Any feedback?
Information on EC 4.4.1.11 - methionine gamma-lyase and Organism(s) Citrobacter freundii and UniProt Accession Q84AR1
for references in articles please use BRENDA:EC4.4.1.11Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
Word Map
- 4.4.1.11
- lipase
- monoacylglycerol
-
endocannabinoids
- cannabinoids
- lectin
- putida
-
c-type
- 2-arachidonoylglycerol
- pyridoxal
- medicine
- monoglyceride
-
orthotopic
-
galactose-type
- galnac
- selenomethionine
- anandamide
- freundii
-
2-arachidonoyl
-
citrobacter
- alpha-ketobutyrate
- methylselenol
-
meibomian
-
methionine-dependent
- mercaptan
-
beta-lyase
-
5'-phosphate-dependent
-
dc-sign
-
s-substituted
- synthesis
- nutrition
- environmental protection
- analysis
- drug development
The taxonomic range for the selected organisms is: Citrobacter freundii
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
mgl, rmetase, metase, methioninase, l-methioninase, methionine gamma-lyase, l-methionine gamma-lyase, methionine-gamma-lyase, cale6, l-methionase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-methioninase
L-methionine gamma-lyase
L-methionine-alpha-deamino-gamma-mercaptomethane-lyase
-
-
-
-
lyase, methionine
-
-
-
-
methioninase
-
-
-
-
methionine dethiomethylase
-
-
-
-
methionine gamma-lyase
methionine lyase
-
-
-
-
L-methioninase
-
-
-
-
L-methionine gamma-lyase
-
-
-
-
methionine gamma-lyase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-methionine + H2O = methanethiol + NH3 + 2-oxobutanoate
gamma-elimination reaction mechanism and intermediates, overview
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
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -
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.
CAS REGISTRY NUMBER
COMMENTARY
42616-25-1
-
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
-
-
-
?
DL-homocysteine + H2O
2-oxobutanoate + NH3 + hydrogen sulfide
-
-
-
?
DL-homocysteine + H2O
hydrogen sulfide + NH3 + 2-oxobutanoate
-
-
-
?
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
-
-
?
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-ethyl-L-homocysteine + H2O
ethanethiol + NH3 + 2-oxobutanoate
-
-
-
?
S-propyl-L-cysteine + H2O
propanethiol + NH3 + 2-oxopropanoate
-
-
-
?
S-benzyl-L-cysteine + H2O
thiobenzyl alcohol + NH3 + 2-oxopropanoate
-
-
-
-
?
S-ethyl-L-homocysteine + H2O
ethanethiol + NH3 + 2-oxobutanoate
-
-
-
-
?
S-methyl-L-cysteine + H2O
methanethiol + NH3 + 2-oxopropanoate
-
-
-
-
?
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, 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
-
-
?
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-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
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
gamma-elimination reaction
-
-
?
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
?
-
-
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
-
-
?
