and mutant C116H
-
-
?
L-methionine + 2-mercaptoethanol
methanethiol + S-(beta-hydroxyethyl)-L-homocysteine
-
gamma-replacement reaction, wild-type enzyme
-
-
?
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
ethanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
selenoethionine + H2O
ethylselenol + NH3 + 2-oxobutanoate
-
-
-
?
trifluoromethionine + H2O
trifluoromethanethiol + NH3 + 2-oxobutanoate
-
-
-
?
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
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
-
-
?
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
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847
-
-
-
?
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-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
-
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
-
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
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
Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847
-
-
-
?
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
-
gamma-elimination reaction
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
-
?
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
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
ethanethiol + NH3 + 2-oxopropanoate
-
-
-
?
S-ethyl-L-cysteine + H2O
ethanethiol + NH3 + 2-oxopropanoate
-
weak activity
-
-
?
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
-
-
?
selenomethionine + H2O
methylselenol + NH3 + 2-oxobutanoate
-
-
-
?
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
?
-
-
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
?
-
-
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 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
?
-
-
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
?
-
-
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
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
gamma-elimination reaction
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
Q84AR1
-
-
-
?
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
Q86D27, Q86D28
-
-
?
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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
increases the half-life of methoxypolyethylene glycol succinimidyl glutarate 5000 treated recombinant METase holoenzyme in a dose-dependent manner
pyridoxal 5'-phosphate
-
absence of an aldimine bond between the active site Lys210 and pyridoxal 5'-phosphate in enzyme crystals, grown in monomethyl ether polyethylene glycol 2000 in the presence of ammonium sulfate
pyridoxal 5'-phosphate
-
4 mol of pyridoxal 5'-phosphate per mole of enzyme
pyridoxal 5'-phosphate
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cd2+
Co2+
Cu2+
Li+
Mg2+
Mn2+
Co2+
-
increased enzyme activity after preincubation of the enzyme for 2 h
Cu2+
-
increased enzyme activity after preincubation of the enzyme for 2 h
Mg2+
-
increased enzyme activity after preincubation of the enzyme for 2 h
Mn2+
-
increased enzyme activity after preincubation of the enzyme for 2 h
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-2-amino-4-chloro-4-pentenoate
-
complete inhibition at 5 mol per mol of tetramer enzyme
DL-propargylglycine
; irreversible slow-binding inhibition
DL-propargylglycine
-
inhibition profiles of wild-type and mutant enzymes, overview
glycine
-
competitive inhibitor, subtle conformational changes provide effective binding of the inhibitor and facilitate labilization of Calpha-protons of the external aldimine, binding structure, overview
L-norleucine
-
Arg374 and Ser339 are involved in the binding of carboxyl groups of the inhibitor, the hydroxyl of Tyr113 is a potential acceptor of a proton from the amino groups of the amino acid
additional information
-
recombinant METase alone inhibits the proliferation of 15/15 NB cell lines in vitro in a dose-dependent manner
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.2
L-1-amino-3-methylthiopropylphosphinic acid
-
pH and temperature not specified in the publication
1.4
DL-homocysteine
-
pH 8.0, 37°C, recombinant mutant C166H; pH 8.0, 37°C, recombinant mutant K240M
0.2
L-cysteine
-
pH 8.0, 37°C, recombinant mutant Y114F/C116H; pH 8.0, 37°C, recombinant wild-type enzyme
0.3
L-cysteine
-
pH 8.0, 37°C, recombinant mutant C166H; pH 8.0, 37°C, recombinant mutants K240R and K240M
0.17
S-ethyl-L-cysteine
-
pH and temperature not specified in the publication
additional information
L-methionine
-
values between 0.8 to 1.7, depending on publications
additional information
additional information
-
values for native and cyanylated enzyme
-
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
L-methionine
-
values between 25.3 to 48.6, depending on publications
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.8
DL-homocysteine