Information on EC 4.4.1.11 - methionine gamma-lyase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
4.4.1.11
-
RECOMMENDED NAME
GeneOntology No.
methionine gamma-lyase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-methionine + H2O = methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
mechanism
-
L-methionine + H2O = methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
mechanism
-
L-methionine + H2O = methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
mechanism
-
L-methionine + H2O = methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
gamma-elimination reaction mechanism and intermediates, overview
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
elimination
-
-
of H2S or RSH, C-S bond cleavage, alpha,gamma and alpha,beta-elimination, gamma-replacement
-
PATHWAY
KEGG Link
MetaCyc Link
Cysteine and methionine metabolism
-
methionine metabolism
BRENDA
BRENDA
BRENDA
Selenocompound metabolism
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
EhMGL1
Q86D28
methionine gamma-lyase isoenzyme 1
EhMGL2
Q86D27
methionine gamma-lyase isoenzyme 2
Fn1419
Fusobacterium nucleatum subsp. nucleatum, ATCC 25586
Q8RDT4
-
-
L-methionase
-
-
L-methionase
-
-
L-methioninase
-
-
-
-
L-methioninase
Achromobacter starkeyi, Aeromonas sp.
-
-
L-methioninase
-
-
L-methioninase
-
-
L-methioninase
-
-
L-methioninase
Aspergillus sp. Rs-1a
-
-
-
L-methioninase
-
-
L-methioninase
-
-
L-methioninase
-
-
L-methioninase
-
-
L-methioninase
-
-
L-methioninase
-
-
L-methioninase
-
-
L-methionine gamma-lyase
-
-
-
-
L-methionine gamma-lyase
-
-
L-methionine gamma-lyase
Q84AR1
-
L-methionine gamma-lyase
Citrobacter freundii ATCC29063
Q84AR1
-
-
L-methionine gamma-lyase
-
-
L-methionine gamma-lyase
-
-
L-methionine gamma-lyase
P13254
-
L-methionine gamma-lyase 1
Q86D28
-
L-methionine-alpha-deamino-gamma-mercaptomethane lyase
-
-
L-methionine-alpha-deamino-gamma-mercaptomethane-lyase
-
-
-
-
L-methionine-alpha-deamino-gamma-mercaptomethane-lyase
-
-
L-methionine-alpha-deamino-gamma-mercaptomethane-lyase
-
-
L-methionine-gamma-lyase
-
-
L-methionine-gamma-lyase
Fusobacterium nucleatum JCM8532
-
-
-
L-methionine-gamma-lyase
-
-
L-methionine-gamma-lyase
-
-
-
L-methionine-gamma-lyase
-
-
L-methionine-gamma-lyase
Treponema denticola ATCC35405
-
-
-
lyase, methionine
-
-
-
-
methioninase
-
-
-
-
methioninase
-
-
methioninase
Fusobacterium nucleatum JCM8532
-
-
-
methioninase
-
-
methioninase
-
-
methioninase
-
-
-
methioninase
-
-
methioninase
Treponema denticola ATCC35405
-
-
-
methionine alpha,gamma-lyase
-
-
methionine dethiomethylase
-
-
-
-
methionine gamma-lyase
-
-
-
-
methionine gamma-lyase
-
-
methionine gamma-lyase
Q9SGU9
-
methionine gamma-lyase
-
-
methionine gamma-lyase
-
-
methionine gamma-lyase
-
-
methionine gamma-lyase
O15564, O15565
-
methionine lyase
-
-
-
-
methionine-gamma-lyase
Q5MQ31
-
methionine-gamma-lyase
-
-
MGL
Citrobacter freundii ATCC29063
Q84AR1
-
-
MGL
P13254
-
MGL
Pseudomonas putida ICR 3460
-
-
-
TvMGL1
O15564
-
TvMGL2
O15565
-
YtjE
Lactococcus lactis IL1403
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
42616-25-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Achromobacter starkeyi
-
-
-
Manually annotated by BRENDA team
expression of enzyme is induced in response to high methionine levels
-
-
Manually annotated by BRENDA team
variant Aspergillus flavus columnaris
-
-
Manually annotated by BRENDA team
Aspergillus sp. Rs-1a
-
-
-
Manually annotated by BRENDA team
ATCC 9175
SwissProt
Manually annotated by BRENDA team
ATCC29063
SwissProt
Manually annotated by BRENDA team
Citrobacter freundii ATCC29063
ATCC29063
SwissProt
Manually annotated by BRENDA team
isoenzyme 1
SwissProt
Manually annotated by BRENDA team
isoenzyme 2
SwissProt
Manually annotated by BRENDA team
isoform ehMGL1
SwissProt
Manually annotated by BRENDA team
isoform ehMGL2
SwissProt
Manually annotated by BRENDA team
strain JCM8532
-
-
Manually annotated by BRENDA team
Fusobacterium nucleatum JCM8532
strain JCM8532
-
-
Manually annotated by BRENDA team
Fusobacterium nucleatum subsp. nucleatum, ATCC 25586
-
UniProt
Manually annotated by BRENDA team
strain IL1403
-
-
Manually annotated by BRENDA team
Lactococcus lactis IL1403
strain IL1403
-
-
Manually annotated by BRENDA team
commercial product
-
-
Manually annotated by BRENDA team
no activity in mammalia
-
-
-
Manually annotated by BRENDA team
black-pigmented anaerobe strongly implicated as a major pathogen in adult periodontitis, growth of Porphyromonas gingivalis is inhibited by L-trifluoromethionine
-
-
Manually annotated by BRENDA team
strain PAO1
-
-
Manually annotated by BRENDA team
strain S-313
-
-
Manually annotated by BRENDA team
Pseudomonas putida ICR 3460
-
-
-
Manually annotated by BRENDA team
Pseudomonas putida S-313
strain S-313
-
-
Manually annotated by BRENDA team
cv. Desiree, gene StMGL1
-
-
Manually annotated by BRENDA team
ATCC 35405
-
-
Manually annotated by BRENDA team
strain ATCC35405
-
-
Manually annotated by BRENDA team
Treponema denticola ATCC35405
strain ATCC35405
-
-
Manually annotated by BRENDA team
additional information
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
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
Q9SGU9
involved in isoleucine biosynthesis
metabolism
-
involved in methionine metabolism
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
-
involvled in pathogenicity of periodontal bacterium
physiological function
-
isoleucine biosynthesis, sulfur storage, involved in the alternative reverse-transsulfuration pathway, important roe in the resumption process
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
Q8RDT4
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 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
-
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
Fusobacterium nucleatum subsp. nucleatum, ATCC 25586
-
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
-
metabolism
Pseudomonas putida ICR 3460
-
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
-
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-amino-3-(methylthio)propylphosphinic acid + H2O
1-oxopropylphosphinic acid + methanethiol + NH3
show the reaction diagram
-
-
-
?
2-amino-3-(N,N-dimethylamino)propionic acid
2-iminopropionic acid + ?
show the reaction diagram
-
C-N-bond cleavage
-
?
beta-(S-ethyl-L-cysteine)
?
show the reaction diagram
Q84AR1
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
-
-
?
beta-chloro-L-alanine + H2O
?
show the reaction diagram
-
-
-
-
?
cystathionine + ?
?
show the reaction diagram
-
-
-
-
?
DL-2-amino-3-(N-hydroxyethylamino)-propionic acid
ethanolamine + NH3 + pyruvate
show the reaction diagram
-
-
-
?
DL-2-amino-3-(N-methylamino)propionic acid
methylamine + NH3 + pyruvate
show the reaction diagram
-
-
-
?
DL-ethionine + H2O
?
show the reaction diagram
-
-
-
-
?
DL-homocysteic acid + H2O
?
show the reaction diagram
-
-
-
-
?
DL-homocysteine + H2O
2-oxobutanoate + NH3 + H2S
show the reaction diagram
-
-
-
-
?
DL-homocysteine + H2O
2-oxobutanoate + NH3 + H2S
show the reaction diagram
-, Q86D27, Q86D28
112% of activity with L-methionine
-
?
DL-homocysteine + H2O
2-oxobutanoate + NH3 + H2S
show the reaction diagram
-, Q86D27, Q86D28
294% of EhMGL1 activity with L-methionine
-
?
DL-homocysteine + H2O
hydrogen sulfide + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
DL-homocysteine + H2O
hydrogen sulfide + NH3 + 2-oxobutanoate
show the reaction diagram
-, Q86D27, Q86D28
-
-
-
-
DL-homocysteine + H2O
hydrogen sulfide + NH3 + 2-oxobutanoate
show the reaction diagram
Q86D28
-
-
-
?
DL-homocysteine + H2O
hydrogen sulfide + NH3 + 2-oxobutanoate
show the reaction diagram
Q84AR1
-
-
-
?
DL-homocysteine + H2O
hydrogen sulfide + NH3 + 2-oxobutanoate
show the reaction diagram
-
highest substrate specificity for DL-homocysteine
-
-
?
DL-homocysteine + H2O
hydrogen sulfide + NH3 + 2-oxobutanoate
show the reaction diagram
Citrobacter freundii ATCC29063
Q84AR1
-
-
-
?
DL-homocysteine + H2O
H2S + S-(beta-hydroxyethyl)-L-homocysteine
show the reaction diagram
-
gamma-replacement reaction, wild-type enzyme
-
-
?
DL-homoserine + H2O
NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
ethionine
?
show the reaction diagram
-
-
-
?
ethionine
?
show the reaction diagram
-
-
-
-
?
ethionine
?
show the reaction diagram
-
-
-
?
ethionine
?
show the reaction diagram
-
-
-
?
ethionine
?
show the reaction diagram
-
-
-
-
?
ethionine
?
show the reaction diagram
-
-
-
-
ethionine
?
show the reaction diagram
-
-
-
?
ethionine
?
show the reaction diagram
-
-
-
?
gamma-(L-1-amino-3-methylthiopropylphosphinic acid)
?
show the reaction diagram
Q84AR1
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
-
-
?
homocysteine + alkanethiol
S-alkylhomocysteine
show the reaction diagram
-
-
corresponding
?
