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Information on EC 4.4.1.11 - methionine gamma-lyase
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4.4.1.11 methionine gamma-lyaseIUBMB Comments
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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Word Map
- 4.4.1.11
- lipase
-
endocannabinoids
- monoacylglycerol
- cannabinoids
- lectin
- 2-arachidonoylglycerol
-
c-type
- monoglyceride
- pyridoxal
- putida
- medicine
-
orthotopic
-
galactose-type
- anandamide
-
2-arachidonoyl
- galnac
- selenomethionine
-
citrobacter
- freundii
-
methionine-dependent
- methylselenol
- mercaptan
- alpha-ketobutyrate
-
meibomian
-
5'-phosphate-dependent
-
rimonabant
-
dc-sign
-
s-substituted
-
beta-lyase
-
galactose-binding
-
malodor
- nutrition
- environmental protection
- synthesis
- analysis
- drug development
The enzyme appears in viruses and cellular organisms
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EhMGL1
EhMGL2
fer1MgL2
Fn1419
L-methionase
L-methioninase
L-methionine gamma-lyase
L-methionine-alpha-deamino-gamma-mercaptomethane lyase
L-methionine-alpha-deamino-gamma-mercaptomethane-lyase
L-methionine-gamma-lyase
lyase, methionine
-
-
-
-
MegL
METase
methioninase
methionine dethiomethylase
-
-
-
-
methionine gamma-lyase
methionine lyase
-
-
-
-
methionine-gamma-lyase
MGL
sav7062
YtjE
L-methioninase
-
-
-
-
L-methionine gamma-lyase
-
-
-
-
L-methionine-alpha-deamino-gamma-mercaptomethane-lyase
-
-
-
-
methioninase
-
-
-
-
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
elimination
-
-
of H2S or RSH, C-S bond cleavage
-
elimination
-
-
alpha,gamma and alpha,beta-elimination
-
elimination
-
-
gamma-replacement
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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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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
(+)propiin + H2O
propane-1-sulfenic acid + pyruvate + NH3
-
-
-
?
(+-)-butiin + H2O
butane-1-sulfenic 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
-
?
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
2-oxobutanoate + NH3 + hydrogen sulfide
-
-
-
?
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
-
-
?
O-acetyl-L-homoserine + H2O
2-oxobutanoate + NH3 + acetate
-
-
-
?
S-butyl-L-cysteine + H2O
butanethiol + 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-propyl-L-cysteine + H2O
propanethiol + NH3 + 2-oxopropanoate
-
-
-
?
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-homocysteine + H2O
sulfide + 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
-
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
-
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
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
-
-
-
?
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
-
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
-
-
-
?
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-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
-
-
-
?
S-ethyl-L-cysteine + H2O
ethanethiol + NH3 + 2-oxopropanoate
weak activity
-
-
?
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
-
-
?
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
?
-
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
?
-
-
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
-
?
additional information
?
-
no activity with O-phospho-L-serine
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
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
gamma-elimination reaction
-
-
?
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
-
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
-
-
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
PLP-binding domain (residues 63-261) is typical for PLP-dependent enzymes with the type I fold
pyridoxal 5'-phosphate
protein-to-cofactor ratio is 2:1. The cofactor is removable by incubating with hydroxylamine hydrochloride and is readily restored by incubation with free PLP
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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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-2-amino-4-chloro-4-pentenoate
-
complete inhibition at 5 mol per mol of tetramer enzyme
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-Cycloserine
inactivation by L-cycloserine is completely reversed by dialysis against potassium phosphate buffer (pH 8.0), containing 0.5 mM PLP and 5 mM dithiothreitol
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
0.17
S-ethyl-L-cysteine
pH and temperature not specified in the publication
0.4
S-methyl-L-cysteine
pH 8.0, 37°C, recombinant mutant Y114F/C116H
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
-
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
0.057 - 0.65
DL-homocysteine
wild-type ehMGL2, pH 7.0, 37°C