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Information on EC 4.4.1.11 - methionine gamma-lyase and Organism(s) Porphyromonas gingivalis and UniProt Accession Q7MX71

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EC Tree
IUBMB Comments
A pyridoxal-phosphate protein. The enzyme cleaves a carbon-sulfur bond, releasing methanethiol and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form 2-oxobutanoate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. The enzyme is involved in L-methionine catabolism.
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This record set is specific for:
Porphyromonas gingivalis
UNIPROT: Q7MX71
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The taxonomic range for the selected organisms is: Porphyromonas gingivalis
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-methioninase
-
-
-
-
L-methionine gamma-lyase
-
-
-
-
L-methionine-alpha-deamino-gamma-mercaptomethane lyase
-
-
L-methionine-alpha-deamino-gamma-mercaptomethane-lyase
L-methionine-gamma-lyase
-
-
lyase, methionine
-
-
-
-
methioninase
methionine dethiomethylase
-
-
-
-
methionine gamma-lyase
methionine lyase
-
-
-
-
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 hide
42616-25-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-cysteine + H2O
sulfide + NH3 + pyruvate
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 sulfone + H2O
? + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-methionine sulfoxide + H2O
?
show the reaction diagram
-
gamma-elimination reaction
-
-
?
S-benzyl-L-cysteine + H2O
?
show the reaction diagram
-
beta-elimination reaction
-
-
?
S-ethyl-L-cysteine + H2O
?
show the reaction diagram
-
beta-elimination reaction
-
-
?
S-ethyl-L-homocysteine + H2O
?
show the reaction diagram
-
gamma-elimination reaction
-
-
?
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) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
myrsinoic acid B
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.63
L-cysteine
pH 7.6, 37°C
1.2 - 1.77
L-methionine
38
L-methionine sulfone
pH 7.5, 37°C
12.22
L-methionine sulfoxide
-
pH 8.0, 30°C, recombinant enzyme
1.47
S-Benzyl-L-cysteine
-
pH 8.0, 30°C, recombinant enzyme
2.17
S-ethyl-L-cysteine
-
pH 8.0, 30°C, recombinant enzyme
0.93
S-ethyl-L-homocysteine
-
pH 8.0, 30°C, recombinant enzyme
additional information
additional information
-
steady-state kinetics for beta- and gamma-elimination reactions, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.86
L-cysteine
pH 7.6, 37°C
3.9 - 5.47
L-methionine
34.13
L-methionine sulfone
pH 7.5, 37°C
5.05
L-methionine sulfoxide
-
pH 8.0, 30°C, recombinant enzyme
5.8
S-Benzyl-L-cysteine
-
pH 8.0, 30°C, recombinant enzyme
8.05
S-ethyl-L-cysteine
-
pH 8.0, 30°C, recombinant enzyme
3.84
S-ethyl-L-homocysteine
-
pH 8.0, 30°C, recombinant enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.96
L-cysteine
pH 7.6, 37°C
2.2 - 4.55
L-methionine
0.9
L-methionine sulfone
pH 7.5, 37°C
0.413
L-methionine sulfoxide
-
pH 8.0, 30°C, recombinant enzyme
3.94
S-Benzyl-L-cysteine
-
pH 8.0, 30°C, recombinant enzyme
3.71
S-ethyl-L-cysteine
-
pH 8.0, 30°C, recombinant enzyme
4.13
S-ethyl-L-homocysteine
-
pH 8.0, 30°C, recombinant enzyme
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0824
myrsinoic acid B
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
purified His-tagged recombinant enzyme, pH 8.0, 30°C, substrate L-methionine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
2 * 43000, SDS-PAGE, 2 * 43300, calculated
43300
2 * 43000, SDS-PAGE, 2 * 43300, calculated
81400
gel filtration
170000
-
about, recombinant detagged enzyme, gel filtration
44080
-
4 * 44080, His-tagged enzyme, sequence calcualtion
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 43000, SDS-PAGE, 2 * 43300, calculated
tetramer
-
4 * 44080, His-tagged enzyme, sequence calcualtion
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of mgl gene
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expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
assay for methionine gamma-lyase-catalyzed gamma-elimination reactions of L-methionine and its analogues with 2-oxobutanoate as product. The assay employs UV-Vis spectrophotometry to continuously monitor the rate of formation of 2-oxobutanoate by its absorbance at 315 nm
medicine
-
utilization for the treatment of cancers
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yoshimura, M.; Nakano, Y.; Koga, T.
L-Methionine-gamma-lyase, as a target to inhibit malodorous bacterial growth by trifluoromethionine
Biochem. Biophys. Res. Commun.
292
964-968
2002
Porphyromonas gingivalis
Manually annotated by BRENDA team
Fukamachi, H.; Nakano, Y.; Okano, S.; Shibata, Y.; Abiko, Y.; Yamashita, Y.
High production of methyl mercaptan by L-methionine-alpha-deamino-gamma-mercaptomethane lyase from Treponema denticola
Biochem. Biophys. Res. Commun.
331
127-131
2005
Porphyromonas gingivalis, Treponema denticola
Manually annotated by BRENDA team
Ito, S.; Narise, A.; Shimura, S.
Identification of a methioninase inhibitor, myrsinoic acid B, from Myrsine seguinii Lev., and its inhibitory activities
Biosci. Biotechnol. Biochem.
72
2411-2414
2008
Fusobacterium nucleatum, Fusobacterium nucleatum JCM 8532, Porphyromonas gingivalis, Porphyromonas gingivalis W83, Treponema denticola, Treponema denticola ATCC 35405
Manually annotated by BRENDA team
Sato, D.; Nozaki, T.
Methionine gamma-lyase: the unique reaction mechanism, physiological roles, and therapeutic applications against infectious diseases and cancers
IUBMB Life
61
1019-1028
2009
Arabidopsis thaliana, Porphyromonas gingivalis, Brevibacterium linens, Entamoeba histolytica, Fusobacterium nucleatum, Prevotella denticola, Pseudomonas putida, Trichomonas vaginalis (O15564), Trichomonas vaginalis (O15565)
Manually annotated by BRENDA team
Suwabe, K.; Yoshida, Y.; Nagano, K.; Yoshimura, F.
Identification of an L-methionine gamma-lyase involved in the production of hydrogen sulfide from L-cysteine in Fusobacterium nucleatum subsp. nucleatum ATCC 25586
Microbiology
157
2992-3000
2011
Treponema denticola (Q73KL7), Porphyromonas gingivalis (Q7MX71), Fusobacterium nucleatum subsp. nucleatum (Q8RDT4), Porphyromonas gingivalis W83 (Q7MX71), Treponema denticola ATCC 35405 (Q73KL7), Fusobacterium nucleatum subsp. nucleatum ATCC 25586 / JCM14847 (Q8RDT4)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Foo, T.C.; Terentis, A.C.; Venkatachalam, K.V.
A continuous spectrophotometric assay and nonlinear kinetic analysis of methionine gamma-lyase catalysis
Anal. Biochem.
507
21-26
2016
Porphyromonas gingivalis (C3VMV9), Porphyromonas gingivalis
Manually annotated by BRENDA team
Stephen, A.; Millhouse, E.; Sherry, L.; Aduse-Opoku, J.; Culshaw, S.; Ramage, G.; Bradshaw, D.; Burnett, G.; Allaker, R.
In vitro effect of Porphyromonas gingivalis methionine gamma lyase on biofilm composition and oral inflammatory response
PLoS ONE
11
e0169157
2016
Porphyromonas gingivalis
Manually annotated by BRENDA team