L-cystathionine + ?
?
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
?
show the reaction diagram
-
-
-
-
?
L-cystathionine + H2O
?
show the reaction diagram
-, Q5MQ31
assay at pH 8.0, 37C
-
-
?
L-cystathionine + H2O
?
show the reaction diagram
Lactococcus lactis IL1403
-
-
-
-
?
L-cysteine
?
show the reaction diagram
-
-
-
?
L-cysteine
?
show the reaction diagram
-
-
-
?
L-cysteine
?
show the reaction diagram
-
-
-
?
L-cysteine
2-oxopropanoate + NH3 + H2S
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
?
show the reaction diagram
-
-
-
-
-
L-cysteine + H2O
?
show the reaction diagram
-, Q5MQ31
assay at pH 8.0, 37C
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
Q86D28
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
Q84AR1
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
Q8RDT4
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
Q7MX71
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
Q73KL7
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-, Q86D27, Q86D28
160% of EhMGL1 activity with L-methionine
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-, Q86D27, Q86D28
20% of activity with L-methionine
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
Fusobacterium nucleatum subsp. nucleatum, ATCC 25586
Q8RDT4
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
Q7MX71
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
Citrobacter freundii ATCC29063
Q84AR1
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
Q73KL7
-
-
-
?
L-cysteine + H2O
H2S + S-(beta-hydroxyethyl)-L-cysteine
show the reaction diagram
-
beta-replacement reaction, wild-type enzyme and mutant C116H
-
-
?
L-cystine + H2O
?
show the reaction diagram
-, Q5MQ31
assay at pH 8.0, 37C
-
-
?
L-ethionine + H2O
ethanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-ethionine + H2O
ethanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-ethionine + H2O
ethanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-ethionine + H2O
ethanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
Q84AR1
-
-
-
?
L-ethionine + H2O
ethanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
60% of activity with L-methinine
-
?
L-ethionine + H2O
ethanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
Citrobacter freundii ATCC29063
Q84AR1
-
-
-
?
L-ethionine + H2O
?
show the reaction diagram
-
-
-
-
?
L-ethionine + H2O
?
show the reaction diagram
-
-
-
-
-
L-Gly(vinyl) + H2O
?
show the reaction diagram
-
-
-
-
?
L-homocysteine
2-oxobutanoate + NH3 + hydrogen sulfide
show the reaction diagram
-
-
-, 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
show the reaction diagram
Pseudomonas putida ICR 3460
-
-
-, 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
?
show the reaction diagram
-
-
-
-
?
L-homocysteine + H2O
hydrogen sulfide + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-homocysteine + H2O
hydrogen sulfide + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-homoserine
NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-homoserine + H2O
?
show the reaction diagram
Pseudomonas putida, Aspergillus sp., Aspergillus sp. Rs-1a
-
-
-
-
?
L-methionine
?
show the reaction diagram
-
bacterial metabolism of methionine
-
-
-
L-methionine
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-methionine
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-methionine
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
Pseudomonas putida S-313
-
-
-
-
?
L-methionine + 2-butylthiol
S-2-butylhomocysteine
show the reaction diagram
-
-
-
?
L-methionine + 2-mercaptoethanol
methanethiol + S-(beta-hydroxyethyl)-L-homocysteine
show the reaction diagram
-
gamma-replacement reaction, wild-type enzyme
-
-
?
L-methionine + 2-propylthiol
S-2-propylhomocysteine
show the reaction diagram
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
ir
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
ir
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-, Q86D27, Q86D28
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
Q86D28
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-, Q86D28
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-, Q5MQ31
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
Q84AR1
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
Q8RDT4
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
Q7MX71
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
Q73KL7
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
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
show the reaction diagram
-, Q86D27, Q86D28
181% of EhMGL1 activity with L-methionine
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
gamma-elimination reaction
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
gamma-elimination reaction
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
gamma-elimination reaction, 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
show the reaction diagram
Lactococcus lactis IL1403
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
Fusobacterium nucleatum subsp. nucleatum, ATCC 25586
Q8RDT4
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
Treponema denticola ATCC35405, Porphyromonas gingivalis W83
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
Q7MX71
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
Fusobacterium nucleatum JCM8532
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
Citrobacter freundii ATCC29063
Q84AR1
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
Q73KL7
-
-
-
?
L-methionine + H2O
?
show the reaction diagram
-, Q5MQ31
assay at pH 8.0, 37C
-
-
?
L-methionine + H2O
?
show the reaction diagram
Aspergillus sp. Rs-1a
-
-
-
-
?
L-methionine sulfone
?
show the reaction diagram
-
-
-
?
L-methionine sulfone
?
show the reaction diagram
-
-
-
-
?
L-methionine sulfoxide
?
show the reaction diagram
-
-
-
-
?
L-methionine sulfoxide + H2O
?
show the reaction diagram
-
gamma-elimination reaction
-
-
?
L-selenodjenkolate
pyruvate + NH3 + H2Se + formaldehyde
show the reaction diagram
-
-
-
?
L-selenomethionine + H2O
?
show the reaction diagram
-
-
-
-
?
L-vinylglycine
?
show the reaction diagram
-
-
-
?
O-acetyl-DL-homoserine + H2O
NH3 + 2-oxobutanoate + acetate
show the reaction diagram
-
-
-
-
?
O-acetyl-L-homoserine
?
show the reaction diagram
-
-
-
?
O-acetyl-L-homoserine + H2O
?
show the reaction diagram
-
-
-
-
?
O-acetyl-L-serine + H2O
2-oxopropanoate + NH3 + acetate
show the reaction diagram
Q86D28
-
-
-
?
O-acetyl-L-serine + H2O
2-oxopropanoate + NH3 + acetate
show the reaction diagram
-
weak activity
-
-
?
O-acetyl-L-serine + H2O
2-oxopropanoate + NH3 + acetate
show the reaction diagram
-, Q86D27, Q86D28
11% of activity with L-methionine
-
?
O-acetyl-L-serine + H2O
2-oxopropanoate + NH3 + acetate
show the reaction diagram
-, Q86D27, Q86D28
34% of EhMGL1 activity with L-methionine
-
?
O-succinyl-L-homoserine + H2O
?
show the reaction diagram
-
weak activity
-
-
?
S-benzyl-L-cysteine + H2O
thiobenzyl alcohol + NH3 + 2-oxopropanoate
show the reaction diagram
-
-
-
-
?
S-benzyl-L-cysteine + H2O
thiobenzyl alcohol + NH3 + 2-oxopropanoate
show the reaction diagram
Citrobacter freundii, Citrobacter freundii ATCC29063
Q84AR1
-
-
-
?
S-benzyl-L-cysteine + H2O
?
show the reaction diagram
-
beta-elimination reaction
-
-
?
S-ethyl-L-cysteine
?
show the reaction diagram
-
-
-
?
S-ethyl-L-cysteine + H2O
?
show the reaction diagram
-
beta-elimination reaction
-
-
?
S-ethyl-L-cysteine + H2O
ethanethiol + NH3 + 2-oxopropanoate
show the reaction diagram
-
-
-
-
?
S-ethyl-L-cysteine + H2O
ethanethiol + NH3 + 2-oxopropanoate
show the reaction diagram
Q84AR1
-
-
-
?
S-ethyl-L-cysteine + H2O
ethanethiol + NH3 + 2-oxopropanoate
show the reaction diagram
-
weak activity
-
-
?
S-ethyl-L-homocysteine + H2O
ethanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
S-ethyl-L-homocysteine + H2O
?
show the reaction diagram
-
gamma-elimination reaction
-
-
?
S-methyl-L-cysteine
?
show the reaction diagram
-
-
-
?
S-methyl-L-cysteine + 2-mercaptoethanol
?
show the reaction diagram
-
-
-
-
?
S-methyl-L-cysteine + H2O
pyruvate + NH3 + CH3SH
show the reaction diagram
-
-
-
-
?
S-methyl-L-cysteine + H2O
pyruvate + NH3 + CH3SH
show the reaction diagram
-
-
-
ir
S-methyl-L-cysteine + H2O
pyruvate + NH3 + CH3SH
show the reaction diagram
-
-
-
-
?
S-methyl-L-cysteine + H2O
?
show the reaction diagram
-
-
-
-
?
S-methyl-L-cysteine + H2O
methanethiol + NH3 + 2-oxopropanoate
show the reaction diagram
-
-
-
-
?
S-methyl-L-cysteine + H2O
methanethiol + NH3 + 2-oxopropanoate
show the reaction diagram
Q84AR1
-
-
-
?
S-methyl-L-cysteine + H2O
methanethiol + NH3 + 2-oxopropanoate
show the reaction diagram
-
weak activity
-
-
?
S-methylcysteine + H2O
?
show the reaction diagram
-
-
-
-
?
Se-methylselenocysteine
?
show the reaction diagram
-
-
-
-
-
Se-methylselenocysteine
?
show the reaction diagram
-
-
-
?
selenoethionine + H2O
ethylselenol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
selenomethionine + H2O
methylselenol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
selenomethionine + H2O
methylselenol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
trifluoromethionine + H2O
trifluoromethanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
Q86D28
-
-
-
?
trifluoromethionine + H2O
?
show the reaction diagram
-
-
-
-
?
L-methionine
?
show the reaction diagram
-
bacterial metabolism of methionine
-
-
-
L-methionine
?
show the reaction diagram
additional information
-
bacterial metabolism of methionine
-
-
-
L-vinylglycine
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
-
-
-
additional information
?
-
-
-
-
-
additional information
?
-
-
-
-
-
additional information
?
-
-
-
-
-
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 substrate: L-cysteine
-
-
-
additional information
?
-
Q86D28
under normal conditions, isoform ehMGL1 is involved in degradation of L-methionine, under normal conditions, isoform ehMGL2 is not involved degradation of L-methionine
-
-
-
additional information
?
-
-
no activity with O-phospho-L-serine
-
-
-
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
?