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
gamma-elimination reaction
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
gamma-elimination reaction
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
additional information
additional information
steady-state kinetics
-
additional information
additional information
-
steady-state kinetics for beta- and gamma-elimination reactions, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.6
L-norleucine
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10.2
-
purified recombinant enzyme, pH 8.0, 30°C, substrate L-methionine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the subclass of cystathionine beta-lyase with type I folding of the polypeptide chain of pyridoxal 5'-phosphate-dependent enzymes
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
additional information
catalytic residues: Lys210 is the base, and Tyr113 acts as a general acid, active site structure, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
tetramer
-
crystallization data. Tetramer with four active sites, each active site is formed by aminoacid residues from two subunits and contains pyridoxal 5'-phosphate
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
computational model of the enzyme and the external aldimine intermediate, based on the crystal structures of methionine gamma-lyase from Clostridium sporogenes and Citrobacter freundii. The catalytic reaction can be divided into the formation of external aldimine intermediate from the internal aldimine intermediate, and a second step, when the external aldimine intermediate converts to the aminocrotonate intermediate, which contains complex asynchronous and concerted proton transfer processes
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
mutant C115H, in complex with inhibitor L-norleucine, to 1.45 A resolution. The inhibotor binds both noncovalently and covalently at the active site, corresponding to the intermediates of the gamma- and beta-elimination reactions, Michaelis complex and the external aldimine
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
structure of mutant Y58F, to 1.96 A resolution. The mutation does not result in essential changes of the conformation of the active site
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A366Y
mutant of the C-terminal flexible loop at the active site entry channel
C115A
mutation leads to a decrease of the catalytic efficiency in the gamma-elimination reaction of the physiological substrate by more than an order of magnitude
C115H
P357I
mutant of the C-terminal flexible loop at the active site entry channel
P360Q
mutant of the C-terminal flexible loop at the active site entry channel
V358Y
mutant exhibits a 1.9fold increase in the catalytic rate and a 3fold increase in Km value, catalytic efficiency is similar to wild type MGL. The cytotoxic activity towards a panel of cancer and nonmalignant cell lines is lower than that of wild-type
Y58F
mutation leads to a decrease of catalytic efficiencies in both gamma- and beta-elimination reactions of about two orders of magnitude and to a change of rate the limiting step of the physiological reaction
additional information
C115H
mutant cleaves S-alk(en)yl-L-cysteine sulfoxides more effectively than the wild type, reaction of EC 4.4.1.4
C115H
mutant is inactive in the gamma-elimination reaction of methionine while fully active in the gamma-elimination reaction of O-acetyl-L-homoserine and in the beta-elimination reaction of S-alk(en)yl-substituted cysteines
C115H
mutation leads to loss of activity in the gamma-elimination reaction of the physiological substrate. The catalytic efficiency in the beta-elimination reaction of S-substituted L-cysteine sulfoxides is increased by about an order of magnitude compared to the wild type
additional information
site-saturation mutagenesis at residues of the C-terminal flexible loop at the active site entry channel, P357, V358, P360 and A366
additional information
-
site-saturation mutagenesis at residues of the C-terminal flexible loop at the active site entry channel, P357, V358, P360 and A366
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
synthesis
-
presence of a hybrid plasmid in Escherichia coli K12 containing the enzyme gene leads to a decrease in efficiciency of EcoKI restriction
medicine
encapsulation of enzyme in nanoporous wet silica gels to be delivered at the site of action. Gels exhibit spectroscopic properties very similar to methionine gamma lyase in solution, a higher stability with respect to the soluble enzyme and catalytic activity is 6fold lower than in solution
medicine
mice plasma methionine decreases to undetectable level 10 min after methionine gamma lyase 1000 U/kg injection. The enzyme shows a pharmakokinetic half-life of 1.69 h
medicine
mutant V358Y selectively inhibits cancer cell growth with a half-maximal inhibitory concentration almost 2fold lower than the wild type
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mamaeva, D.V.; Morozova, E.A.; Nikulin, A.D.; Revtovich, S.V.; Nikonov, S.V.; Garber, M.B.; Demidkina, T.V.
Structure of Citrobacter freundii L-methionine gamma-lyase
Acta Crystallogr. Sect. F
61
546-549
2005
Citrobacter freundii
Manukhov, I.V.; Mamaeva, D.V.; Rastorguev, S.M.; Faleev, N.G.; Morozova, E.A.; Demidkina, T.V.; Zavilgelsky, G.B.
A gene encoding L-methionine gamma-lyase is present in Enterobacteriaceae family genomes: identification and characterization of Citrobacter freundii L-methionine gamma-lyase
J. Bacteriol.
187
3889-3893
2005
Citrobacter freundii (Q84AR1), Citrobacter freundii, Citrobacter freundii ATCC 29063 (Q84AR1)
Nikulin, A.; Revtovich, S.; Morozova, E.; Nevskaya, N.; Nikonov, S.; Garber, M.; Demidkina, T.
High-resolution structure of methionine gamma-lyase from Citrobacter freundii
Acta Crystallogr. Sect. D
64
211-218
2008
Citrobacter freundii
Manukhov, I.V.; Mamaeva, D.V.; Morozova, E.A.; Rastorguev, S.M.; Faleev, N.G.; Demidkina, T.V.; Zavilgelsky, G.B.