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-homocysteine
2-oxobutanoate + NH3 + hydrogen sulfide
show the reaction diagram
Pseudomonas putida, Pseudomonas putida ICR 3460
-
-
-
-
?
L-methionine
?
show the reaction diagram
-
bacterial metabolism of methionine
-
-
-
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-, Q86D27, Q86D28
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-, Q5MQ31
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
Q84AR1
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
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
show the reaction diagram
-
gamma-elimination reaction
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
gamma-elimination reaction
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
gamma-elimination reaction
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
Citrobacter freundii ATCC29063
Q84AR1
-
-
-
?
L-methionine
?
show the reaction diagram
-
bacterial metabolism of methionine
-
-
-
L-methionine
?
show the reaction diagram
additional information
-
bacterial metabolism of methionine
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
4 mol per mol of enzyme
pyridoxal 5'-phosphate
-
4 mol per mol of enzyme
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
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
Achromobacter starkeyi
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
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
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
4 mol of pyridoxal 5'-phosphate per mole of enzyme
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Cd2+
-
significant enzyme inhibition
Cd2+
-
inhibitor
Co2+
-
slightly stimulatory effect on the enzyme activity
Co2+
-
increased enzyme activity after preincubation of the enzyme for 2 h
Cu2+
-
slightly stimulatory effect on the enzyme activity
Cu2+
-
increased enzyme activity after preincubation of the enzyme for 2 h
Li+
-
significant enzyme inhibition
Li+
-
inhibitor
Mg2+
-
slightly stimulatory effect on the enzyme activity
Mg2+
-
increased enzyme activity after preincubation of the enzyme for 2 h
Mn2+
-
slightly stimulatory effect on the enzyme activity
Mn2+
-
increased enzyme activity after preincubation of the enzyme for 2 h
Na+
-
significant enzyme inhibition
Ni2+
-
slightly stimulatory effect on the enzyme activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
-
3-Methyl-2-benzothiazolinone hydrazone
-
-
3-methyl-2-benzothiazonlinone hydrazone
-
1 mM, 23.6% residual activity
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5-5'-dithiobis-(2-nitrobenzoic acid)
-
-
Carbonyl reagents
-
-
-
Carbonyl reagents
-
-
-
DL-propargylglycine
-
-
DL-propargylglycine
Q86D27, Q86D28
; irreversible slow-binding inhibition
DL-propargylglycine
-
-
DL-propargylglycine
-
-
DL-propargylglycine
-
inhibition profiles of wild-type and mutant enzymes, overview
glycine
-
microspectrophotometric measurements
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
hydroxylamine
-
-
hydroxylamine
-
1 mM, 1.42% residual activity
iodoacetate
-
slightly
iodoacetate
Achromobacter starkeyi
-
-
iodoacetic acid
-
1 mM, 24.1% residual activity
L-2-amino-4-chloro-4-pentenoate
-
complete inhibition at 5 mol per mol of tetramer enzyme
L-2-aminobutanoate
-
-
L-Cycloserine
-
microspectrophotometric measurements
L-norleucine
-
-
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
myrsinoic acid B
-
-
myrsinoic acid B
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
NaCl
-
0.4% wt/vol, 78% residual activity
p-chloromercuri-benzoic acid
Achromobacter starkeyi, Trichomonas vaginalis
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoic acid
-
-
propargylglycine
-
-
Semicarbazide
-
-
Semicarbazide
Achromobacter starkeyi
-
-
Sodium arsenate
Achromobacter starkeyi
-
-
Sulfhydryl inhibitors
-
-
-
Sulfhydryl inhibitors
-
-
-
L-Vinylglycine
-
microspectrophotometric measurements
additional information
-
chemical modification by cyanylation
-
additional information
-
recombinant METase alone inhibits the proliferation of 15/15 NB cell lines in vitro in a dose-dependent manner
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
EDTA
-
1 mM, 115% of initial activity
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.25
-
1-amino-3-(methylthio)propylphosphinic acid
-
30C
18.2
-
2-amino-3-(N,N-dimethylamino)propionic acid
-
-
0.17
-
beta-(S-ethyl-L-cysteine)
-
pH and temperature not specified in the publication
-
3.6
-
cysteine
-
recombinant, MGL2 C116G
8.5
-
cysteine
-
recombinant MGL1
9.7
-
cysteine
-
recombinant MGL1, C113G
22.3
-
cysteine
-
recombinant MGL2
12.3
-
DL-2-amino-3(N-hydroxyethyl)propionic acid
-
-
2.3
-
DL-amino-3-(N-methylamino)propionic acid
-
-
0.2
-
DL-homocysteine
-
pH 8.0, 37C, recombinant mutant Y114F/C116H
0.24
-
DL-homocysteine
-
mutant enzyme C116S, at 37C
0.5
-
DL-homocysteine
-
-
0.6
-
DL-homocysteine
-
pH 8.0, 37C, recombinant mutant K240R
0.8
-
DL-homocysteine
-
pH 8.0, 37C, recombinant mutant K240N
0.97
-
DL-homocysteine
Q84AR1
recombinant enzyme
0.97
-
DL-homocysteine
-
pH 8.0, 30C
1
-
DL-homocysteine
-
30C, pH 8.0
1.1
-
DL-homocysteine
Q84AR1
wild-type
1.1
-
DL-homocysteine
-
-
1.1
-
DL-homocysteine
-
pH 8.0, 37C, recombinant wild-type enzyme
1.4
-
DL-homocysteine
-
pH 8.0, 37C, recombinant mutant C166H; pH 8.0, 37C, recombinant mutant K240M
1.47
-
DL-homocysteine
Q86D28
wild-type ehMGL2, pH 7.0, 37C
1.61
-
DL-homocysteine
-
mutant enzyme C116A, at 37C
1.8
-
DL-homocysteine
-
mutant enzyme C116H, at 37C
1.8
-
DL-homocysteine
-
-
1.82
-
DL-homocysteine
-
wild type enzyme, at 37C
1.87
-
DL-homocysteine
Q86D27, Q86D28
36C, pH 6.8, recombinant EhMGL2
3.03
-
DL-homocysteine
Q86D28
wild-type ehMGL1, pH 7.0, 37C
3.03
-
DL-homocysteine
-
-
3.4
-
DL-homocysteine
Q86D27, Q86D28
36C, pH 6.8, recombinant EhMGL1
6
-
DL-homocysteine
-
pH 8.0, 37C, recombinant mutant K240I
56.5
-
DL-homoserine
-
30C, pH 8.0
56.5
-
DL-homoserine
-
pH 8.0, 30C
1.2
-
gamma-(L-1-amino-3-methylthiopropylphosphinic acid)
-
pH and temperature not specified in the publication
-
0.27
-
L-cystathionine
-
-
0.12
-
L-cysteine
-
mutant enzyme C116S, at 37C
0.16
-
L-cysteine
Q84AR1
recombinant enzyme
0.16
-
L-cysteine
-
30C, pH 8.0
0.18
-
L-cysteine
Q84AR1
wild-type
0.18
-
L-cysteine
-
-
0.18
-
L-cysteine
Q73KL7
pH 7.6, 37C
0.2
-
L-cysteine
-
pH 8.0, 37C, recombinant mutant Y114F/C116H; pH 8.0, 37C, recombinant wild-type enzyme
0.3
-
L-cysteine
-
pH 8.0, 37C, recombinant mutant C166H; pH 8.0, 37C, recombinant mutants K240R and K240M
0.32
-
L-cysteine
Q8RDT4
pH 7.6, 37C
0.34
-
L-cysteine
Q86D28
mutant C110G, pH 7.0, 37C
0.39
-
L-cysteine
-
mutant enzyme C116A, at 37C
0.46
-
L-cysteine
Q86D28
mutant C110S, pH 7.0, 37C
0.46
-
L-cysteine
-
-
0.53
-
L-cysteine
-
wild type enzyme, at 37C
0.53
-
L-cysteine
-
-
0.63
-
L-cysteine
-
mutant enzyme C116H, at 37C
0.63
-
L-cysteine
Q7MX71
pH 7.6, 37C
0.64
-
L-cysteine
Q86D28
wild-type ehMGL1, pH 7.0, 37C
0.64
-
L-cysteine
-
-
1
-
L-cysteine
-
pH 8.0, 37C, recombinant mutants K240I and K240N
1.01
-
L-cysteine
Q86D28
mutant Y108F, pH 7.0, 37C
1.7
-
L-cysteine
Q86D28
wild-type ehMGL2, pH 7.0, 37C
3.6
-
L-cysteine
-
-
0.2
-
L-ethionine
-
37C, pH 8.0
0.2
-
L-ethionine
-
-
0.27
-
L-ethionine
-
37C, pH 8.0
0.31
-
L-ethionine
-
-
0.43
-
L-ethionine
-
-
0.45
-
L-ethionine
-
-
0.54
-
L-ethionine
Q84AR1
recombinant enzyme
0.56
-
L-ethionine
Q84AR1
wild-type
0.56
-
L-ethionine
-
-
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
6.7
-
L-Gly(vinyl)
-
30C, pH 8.0
6.43
-
L-homocysteine
-
-
30
-
L-homoserine
-
37C, pH 8.0
0.0013
-
L-methionine
-
-
0.04
-
L-methionine
-
pH 8.0, 37C, recombinant mutant K240R
0.11
-
L-methionine
-
mutant enzyme C116S, at 37C
0.19
-
L-methionine
Q86D28
mutant C110G, pH 7.0, 37C
0.432
-
L-methionine
-
pH 8.0, 30C, recombinant enzyme
0.5
-
L-methionine
-
pH 8.0, 37C, recombinant wild-type enzyme
0.55
-
L-methionine
-
-
0.61
-
L-methionine
Q86D28
wild-type ehMGL1, pH 7.0, 37C
0.61
-
L-methionine
-
-
0.7
-
L-methionine
Q84AR1
recombinant enzyme; wild-type
0.7
-
L-methionine
-
30C, pH 8.0
0.7
-
L-methionine
-
-
0.7
-
L-methionine
-
pH 8.0, 30C
0.72
-
L-methionine
Q86D28
mutant C110S, pH 7.0, 37C
0.87
-
L-methionine
-
-
0.9
-
L-methionine
-
37C, pH 8.0
0.92
-
L-methionine
-
wild type enzyme, at 37C
0.94
-
L-methionine
Q86D27, Q86D28
36C, pH 6.8, recombinant EhMGL1
0.947
-
L-methionine
-
pH 8.0, 30C, recombinant enzyme
0.99
-
L-methionine
-
-
1
-
L-methionine
-
-
1.13
-
L-methionine
-
30C
1.13
-
L-methionine
-
-
1.33
-
L-methionine
-
-
1.42
-
L-methionine
-
mutant enzyme C116H, at 37C
1.58
-
L-methionine
-
-
1.7
-
L-methionine
-
37C, pH 8.0
1.77
-
L-methionine
-
pH 8.0, 30C, recombinant enzyme
1.9
-
L-methionine
Q86D27, Q86D28
36C, pH 6.8, recombinant EhMGL2
2.3
-
L-methionine
-
pH 8.0, 37C, recombinant mutant C166H
2.85
-
L-methionine
-
mutant enzyme C116A, at 37C
3.58
-
L-methionine
Q86D28
wild-type ehMGL2, pH 7.0, 37C
4.8
-
L-methionine
-
pH 8.0, 37C, recombinant mutant K240I
5.7
-
L-methionine
-
pH 8.0, 37C, recombinant mutant K240M
6.12
-
L-methionine
-
-
9.8
-
L-methionine
-
pH 8.0, 37C, recombinant mutant K240N
10.6
-
L-methionine
-
pH 7.2, 30C
11.6
-
L-methionine
-
-
15.12
-
L-methionine
Q86D28
mutant C113S, pH 7.0, 37C
90
-
L-methionine
-
-
4
-
L-Methionine sulfone
-
pH 8.0, 30C
8.22
-
L-Methionine sulfone
-
37C, pH 8.0
6.2
-
L-methionine sulfoxide
-
pH 8.0, 30C
7.07
-
L-methionine sulfoxide
-
pH 8.0, 30C, recombinant enzyme
12.22
-
L-methionine sulfoxide
-
pH 8.0, 30C, recombinant enzyme
33.51
-
L-methionine sulfoxide
-
pH 8.0, 30C, recombinant enzyme
2.3
-
L-selenodjenkolate
-
-
6.7
-
L-Vinylglycine
-
pH 8.0, 30C
5.82
-
O-acetyl-DL-homoserine
-
pH 8.0, 30C
2.22
-
O-acetyl-L-homoserine
-
37C, pH 8.0
6.28
-
O-acetyl-L-serine
Q86D28
wild-type ehMGL1, pH 7.0, 37C
52.33
-
O-acetyl-L-serine
Q86D28
wild-type ehMGL2, pH 7.0, 37C
2.8
-
O-methyl-L-serine
-
-
0.18
-
S-Benzyl-L-cysteine
Q84AR1
recombinant enzyme
0.18
-
S-Benzyl-L-cysteine
-
30C, pH 8.0
0.19
-
S-Benzyl-L-cysteine
Q84AR1
wild-type
0.348
-
S-Benzyl-L-cysteine
-
pH 8.0, 30C, recombinant enzyme
0.766
-
S-Benzyl-L-cysteine
-
pH 8.0, 30C, recombinant enzyme
1.47
-
S-Benzyl-L-cysteine
-
pH 8.0, 30C, recombinant enzyme
0.17
-
S-ethyl-L-cysteine
-
30C, pH 8.0
0.358
-
S-ethyl-L-cysteine
-
pH 8.0, 30C, recombinant enzyme
0.48
-
S-ethyl-L-cysteine
-
37C, pH 8.0
0.49
-
S-ethyl-L-cysteine
Q84AR1
wild-type
0.72
-
S-ethyl-L-cysteine
-
pH 8.0, 30C, recombinant enzyme
2.17
-
S-ethyl-L-cysteine
-
pH 8.0, 30C, recombinant enzyme
0.278
-
S-ethyl-L-homocysteine
-
pH 8.0, 30C, recombinant enzyme
0.5
-
S-ethyl-L-homocysteine
-
30C, pH 8.0
0.545
-
S-ethyl-L-homocysteine
-
pH 8.0, 30C, recombinant enzyme
0.93
-
S-ethyl-L-homocysteine
-
pH 8.0, 30C, recombinant enzyme
0.17
-
S-etyhl-L-cysteine
Q84AR1
recombinant enzyme
0.4
-
S-methyl-L-cysteine
-
37C, pH 8.0
0.4
-
S-methyl-L-cysteine
-
pH 8.0, 37C, recombinant mutant Y114F/C116H
0.61
-
S-methyl-L-cysteine
Q84AR1
wild-type
0.61
-
S-methyl-L-cysteine
-
-
0.69
-
S-methyl-L-cysteine
-
-
0.7
-
S-methyl-L-cysteine
-
pH 8.0, 37C, recombinant wild-type enzyme
0.71
-
S-methyl-L-cysteine
Q84AR1
recombinant enzyme
0.71
-
S-methyl-L-cysteine
-
30C, pH 8.0
0.77
-
S-methyl-L-cysteine
-
-
1.4
-
S-methyl-L-cysteine
-
-
2.1
-
S-methyl-L-cysteine
-
pH 8.0, 37C, recombinant mutant C166H
0.77
-
S-methylcysteine
-
-
0.13
-
Se-methyl-L-selenocysteine
-
-
0.1
-
trifluoromethionine
Q86D28
wild-type ehMGL1, pH 7.0, 37C
0.1
-
trifluoromethionine
-
-
0.29
-
trifluoromethionine
Q86D28
mutant Y111F, pH 7.0, 37C
0.57
-
trifluoromethionine
Q86D28
mutant Y108F, pH 7.0, 37C
0.83
-
trifluoromethionine
Q86D28
mutant R55A, pH 7.0, 37C
0.92
-
trifluoromethionine
Q86D28
wild-type ehMGL2, pH 7.0, 37C
1.62
-
trifluoromethionine
Q86D28
mutant R58A, pH 7.0, 37C
5.45
-
trifluoromethionine
Q86D28
mutant C113S, pH 7.0, 37C
30
-
L-homoserine
-
-
additional information
-
L-methionine
-
values between 0.8 to 1.7, depending on publications
7.22
-
L-Vinylglycine
-
37C, pH 8.0
additional information
-
additional information
-
values for native and cyanylated enzyme
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
steady-state kinetics for beta- and gamma-elimination reactions, overview
-
additional information
-
additional information
-
steady-state kinetics
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.057
0.65
DL-homocysteine
Q86D28
wild-type ehMGL2, pH 7.0, 37C
1.36
-
DL-homocysteine
-
pH 8.0, 37C, recombinant mutant Y114F/C116H
1.74
-
DL-homocysteine
-
mutant enzyme C116A, at 37C
2.59
-
DL-homocysteine
-
mutant enzyme C116S, at 37C
3.13
-
DL-homocysteine
Q86D28
wild-type ehMGL1, pH 7.0, 37C
3.91
-
DL-homocysteine
Q86D28
wild-type ehMGL1, pH 7.0, 37C
3.92
-
DL-homocysteine
-
-
5.03
-
DL-homocysteine
-
pH 8.0, 37C, recombinant mutant K240N
5.1
-
DL-homocysteine
Q84AR1
wild-type
5.1
-
DL-homocysteine
-
-
8.5
-
DL-homocysteine
-
30C, pH 8.0
8.5
-
DL-homocysteine
-
pH 8.0, 30C
8.51
-
DL-homocysteine
Q84AR1
recombinant enzyme
10.56
-
DL-homocysteine
Q86D28
wild-type ehMGL2, pH 7.0, 37C
22.7
-
DL-homocysteine
-
pH 8.0, 37C, recombinant mutant K240R
28.8
-
DL-homocysteine
-
pH 8.0, 37C, recombinant mutant K240M
30
-
DL-homocysteine
-
mutant enzyme C116H, at 37C
44.8
-
DL-homocysteine
-
-
44.84
-
DL-homocysteine
-
wild type enzyme, at 37C
48.4
-
DL-homocysteine
-
pH 8.0, 37C, recombinant mutant C166H
62.2
-
DL-homocysteine
-
pH 8.0, 37C, recombinant mutant K240I
71
-
DL-homocysteine
-
pH 8.0, 37C, recombinant wild-type enzyme
0.5
-
DL-homoserine
-
30C, pH 8.0
0.52
-
DL-homoserine
-
pH 8.0, 30C
0.43
-
L-cysteine
-
mutant enzyme C116A, at 37C
0.57
-
L-cysteine
-
mutant enzyme C116S, at 37C
0.67
-
L-cysteine
Q86D28
mutant Y108F, pH 7.0, 37C
0.69
-
L-cysteine
Q8RDT4
pH 7.6, 37C
0.78
-
L-cysteine
Q86D28
mutant C110S, pH 7.0, 37C
0.79
-
L-cysteine
Q73KL7
pH 7.6, 37C
0.8
-
L-cysteine
Q86D28
wild-type ehMGL2, pH 7.0, 37C
0.89
-
L-cysteine
-
pH 8.0, 37C, recombinant mutant Y114F/C116H
1.01
-
L-cysteine
Q86D28
mutant C110G, pH 7.0, 37C
1.06
-
L-cysteine
-
pH 8.0, 37C, recombinant mutant K240N
1.45
-
L-cysteine
-
pH 8.0, 37C, recombinant mutant K240R
1.59
-
L-cysteine
Q86D28
wild-type ehMGL1, pH 7.0, 37C
1.59
-
L-cysteine
-
-
1.66
-
L-cysteine
-
pH 8.0, 37C, recombinant mutant K240M
1.86
-
L-cysteine
Q7MX71
pH 7.6, 37C
2.13
-
L-cysteine
-
pH 8.0, 37C, recombinant wild-type enzyme
2.23
-
L-cysteine
-