L-methionine gamma-lyase from Citrobacter freundii: cloning of the gene and kinetic parameters of the enzyme
Biochemistry (Moscow)
71
361-369
2006
Citrobacter freundii
El-Sayed, A.S.
Microbial L-methioninase: production, molecular characterization, and therapeutic applications
Appl. Microbiol. Biotechnol.
86
445-467
2010
Achromobacter starkeyi, Aeromonas sp., Aspergillus flavipes, Aspergillus sp., Citrobacter freundii, Citrobacter intermedius, Cladosporium cladosporioides, Clostridium sporogenes, Entamoeba histolytica, Lactococcus lactis, no activity in mammalia, Pseudomonas putida, Treponema denticola, Trichomonas vaginalis, Brevibacterium linens BL2, Aspergillus sp. Rs-1a
Faleev, N.G.; Alferov, K.V.; Tsvetikova, M.A.; Morozova, E.A.; Revtovich, S.V.; Khurs, E.N.; Vorobev, M.M.; Phillips, R.S.; Demidkina, T.V.; Khomutov, R.M.
Methionine gamma-lyase: mechanistic deductions from the kinetic pH-effects. The role of the ionic state of a substrate in the enzymatic activity
Biochim. Biophys. Acta
1794
1414-1420
2009
Citrobacter freundii
Morozova, E.A.; Bazhulina, N.P.; Anufrieva, N.V.; Mamaeva, D.V.; Tkachev, Y.V.; Streltsov, S.A.; Timofeev, V.P.; Faleev, N.G.; Demidkina, T.V.
Kinetic and spectral parameters of interaction of Citrobacter freundii methionine gamma-lyase with amino acids
Biochemistry (Moscow)
75
1272-1280
2010
Citrobacter freundii
Ronda, L.; Bazhulina, N.P.; Morozova, E.A.; Revtovich, S.V.; Chekhov, V.O.; Nikulin, A.D.; Demidkina, T.V.; Mozzarelli, A.
Exploring methionine gamma-lyase structure-function relationship via microspectrophotometry and X-ray crystallography
Biochim. Biophys. Acta
1814
834-842
2011
Citrobacter freundii
Morozova, E.A.; Kulikova, V.V.; Yashin, D.V.; Anufrieva, N.V.; Anisimova, N.Y.; Revtovich, S.V.; Kotlov, M.I.; Belyi, Y.F.; Pokrovsky, V.S.; Demidkina, T.V.
Kinetic parameters and cytotoxic activity of recombinant methionine gamma-lyase from Clostridium tetani, Clostridium sporogenes, Porphyromonas gingivalis and Citrobacter freundii
Acta Naturae
5
92-98
2013
Porphyromonas gingivalis, Citrobacter freundii, Clostridium sporogenes, Clostridium tetani
Revtovich, S.V.; Morozova, E.A.; Khurs, E.N.; Zakomirdina, L.N.; Nikulin, A.D.; Demidkina, T.V.; Khomutov, R.M.
Three-dimensional structures of noncovalent complexes of Citrobacter freundii methionine gamma-lyase with substrates
Biochemistry (Moscow)
76
564-570
2011
Citrobacter freundii (Q84AR1)
Revtovich, S.V.; Faleev, N.G.; Morozova, E.A.; Anufrieva, N.V.; Nikulin, A.D.; Demidkina, T.V.
Crystal structure of the external aldimine of Citrobacter freundii methionine gamma-lyase with glycine provides insight in mechanisms of two stages of physiological reaction and isotope exchange of alpha- and beta-protons of competitive inhibitors
Biochimie
101
161-167
2014
Citrobacter freundii (Q84AR1)
Anufrieva, N.V.; Faleev, N.G.; Morozova, E.A.; Bazhulina, N.P.; Revtovich, S.V.; Timofeev, V.P.; Tkachev, Y.V.; Nikulin, A.D.; Demidkina, T.V.