pH 8.0, 37C, recombinant mutant K240I
2.24
-
L-cysteine
Q84AR1
wild-type
2.27
-
L-cysteine
-
wild type enzyme, at 37C
2.27
-
L-cysteine
-
-
2.3
-
L-cysteine
-
30C, pH 8.0
2.3
-
L-cysteine
-
-
2.33
-
L-cysteine
Q84AR1
recombinant enzyme
23.3
-
L-cysteine
-
pH 8.0, 37C, recombinant mutant C166H
43.8
-
L-cysteine
-
mutant enzyme C116H, at 37C
0.017
-
L-ethionine
-
37C, pH 8.0
6.2
-
L-ethionine
Q84AR1
wild-type
6.2
-
L-ethionine
-
-
6.78
-
L-ethionine
Q84AR1
recombinant enzyme
33.4
-
L-ethionine
-
37C, pH 8.0
33.4
-
L-ethionine
-
-
1.9
-
L-Gly(vinyl)
-
30C, pH 8.0
0.03
-
L-methionine
-
pH 8.0, 37C, recombinant mutant C166H
0.07
-
L-methionine
-
mutant enzyme C116H, at 37C
0.17
-
L-methionine
-
37C, pH 8.0
0.36
-
L-methionine
Q86D28
mutant C110G, pH 7.0, 37C
0.47
-
L-methionine
Q86D28
mutant C113S, pH 7.0, 37C
0.93
-
L-methionine
Q86D28
mutant C110S, pH 7.0, 37C
1.11
-
L-methionine
Q86D28
wild-type ehMGL2, pH 7.0, 37C
1.46
-
L-methionine
-
mutant enzyme C116A, at 37C
1.77
-
L-methionine
-
mutant enzyme C116S, at 37C
1.82
-
L-methionine
Q86D28
wild-type ehMGL1, pH 7.0, 37C
1.82
-
L-methionine
-
-
3.9
-
L-methionine
-
pH 8.0, 30C, recombinant enzyme
6.2
-
L-methionine
Q84AR1
recombinant enzyme
6.2
-
L-methionine
-
30C, pH 8.0
6.2
-
L-methionine
-
pH 8.0, 30C
6.5
-
L-methionine
Q84AR1
wild-type
6.5
-
L-methionine
-
-
9.86
-
L-methionine
-
pH 8.0, 30C, recombinant enzyme
12
-
L-methionine
-
pH 8.0, 30C, recombinant enzyme
25.39
-
L-methionine
-
wild type enzyme, at 37C
33.4
-
L-methionine
-
pH 8.0, 37C, recombinant wild-type enzyme
48.6
-
L-methionine
-
37C, pH 8.0
2.1
-
L-Methionine sulfone
-
pH 8.0, 30C
40.4
-
L-Methionine sulfone
-
37C, pH 8.0
2.5
-
L-methionine sulfoxide
-
pH 8.0, 30C
2.7
-
L-methionine sulfoxide
-
pH 8.0, 30C, recombinant enzyme
5.05
-
L-methionine sulfoxide
-
pH 8.0, 30C, recombinant enzyme
6.7
-
L-methionine sulfoxide
-
pH 8.0, 30C, recombinant enzyme
1.9
-
L-Vinylglycine
-
pH 8.0, 30C
44.4
-
L-Vinylglycine
-
37C, pH 8.0
2.1
-
O-acetyl-DL-homoserine
-
pH 8.0, 30C
78
-
O-acetyl-L-homoserine
-
37C, pH 8.0
1.74
-
O-acetyl-L-serine
Q86D28
wild-type ehMGL1, pH 7.0, 37C
6.22
-
O-acetyl-L-serine
Q86D28
wild-type ehMGL2, pH 7.0, 37C
5.8
-
S-Benzyl-L-cysteine
-
pH 8.0, 30C, recombinant enzyme
8.16
-
S-Benzyl-L-cysteine
Q84AR1
recombinant enzyme
8.2
-
S-Benzyl-L-cysteine
-
30C, pH 8.0
8.5
-
S-Benzyl-L-cysteine
-
pH 8.0, 30C, recombinant enzyme
10
-
S-Benzyl-L-cysteine
-
pH 8.0, 30C, recombinant enzyme
5
-
S-ethyl-L-cysteine
-
30C, pH 8.0
5.03
-
S-ethyl-L-cysteine
Q84AR1
recombinant enzyme
5.79
-
S-ethyl-L-cysteine
-
37C, pH 8.0
6.3
-
S-ethyl-L-cysteine
-
pH 8.0, 30C, recombinant enzyme
6.8
-
S-ethyl-L-cysteine
Q84AR1
wild-type
7.08
-
S-ethyl-L-cysteine
-
pH 8.0, 30C, recombinant enzyme
8.05
-
S-ethyl-L-cysteine
-
pH 8.0, 30C, recombinant enzyme
3.84
-
S-ethyl-L-homocysteine
-
pH 8.0, 30C, recombinant enzyme
5.89
-
S-ethyl-L-homocysteine
-
pH 8.0, 30C, recombinant enzyme
6.8
-
S-ethyl-L-homocysteine
-
30C, pH 8.0
0.12
-
S-methyl-L-cysteine
-
pH 8.0, 37C, recombinant mutant Y114F/C116H
1.58
-
S-methyl-L-cysteine
-
pH 8.0, 37C, recombinant wild-type enzyme
4.6
-
S-methyl-L-cysteine
Q84AR1
recombinant enzyme
4.6
-
S-methyl-L-cysteine
-
30C, pH 8.0
5.53
-
S-methyl-L-cysteine
-
37C, pH 8.0
5.9
-
S-methyl-L-cysteine
-
-
5.97
-
S-methyl-L-cysteine
Q84AR1
wild-type
46.3
-
S-methyl-L-cysteine
-
pH 8.0, 37C, recombinant mutant C166H
0.24
-
trifluoromethionine
Q86D28
mutant C113S, pH 7.0, 37C
0.81
-
trifluoromethionine
Q86D28
wild-type ehMGL1, pH 7.0, 37C
0.81
-
trifluoromethionine
-
-
0.97
-
trifluoromethionine
Q86D28
wild-type ehMGL2, pH 7.0, 37C
1.19
-
trifluoromethionine
Q86D28
mutant R58A, pH 7.0, 37C
1.26
-
trifluoromethionine
Q86D28
mutant R55A, pH 7.0, 37C
2.22
-
trifluoromethionine
Q86D28
mutant Y108F, pH 7.0, 37C
5.8
-
trifluoromethionine
Q86D28
mutant Y111F, pH 7.0, 37C
17.46
-
trifluoromethionine
Q86D28
wild-type ehMGL2, pH 7.0, 37C
1.4
-
L-homoserine
-
-
additional information
-
L-methionine
-
values between 25.3 to 48.6, depending on publications
10.9
-
S-Benzyl-L-cysteine
Q84AR1
wild-type
additional information
-
S-ethyl-L-cysteine
-
37C, pH 8.0
7.05
-
S-ethyl-L-homocysteine
-
pH 8.0, 30C, recombinant enzyme
additional information
-
S-methyl-L-cysteine
-
37C, pH 8.0
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
6.29
-
DL-homocysteine
-
pH 8.0, 37C, recombinant mutant K240N
859
6.8
-
DL-homocysteine
-
pH 8.0, 37C, recombinant mutant Y114F/C116H
859
8.8
-
DL-homocysteine
-
pH 8.0, 30C
859
10.4
-
DL-homocysteine
-
pH 8.0, 37C, recombinant mutant K240I
859
20.6
-
DL-homocysteine
-
pH 8.0, 37C, recombinant mutant K240M
859
34.6
-
DL-homocysteine
-
pH 8.0, 37C, recombinant mutant C166H
859
37.8
-
DL-homocysteine
-
pH 8.0, 37C, recombinant mutant K240R
859
64.5
-
DL-homocysteine
-
pH 8.0, 37C, recombinant wild-type enzyme
859
0.01
-
DL-homoserine
-
pH 8.0, 30C
6515
1.06
-
L-cysteine
-
pH 8.0, 37C, recombinant mutant K240N
74
2.15
-
L-cysteine
Q8RDT4
pH 7.6, 37C
74
2.23
-
L-cysteine
-
pH 8.0, 37C, recombinant mutant K240I
74
2.96
-
L-cysteine
Q7MX71
pH 7.6, 37C
74
4.45
-
L-cysteine
-
pH 8.0, 37C, recombinant mutant Y114F/C116H
74
4.46
-
L-cysteine
Q73KL7
pH 7.6, 37C
74
4.83
-
L-cysteine
-
pH 8.0, 37C, recombinant mutant K240R
74
5.53
-
L-cysteine
-
pH 8.0, 37C, recombinant mutant K240M
74
10.7
-
L-cysteine
-
pH 8.0, 37C, recombinant wild-type enzyme
74
77.7
-
L-cysteine
-
pH 8.0, 37C, recombinant mutant C166H
74
0.01
-
L-methionine
-
pH 8.0, 37C, recombinant mutant C166H
88
1.8
-
L-methionine
-
pH 8.0, 37C, recombinant mutant K240N
88
2.2
-
L-methionine
-
pH 8.0, 30C, recombinant enzyme
88
5.46
-
L-methionine
-
pH 8.0, 37C, recombinant mutant K240I
88
8.9
-
L-methionine
-
pH 8.0, 30C
88
12.7
-
L-methionine
-
pH 8.0, 30C, recombinant enzyme
88
20.6
-
L-methionine
-
pH 8.0, 37C, recombinant mutant K240M
88
22.8
-
L-methionine
-
pH 8.0, 30C, recombinant enzyme
88
39
-
L-methionine
-
pH 8.0, 37C, recombinant mutant K240R
88
66.8
-
L-methionine
-
pH 8.0, 37C, recombinant wild-type enzyme
88
0.52
-
L-Methionine sulfone
-
pH 8.0, 30C
3081
0.2
-
L-methionine sulfoxide
-
pH 8.0, 30C, recombinant enzyme
5988
0.382
-
L-methionine sulfoxide
-
pH 8.0, 30C, recombinant enzyme
5988
0.4
-
L-methionine sulfoxide
-
pH 8.0, 30C
5988
0.413
-
L-methionine sulfoxide
-
pH 8.0, 30C, recombinant enzyme
5988
0.28
-
L-Vinylglycine
-
pH 8.0, 30C
2204
0.36
-
O-acetyl-DL-homoserine
-
pH 8.0, 30C
41724
3.94
-
S-Benzyl-L-cysteine
-
pH 8.0, 30C, recombinant enzyme
3362
11.1
-
S-Benzyl-L-cysteine
-
pH 8.0, 30C, recombinant enzyme
3362
28.7
-
S-Benzyl-L-cysteine
-
pH 8.0, 30C, recombinant enzyme
3362
3.71
-
S-ethyl-L-cysteine
-
pH 8.0, 30C, recombinant enzyme
2417
9.83
-
S-ethyl-L-cysteine
-
pH 8.0, 30C, recombinant enzyme
2417
17.6
-
S-ethyl-L-cysteine
-
pH 8.0, 30C, recombinant enzyme
2417
4.13
-
S-ethyl-L-homocysteine
-
pH 8.0, 30C, recombinant enzyme
22159
10.8
-
S-ethyl-L-homocysteine
-
pH 8.0, 30C, recombinant enzyme
22159
25.4
-
S-ethyl-L-homocysteine
-
pH 8.0, 30C, recombinant enzyme
22159
0.3
-
S-methyl-L-cysteine
-
pH 8.0, 37C, recombinant mutant Y114F/C116H
929
2.36
-
S-methyl-L-cysteine
-
pH 8.0, 37C, recombinant wild-type enzyme
929
22
-
S-methyl-L-cysteine
-
pH 8.0, 37C, recombinant mutant C166H
929
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.035
-
DL-propargylglycine
Q86D27, Q86D28
-
49
-
glycine
-
pH 8.0, 30C
8.3
-
L-2-aminobutanoate
-
pH 8.0, 30C
3.4
-
L-alanine
-
pH 8.0, 30C
0.6
-
L-norleucine
-
pH 8.0, 30C
0.6
-
L-norleucine
-
pH and temperature not specified in the publication
4.7
-
L-norvaline
-
pH 8.0, 30C
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000389
-
myrsinoic acid B
-
-
0.0105
-
myrsinoic acid B
-
in 50 mM Tris-HCl (pH 7.5) containing 0.05 mM pyridoxal 5'-phosphate, at 37C
0.0303
-
myrsinoic acid B
-
in 50 mM Tris-HCl (pH 7.5) containing 0.05 mM pyridoxal 5'-phosphate, at 37C
0.0303
-
myrsinoic acid B
-
-
0.0824
-
myrsinoic acid B
-
in 50 mM Tris-HCl (pH 7.5) containing 0.05 mM pyridoxal 5'-phosphate, at 37C
0.0824
-
myrsinoic acid B
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0013
-
-
in citrate phosphate buffer, pH 7.0, at 30C
0.0014
-
-
in citrate phosphate buffer, pH 7.0, at 30C
0.0015
-
-
in citrate phosphate buffer, pH 7.0, at 30C
0.0016
-
-
in citrate phosphate buffer, pH 7.0, at 30C
0.0017
-
-
in citrate phosphate buffer, pH 7.0, at 30C
0.0019
-
-
in citrate phosphate buffer, pH 7.0, at 30C
0.002
-
-
in citrate phosphate buffer, pH 7.0, at 30C
0.0021
-
-
in citrate phosphate buffer, pH 7.0, at 30C
0.0023
-
-
in citrate phosphate buffer, pH 7.0, at 30C
0.0026
-
-
in citrate phosphate buffer, pH 7.0, at 30C
0.0028
-
-
in citrate phosphate buffer, pH 7.0, at 30C
0.003
-
-
in citrate phosphate buffer, pH 7.0, at 30C
0.173
-
-
coconut seed as solid substrate
0.215
-
-
cotton seed as solid substrate
0.235
-
-
rice bran as solid substrate
0.328
-
-
wheat flour as solid substrate
0.36
-
Q86D27, Q86D28
recombinant EhMGL1
0.44
-
Q86D27, Q86D28
recombinant EhMGL2
0.536
-
-
lentil hulls as solid substrate
0.62
-
-
wheat bran as solid substrate
0.63
-
-
broad bean as solid substrate
0.67
-
-
chicken feathers as solid substrate
0.723
-
-
suya bean as solid substrate
5
-
-
purified His-tagged recombinant enzyme, pH 8.0, 30C, substrate L-methionine
10
-
Q84AR1
purified enzyme
10.2
-
-
purified recombinant enzyme, pH 8.0, 30C, substrate L-methionine
11
-
-
after treatment with PEG
12.8
-
-
purified His-tagged recombinant enzyme, pH 8.0, 30C, substrate L-methionine
14
-
-, Q5MQ31
recombinant enzyme, substrate L-cystathionine, without nisin induction
16.6
-
-
purified His-tagged recombinant enzyme, pH 8.0, 30C, substrate L-methionine
19
-
-, Q5MQ31
recombinant enzyme, substrate L-cystine or L-methionine, without nisin induction
31
-
-
-
40
-
-
after DEAE-Sepharose FF; after diafiltration; after Sephacryl S-200 HR
41
-
-
after DTT treatment
44
-
-
methoxypolyethylene glycol succinimidyl glutarate 5000 treated recombinant METase
54
-
-
crystals
57
-
-
purified recombinant enzyme
57
-
-
after concentration
60
-
-, Q5MQ31
wild-type enzyme, substrate L-cystathionine, without nisin induction
90
-
-, Q5MQ31
wild-type enzyme, substrate L-methionine, without nisin induction
123
-
-, Q5MQ31
wild-type enzyme, substrate L-cystine, without nisin induction
additional information
-
-
-
additional information
-
-
-
additional information
-
-, Q5MQ31
recombinant enzyme, substrate L-cystathione, with nisin induction, value from 15 to 65 micromol/min/mg; recombinant enzyme, substrate L-cystine, with nisin induction, value from 21 to 137 micromol/min/mg; recombinant enzyme, substrate L-methionine, with nisin induction, value from 21 to 103 micromol/min/mg
additional information
-
-
value is 31.0 U/mg protein
additional information
-
-
value is 61 U/mg protein
additional information
-
-
value is 44.8 U/mg protein
additional information
-
-
value is 228.9 U/mg protein
additional information
-
-
value is 10 U/mg protein
additional information
-
-
value is 0.26 U/mg protein
additional information
-
-
value is 0.44 U/mg protein
additional information
-
-
value is 0.04 U/mg protein
additional information
-
-
value is 1.8 U/mg protein; value is 45.3 U/mg protein
additional information
-
-
value is 36.6 U/mg protein
additional information
-
-
value is 3.17 U/mg protein
additional information
-
-
0.08 micromol/min/ml, substrate is tyrosine; 0.18 micromol/min/ml, substrate is casein; 0.23 micromol/min/ml, substrate is asparagine; 0.24 micromol/min/ml, substrate is chicken feather; 0.25 micromol/min/ml, substrate is arginine; 0.25 micromol/min/ml, substrate is keratin; 0.25 micromol/min/ml, substrate is urea; 0.27 micromol/min/ml, substrate is gelatine; 0.27 micromol/min/ml, substrate is glutamic acid; 0.27 micromol/min/ml, substrate is glutamine; 0.29 micromol/min/ml, substrate is bovine serum albumin; 0.29 micromol/min/ml, substrate is glycine; 0.29 micromol/min/ml, substrate is N-acetylglucosamine; 0.2 micromol/min/ml, substrate is sheep wool; 0.30 micromol/min/ml, substrate is L-methionine
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.6
8.2
Q86D27, Q86D28
approx. 14% of maximal activity at pH 5.6, approx. 10% of maximal activity at pH 8.2; approx. 55% of maximal activity at pH 5.6, approx. 95% of maximal activity at pH 8.2
7
8
-
decrease of kcat/Km at high pH
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.9
-
Q86D27, Q86D28
two-dimensional PAGE, recombinant EhMGL1
6
-
Q86D27, Q86D28
two-dimensional PAGE, native EhMGL1
6.5
-
Q86D27, Q86D28
two-dimensional PAGE, recombinant EhMGL2
6.7
-
Q86D27, Q86D28
two-dimensional PAGE, native EhMGL2
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Pseudomonas putida ICR 3460
-
-
-
Manually annotated by BRENDA team
-
expression is increased 2.5fold by growth on low sulfate medium
Manually annotated by BRENDA team
-
prostate cancer cell
Manually annotated by BRENDA team
additional information
-
expression in aerial organs
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
42560
-
-
METase, mass spectrometry
42630
-
-
METase, calculated from amino acid sequence
43000
45000
Q84AR1
SDS-PAGE
43000
-
-
SDS-PAGE
43000
-
-, Q5MQ31
SDS-PAGE
43000
-
-
SDS-PAGE
43500
-
-
SDS-PAGE
44670
-
-, Q5MQ31
calculated from amino acid sequence
77510
-
-
DTT-treated PEG-METase, mass spectrometry
81400
-
Q7MX71
gel filtration
82500
-
-
DTT-treated PEG-METase, calculated from amino acid sequence; DTT-untreated PEG-METase, mass spectrometry
86700
-
-
DTT-untreated PEG-METase, calculated from amino acid sequence
149000
-
-
gel filtration
154100
-
Q8RDT4
gel filtration
159000
-
-
low-angle light-scattering method
159000
-
-
-
160000
-
-
gel filtration
160000
-
-
gel filtration
160000
-
-
gel filtration
165000
-
-
sedimentation equilibrium method
167500
-
Q73KL7
gel filtration
170000
-
-
gel filtration
170000
-
-, Q5MQ31
SDS-PAGE
170000
-
-
about, recombinant detagged enzyme, gel filtration
171000
177000
Q86D27, Q86D28
gel filtration, native and recombinant EhMGL1; gel filtration, native and recombinant EhMGL2
172000
-
-
PEG-conjugated methioninase, native PAGE
172000
-
-
gel filtration
173000
-
-
sedimentation equilibrium method
173000
-
-
-
174000
-
-
low-angle light-scattering method
180000
-
-
gel filtration
258000
-
-
native enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 43100, calculated
?