The role of active site tyrosine 58 in Citrobacter freundii methionine gamma-lyase
Biochim. Biophys. Acta
1854
1220-1228
2015
Citrobacter freundii (Q84AR1), Citrobacter freundii
Revtovich, S.V.; Morozova, E.A.; Kulikova, V.V.; Anufrieva, N.V.; Osipova, T.I.; Koval, V.S.; Nikulin, A.D.; Demidkina, T.V.
Crystal structure of mutant form Cys115His of Citrobacter freundii methionine gamma-lyase complexed with l-norleucine
Biochim. Biophys. Acta
1865
1123-1128
2017
Citrobacter freundii (Q84AR1)
Raboni, S.; Revtovich, S.; Demitri, N.; Giabbai, B.; Storici, P.; Cocconcelli, C.; Faggiano, S.; Rosini, E.; Pollegioni, L.; Galati, S.; Buschini, A.; Morozova, E.; Kulikova, V.; Nikulin, A.; Gabellieri, E.; Cioni, P.; Demidkina, T.; Mozzarelli, A.
Engineering methionine gamma-lyase from Citrobacter freundii for anticancer activity
Biochim. Biophys. Acta
1866
1260-1270
2018
Citrobacter freundii (Q84AR1), Citrobacter freundii
Morozova, E.; Kulikova, V.; Rodionov, A.; Revtovich, S.; Anufrieva, N.; Demidkina, T.
Engineered Citrobacter freundii methionine gamma-lyase effectively produces antimicrobial thiosulfinates
Biochimie
128-129
92-98
2016
Citrobacter freundii (Q84AR1), Citrobacter freundii
Kulikova, V.; Morozova, E.; Rodionov, A.; Koval, V.; Anufrieva, N.; Revtovich, S.; Demidkina, T.
Non-stereoselective decomposition of (+-)-S-alk(en)yl-l-cysteine sulfoxides to antibacterial thiosulfinates catalyzed by C115H mutant methionine gamma-lyase from Citrobacter freundii
Biochimie
151
42-44
2018
Citrobacter freundii (Q84AR1), Citrobacter freundii
Morozova, E.A.; Anufrieva, N.V.; Davydov, D.Z.; Komarova, M.V.; Dyakov, I.N.; Rodionov, A.N.; Demidkina, T.V.; Pokrovsky, V.S.
Plasma methionine depletion and pharmacokinetic properties in mice of methionine gamma-lyase from Citrobacter freundii, Clostridium tetani and Clostridium sporogenes
Biomed. Pharmacother.
88
978-984
2017
Clostridium tetani (A0A1L7H888), Clostridium tetani, Clostridium sporogenes (J7TA22), Clostridium sporogenes, Citrobacter freundii (Q84AR1), Citrobacter freundii, Clostridium sporogenes ATCC 15579 (J7TA22)
Kuznetsov, N.A.; Faleev, N.G.; Kuznetsova, A.A.; Morozova, E.A.; Revtovich, S.V.; Anufrieva, N.V.; Nikulin, A.D.; Fedorova, O.S.; Demidkina, T.V.
Pre-steady-state kinetic and structural analysis of interaction of methionine gamma-lyase from Citrobacter freundii with inhibitors
J. Biol. Chem.
290
671-681
2015
Citrobacter freundii (Q84AR1), Citrobacter freundii
Morozova, E.A.; Kulikova, V.V.; Faggiano, S.; Raboni, S.; Gabellieri, E.; Cioni, P.; Anufrieva, N.V.; Revtovich, S.V.; Demidkina, T.; Mozzarelli, A.
Soluble and nanoporous silica gel-entrapped C. freundii methionine gamma-lyase
J. Nanosci. Nanotechnol.
18
2210-2219
2018
Citrobacter freundii (Q84AR1)
Lin, B.; Tian, G.; Liu, Y.
Mechanistic insights into the gamma-elimination reaction of L-methionine catalyzed by methionine gamma-lyase (MGL)
Theoret. Chem. Accounts
136
105
2017
Clostridium sporogenes (J7TA22), Citrobacter freundii (Q84AR1), Clostridium sporogenes ATCC 15579 (J7TA22)
-
EXTERNAL LINKS (specific for EC-Number 4.4.1.11)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