-
x * 47820, calculated, x * 48000, SDS-PAGE
dimer
Q7MX71
2 * 43000, SDS-PAGE, 2 * 43300, calculated
dimer
-
2 * 43000, SDS-PAGE, 2 * 43300, calculated
-
homotetramer
-
-
polymer
-
x * 40000, x * 48000, disc gel electrophoresis, guanidine hydrochloride
tetramer
-
4 * 43000, SDS-PAGE
tetramer
-
4 * 43000, SDS-PAGE
tetramer
-
4 * 43000, SDS-PAGE
tetramer
-
4 * 43000, SDS-PAGE
tetramer
-
4 * 45000, SDS-PAGE
tetramer
-
4 * 41000, SDS-PAGE
tetramer
-
4 * 55000, SDS-PAGE
tetramer
-
4 * 43000-45000, SDS-PAGE
tetramer
-
4 * 37500, SDS-PAGE
tetramer
-
4 * 44000, SDS-PAGE
tetramer
-, Q86D28
x-ray crystallography
tetramer
Q86D27, Q86D28
4 * 43300, SDS-PAGE, immunoblot, native and recombinant EhMGL1 form homotetramers
tetramer
Q86D27, Q86D28
4 * 43700, SDS-PAGE, immunoblot, native and recombinant EhMGL2 form homotetramers
tetramer
-
4 * 42000, SDS-PAGE, gel filtration
tetramer
-
alpha4, crystal structure
tetramer
-
crystallization data. Tetramer with four active sites, each active site is formed by aminoacid residues from two subunits and contains pyridoxal 5'-phosphate
tetramer
-
4 * 42600, SDS-PAGE
tetramer
-
4*43500, SDS-PAGE
tetramer
Q8RDT4
4 * 43000, SDS-PAGE, 4 * 43300, calculated
tetramer
Q73KL7
4 * 43500, calculated and SDS-PAGE
tetramer
-
4 * 44040, His-tagged enzyme, sequence calcualtion
tetramer
-
4 * 44080, His-tagged enzyme, sequence calcualtion
tetramer
-
4 * 44360, His-tagged enzyme, sequence calcualtion
tetramer
-
dimer of dimers, 2 active sites, structure model
tetramer
-
dimer of dimers, each dimer contains two active centers formed by amino acid residues of both subunits of the dimer. The protein monomer consists of three domains: N-terminal, central PLP-binding, and C-terminal
tetramer
Fusobacterium nucleatum subsp. nucleatum, ATCC 25586
-
4 * 43000, SDS-PAGE, 4 * 43300, calculated
-
tetramer
Aspergillus sp. Rs-1a
-
-
-
tetramer
-
4 * 43500, calculated and SDS-PAGE
-
tetramer
Pseudomonas putida ICR 3460
-
4 * 43000, SDS-PAGE
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
sequence contains no targeting signal
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging-drop vapor-diffusion method
-
hanging-drop vapor-diffusion method
-
hanging-drop vapor-diffusion method
-
at 1.35 A resolution
-
enzyme in complex with gamma-(L-1-amino-3-methylthiopropylphosphinic acid), beta-(S-ethyl-L-cysteine), and L-norleucine, soaking of holoenzyme crystals in a cryoprotective solution containing 35% PEG monomethyl ether 2000, 50 mM Tris-HCl, pH 8.5, 0.2 mM pyridoxal 5'-phosphate, 25 mM DTT, with addition of the respective ligand, 6.8 mM of beta-(S-ethyl-L-cysteine), 40 mM L-norleucine, or 48 mM gamma-(L-1-amino-3-methylthiopropylphosphinic acid), during different time intervals of 5-120 min, 1-2 weeks, X-ray diffraction structure determination and anaysis at 1.45-1.84 A resolution, molecular replacement
-
hanging-drop vapor-diffusion method
-
purified recombinant enzyme in complex with inhibitor glycine, crystals are obtained using a method without the presence of ammonium sulfate, complexing with glycine by soaking of holoenzyme crystals in a cryoprotective mother liquid solution to which glycine is added stepwise from 5 mM to 20 mM during 20 min,, 1-2 weeks, X-ray diffraction structure determination and analysis at 2.45 A resolution, molecular replacement
-
to 1.65 A resolution. Absence of an aldimine bond between the active site Lys210 and pyridoxal 5'-phosphate in crystals, grown in monomethyl ether polyethylene glycol 2000 in the presence of ammonium sulfate
-
hanging-drop vapor-diffusion method
-
sitting drop vapour diffusion method, using 1.8 M ammonium sulfate, 0.1 M cacodylate buffer pH 6.2, 0.1 M lithium citrate, and 0.01 M betaine
-, Q86D28
space group P212121
-
hanging-drop vapor-diffusion method
-
1.8 A resolution. Residues Y59 and R61 of neighbouring subunits contact the phosphate group of pyridoxal 5-phosphate. Residues K240, D241 and R61 of one partner monomer and Y114 and C116 of the other form a hydrogen-bond network in the active site
-
hanging-drop vapor diffusion, protein solution containing 10-20 mg/ml protein in 20 mM sodium phosphate, pH 7.2, 0.5 mM pyridoxal 5'-phosphate and 0.5% 2-mercaptoethanol is equilibrated against a reservoir solution consisting of 15% polyethylene glycol 6000, 250 mM NaCl, 200 mM MES-NaOH, pH 6.5, 0.5 mM pyridoxal 5'-phosphate and 0.5% 2-mercaptoethanol, crystals grow at room temperatur within 1 week, crystals diffract to 1.7 A
-
hanging-drop vapor-diffusion method
-
purified recombinant wild-type and mutant C116H enzymes, the latter complexed with L-methionine or L-homocysteine, sitting drop vapour diffusion method, mixing of 500 nl of 20 mg/ml protein 10 mM HEPES-NaOH, pH 7.4, with 500 nl of reservoir solution containing 200 mM MES-NaOH, pH 6.2, with 12.5% w/v PEG6000, 250 mm ammonium sulfate, 0.5 mM pyridoxal 5'-phosphate, and 0.5% v/v 2-mercaptoethanol, and equilibration against 0.1 ml of reservoir solution, 20C, for ligand binding soaking of crystals in reservoir solution containing 50 mM amino acid, method optimization, X-ray diffraction structure determination and analysis at 2.1-2.6 A resolution, molecular replacement
-
sitting-drop vapor diffusion, 1.25 M ammonium sulfate in 100 mM MES-HCl, pH 6.0 as reservoir solution, protein solution consists of 10-20 mg/ml METase in 120 mM sodium chloride, 10 mM sodium phosphate, pH 7.2, crystals diffract to at least 2.68 A
-
hanging-drop vapor-diffusion method
-
;
O15564, O15565
hanging-drop vapor-diffusion method
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.1
-
-
99% loss of activity after 24 h
6
7.5
-
stable for 24 h at 4C
6
8
-
stable for 24 h
6
9
-
stable, at least 3 h
6
9
-
at 0C; stable, at least 3 h
6.5
9
-
50C, 5 min, stable in pH-range
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
several days without loss of activity
50
-
-
pH 6.5-9.0, stable, 5 min
50
-
-
stable up to 30 min
50
-
-
purified wild-type enzyme and mutants, all completely stable, except for mutants D241H and D241I loosing about 10% activity
60
-
-
18% loss of activity, 5 min
70
-
-
purified mutant D241R, loss of 70% activity
75
-
-
30% loss of activity after 25 min
75
-
-
purified wild-type enzyme and mutants D241T, D241M, D241N, D241E, D241H, D241K, K240S, K240R, and K240C completely stable up to, loss of 35% activity for mutant K240N, of 15% for D241I, of 85% for mutant K240M, and of 95% for mutant K240I and D241R, profiles, overview
80
-
-
purified wild-type enzyme and mutants, inactivation of all besides mutants D241E, and K240N, retaining 20% and K240M retaining 10% activity, respectively
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
significantly inactivated in dilute buffer
-
the purified highly potent PEG-METase can be stored at -80C for several months with no significant loss of activity
-
freezing and thawing, slight decrease in activity
-
plasma half-life of polyethylene glycolylated rMETase in mice increases from 2 h for naked rMETase to 38 h for polyethylene glycolylated rMETase
-
significantly inactivated in dilute buffer
-
the purified enzyme can be stored at -80C for several months with no significant loss of activity
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
NaBH4, irreversible inactivation
-
34529
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C for several month without loss of activity
-
-20C, pH 7.2, potassium phosphate buffer, 0.1 M, several months
-
4C or -20C, 50-60% loss of activity within 7 days
-
additional information
-
4C, 20 mM potassium phosphate buffer (pH 7.4) with 0.02 mM pyridoxal 5'-phosphate, 1 mM EDTA (pH 8.0), 0.01% (v/v) beta-mercaptoethanol containing 0.3 M NaCl, 2 months, enzyme remains stable
-
additional information
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ion exchange and gel filtration chromatography
-
ion exchange and gel filtration chromatography
-
partially purified by ammonium sulfate fractionation
-
ion exchange and gel filtration chromatography
-
affinity chromatography on nickel-nitrilotriacetic acid resin
-, Q5MQ31
ion exchange and gel filtration chromatography
-
ion exchange and gel filtration chromatography
-
recombinant enzyme from Escherichia coli strain BL21
-
recombinant protein
-
ion exchange and gel filtration chromatography
-
ion exchange and gel filtration chromatography
-
ion exchange and gel filtration chromatography
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, cleavage of the His-tag by thrombin and elimination by gel filtration
-
GSTrap HP column chromatography and Sephacryl S-300 gel filtration
-, Q86D28
ion exchange and gel filtration chromatography
-
recombinant EhMGL1; recombinant EhMGL2
Q86D27, Q86D28
ion exchange and gel filtration chromatography
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, cleavage of the His-tag by thrombin and elimination by gel filtration
-
DEAE-Toyopearl 650M column chromatography and Sephacryl S-200 HR gel filtration
-
ion exchange and gel filtration chromatography
-
native enzyme by anion exchange chromatography and gel filtration
-
purification of recombinant methioninase expressed in Escherichia coli
-
QAE-Sepharose column chromatography
-
recombinant L-methionine gamma-lyase
-
recombinant METase
-
recombinant rMETase
-
recombinant wild-type and mutant enzymes from Escherichia coli strain HB101 by PEG 6000 fractionation, dialysis, folowed by anion exchange chromatography, and gel filtration
-
ion exchange and gel filtration chromatography
-
ion exchange and gel filtration chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
transformed into Agrobacterium tumefaciens
Q9SGU9
expression in Escherichia coli
-, Q5MQ31
expression in Lactococcus lactis
-, Q5MQ31
expression in Escherichia coli
-
expression in Escherichia coli BL21
-
recombinant enzyme expression in Escherichia coli strain BL21
-
expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
expressed in Escherichia coli BL21 Star (DE3) cells
-, Q86D28
expression in Escherichia coli
-
expression of EhMGL1 in Escherichia coli; expression of EhMGL2 in Escherichia coli
Q86D27, Q86D28
expression in Escherichia coli
-
expression in Escherichia coli
-
cloning of mgl gene
-
expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
expressed in Escherichia coli
-
expressed in Escherichia coli strain HB101
-
expression in Escherichia coli
-
overexpression in Escherichia coli
-
PEG conjugated methioninase-expression in Escherichia coli
-
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain HB101
-
gene StMGL1, expression analysis
-
expression in Escherichia coli
-
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
transcription is strongly regulated by exogenous methionine, low sulfate, osmotic stress and availability of threonine or isoleucine
-
about 3fold increased expression during drought stress
Q9SGU9
about 50fold induction of enzyme expression in seedlings defective in isocitrate lyase
-
higher expression in imbibed seeds
-
higher transcript levels in stems and siliques than in leaves
-
strongly expression in siliques
Q9SGU9
upregulation under methionine-rich conditions
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C110G
Q86D28
decrease in kcat values for both L-methionine and L-cysteine
C110S
Q86D28
slightly reduced catalytic activites
C113G
Q86D28
20% increase in activity with L-methionine
C113S
Q86D28
reduced catalytic activites
R55A
Q86D28
decrease in catalytic activity
R58A
Q86D28
complete loss of activity
Y108F
Q86D28
almost 100% reduction in alpha-gamma-elimination of both L-methionine and homocysteine
Y114F
-
reduced enzyme activity
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
-
the mutant possesses little catalytic activity and shows marked increase in activity toward L-cysteine and a decrease in that toward L-methionine
C116H
-
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/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
-
9% of wild-type activity
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
-
40% of wild-type activity
C116T
-
the mutant possesses little catalytic activity, while its affinity for each substrate is almost the same as that of the wild type enzyme
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
F128C
-
112% of wild-type activity
G9C/D385C
-
46% of wild-type activity
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
K240S
-
site-directed mutagenesis
L341H
-
9% of wild-type activity
R61A
-
1% of wild-type activity
R61E
-
no activity
R61F
-
2% of wild-type activity
S248C
-
131% of wild-type activity
C113G
-
MGL1, reduced activity towards methionine and homocysteine
C116G
-
MGL2, reduced activity towards methionine and homocysteine
additional information
-
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
-
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
-, Q5MQ31
delta-mgl knock-out mutant, results in a 62% decrease in thiol-producing activity and a 97% decrease in total volatile sulfur compounds production
Y111F
Q86D28
about 80% reduction in alpha-gamma-elimination of both L-methionine and homocysteine
additional information
-
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
Y114F
-
0.1% of wild-type kcat for L-methionine
additional information
-
gene silencing by siRNA, amino acid profiling of transgenic lines, overview
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
Achromobacter starkeyi, Aeromonas sp.
-
enzyme therapy against various types of methionine-dependent tumors
environmental protection
-
enzyme is not an important source of volatile methanethiol
medicine
-
utilization for the treatment of cancers
medicine
-
enzyme therapy against various types of methionine-dependent tumors
medicine
Aspergillus sp. Rs-1a
-
enzyme therapy against various types of methionine-dependent tumors
-
medicine
-
utilization for the treatment of cancers
nutrition
-, Q5MQ31
the enzymatic degradation of L-methionine and subsequent formation of volatile sulfur compounds is believed to be essential for flavour development in cheese. Overproduction of Brevibacterium linens methionine-gamma-lyase in bacteria such as lactic acid bacteria can be a more efficient way to increase cheese flavour of some cheeses, among others, cheddar, than the addition of Brevibacterium linens cells or extracts, which is not successful in enhancing cheese flavour
medicine
-
enzyme therapy against various types of methionine-dependent tumors
nutrition
-, Q5MQ31
importance in flavor formation during cheese ripening
medicine
-
enzyme therapy against various types of methionine-dependent tumors
medicine
-
the enzyme is of interest as an anticancer agent, since the growth of malignant cells of various origins (unlike the growth of normal cells) is accompanied by obligatory methionine utilization, and the nezyme is absent in mammalian cells. IC50 of MGL for several tumor cell cultures, overview
synthesis
-
presence of a hybrid plasmid in Escherichia coli K12 containing the enzyme gene leads to a decrease in efficiciency of EcoKI restriction
medicine
-
enzyme therapy against various types of methionine-dependent tumors
medicine
-
the enzyme is of interest as an anticancer agent, since the growth of malignant cells of various origins (unlike the growth of normal cells) is accompanied by obligatory methionine utilization, and the enzyme is absent in mammalian cells. IC50 of MGL for several tumor cell cultures, overview
medicine
-
the enzyme is of interest as an anticancer agent, since the growth of malignant cells of various origins (unlike the growth of normal cells) is accompanied by obligatory methionine utilization, and the nezyme is absent in mammalian cells. IC50 of MGL for several tumor cell cultures, overview
medicine
-
causes adverse reaction in treatment of amoebiasis with trifluormethionine by degradation
medicine
-
enzyme therapy against various types of methionine-dependent tumors
medicine
-
utilization for the treatment of cancers
medicine
-
inhibitory effect of fusion protein on an ovaran cancer cell line, fusion protein produces a dose-dependent inhibition of the proliferation of pancreatic cancer cell lines
medicine
-
utilization for the treatment of cancers
medicine
-
wild-type p53-expressing LNCaP human prostate cancer cells are more sensitive to cotreatment with selenomethionine and methionine gamma-lyase than p53-null PC3 human prostate cancer cells. Selenomethionine and and methionine gamma-lyase co-treatment significantly increases levels of superoxide and apoptosis in LNCaP cells. Cotreatment selenomethionine and methionine gamma-lyase results in increased levels of phosphorylated p53, total p53, Bax, and p21Waf1 proteins. LNCaP cells treated with selenomethionine and methionine gamma-lyase also show p53 translocation to mitochondria, decreased mitochondrial membrane potential, cytochrome c release into the cytosol, and activation of caspase 9. The effects selenomethionine and methionine gamma-lyase are suppressed by pre-treatment with a synthetic superoxide dismutase mimic or by knockdown of p53 via RNA interference
medicine
-
enzyme therapy against various types of methionine-dependent tumors
medicine
-
PEG treated METase is a potential anticancer agent that can deplete L-methionine from plasma. DTT-treated PEG-METase can be produced on a large scale in sufficient quality for therapeutic use
medicine
-
recombinant METase targets the elevated methionine dependence of tumor cells and arrests their growth as well as makes tumors more sensitive to standard chemotherapy agents. The combination of methoxypolyethylene glycol succinimidyl glutarate 5000 recombinant METase treatment with pyridoxal-5'-phosphate infusion suggests an effective clinical strategy for long-term methionine depletion to arrest cancer growth
medicine
-
combined treatment of B16-F10 melanoma cells with selenomethionine and L-methionine gamma-lyase added to culture medium decreases expression of integrins alpha4, beta1, alphany and beta3 and inhibits melanoa-extracellular matrix adhesion. Caspase-mediated apoptosis is induced following loss of cell adherence
medicine
-
utilization for the treatment of cancers
analysis
-
the enzyme can be used for detection of S-adenosyl-L-homocysteine hydrolase activity and inhibition in a simple and robust fluorogenic enzymatic assay, method development, overview
drug development
-
endotoxins cause fever in humans and must be eliminated from biopharmaceuticals intended for parenteral administration which are produced by Escherichia coli. Endotoxins can be drastically removed by anion-exchange column chromatography. Thus, the combination of crystallization and anion-exchange column chromatography is suitable for purification of the enzyme
medicine
-
cancer therapy
medicine
-
rMETase is an enzyme active in preclinical mouse models of human cancer
medicine
-
enyzme therapy against various types of methionine-dependent tumors, enzyme therapy against various types of methionine-dependent tumors
medicine
-
utilization for the treatment of cancers
analysis
Pseudomonas putida ICR 3460
-
the enzyme can be used for detection of S-adenosyl-L-homocysteine hydrolase activity and inhibition in a simple and robust fluorogenic enzymatic assay, method development, overview
-
drug development
-
methyl mercaptan may not only cause oral malodour but also play an important role in the pathogenicity of Treptonema denticola. The enzyme may be an exploitable target for novel chemotherapeutic drugs. An inhibitor of METase may represent a new class of compounds with the potential for preventing and treating oral malodor
medicine
-
enzyme therapy against various types of methionine-dependent tumors
medicine
-
utilization for the treatment of cancers