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Information on EC 4.4.1.11 - methionine gamma-lyase and Organism(s) Entamoeba histolytica and UniProt Accession Q86D28

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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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Entamoeba histolytica
UNIPROT: Q86D28
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The taxonomic range for the selected organisms is: Entamoeba histolytica
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-methionine-alpha-deamino-gamma-mercaptomethane-lyase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
EhMGL1
methionine gamma-lyase isoenzyme 1
L-methionine gamma-lyase 1
-
EhMGL2
L-methioninase
L-methionine gamma-lyase
-
-
-
-
L-methionine-alpha-deamino-gamma-mercaptomethane-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
DL-homocysteine + H2O
2-oxobutanoate + NH3 + H2S
show the reaction diagram
DL-homocysteine + H2O
hydrogen sulfide + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
O-acetyl-L-serine + H2O
2-oxopropanoate + NH3 + acetate
show the reaction diagram
trifluoromethionine + H2O
trifluoromethanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
DL-homocysteine + H2O
?
show the reaction diagram
-
-
-
-
?
DL-homocysteine + H2O
hydrogen sulfide + NH3 + 2-oxobutanoate
show the reaction diagram
L-cysteine + H2O
?
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
sulfide + NH3 + pyruvate
show the reaction diagram
-
-
-
?
L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
O-acetyl-L-serine + H2O
2-oxopropanoate + NH3 + acetate
show the reaction diagram
-
-
-
?
trifluoromethionine + H2O
?
show the reaction diagram
-
-
-
-
?
trifluoromethionine + H2O
trifluoromethanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
additional information
?
-
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
-
pyridoxal 5'-phosphate
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
DL-propargylglycine
irreversible slow-binding inhibition
aminoethyloxyvinylglycine
-
-
DL-propargylglycine
-
propargylglycine
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.03
DL-homocysteine
wild-type ehMGL1, pH 7.0, 37°C
0.34 - 1.01
L-cysteine
0.19 - 0.72
L-methionine
6.28
O-acetyl-L-serine
wild-type ehMGL1, pH 7.0, 37°C
0.1 - 0.83
trifluoromethionine
1.47 - 3.4
DL-homocysteine
0.64 - 1.7
L-cysteine
0.61 - 15.12
L-methionine
52.33
O-acetyl-L-serine
wild-type ehMGL2, pH 7.0, 37°C
0.1 - 5.45
trifluoromethionine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.13 - 3.91
DL-homocysteine
0.67 - 1.59
L-cysteine
0.36 - 1.82
L-methionine
1.74
O-acetyl-L-serine
wild-type ehMGL1, pH 7.0, 37°C
0.81 - 2.22
trifluoromethionine
0.057 - 10.56
DL-homocysteine
0.8 - 1.59
L-cysteine
0.47 - 1.82
L-methionine
6.22
O-acetyl-L-serine
wild-type ehMGL2, pH 7.0, 37°C
0.24 - 17.46
trifluoromethionine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.035
DL-propargylglycine
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.36
recombinant EhMGL1
0.44
recombinant EhMGL2
additional information
-
value is 0.44 U/mg protein
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6 - 8.2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
two-dimensional PAGE, native EhMGL1
5.9
two-dimensional PAGE, recombinant EhMGL1
6.5
two-dimensional PAGE, recombinant EhMGL2
6.7
two-dimensional PAGE, native EhMGL2
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q86D28_ENTHI
389
0
42272
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
171000 - 177000
43300
4 * 43300, SDS-PAGE, immunoblot, native and recombinant EhMGL1 form homotetramers
43700
4 * 43700, SDS-PAGE, immunoblot, native and recombinant EhMGL2 form homotetramers
43000
-
4 * 43000, SDS-PAGE
43100
x * 43100, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
?
x * 43100, calculated
tetramer
-
4 * 43000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
hanging-drop vapor-diffusion method
-
space group P212121
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C110G
decrease in kcat values for both L-methionine and L-cysteine
C110S
slightly reduced catalytic activites
R55A
decrease in catalytic activity
Y108F
almost 100% reduction in alpha-gamma-elimination of both L-methionine and homocysteine
C113G
20% increase in activity with L-methionine
C113S
reduced catalytic activites
R58A
complete loss of activity
Y111F
about 80% reduction in alpha-gamma-elimination of both L-methionine and homocysteine
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6 - 8.2
-
-
701880
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
GSTrap HP column chromatography and Sephacryl S-300 gel filtration
ion exchange and gel filtration chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 Star (DE3) cells
expression in Escherichia coli
expression of EhMGL1 in Escherichia coli
expression of EhMGL2 in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tokoro, M.; Asai, T.; Kobayashi, S.; Takeuchi, T.; Nozaki, T.
Identification and characterization of two isoenzymes of methionine gamma-lyase from Entamoeba histolytica: a key enzyme of sulfur-amino acid degradation in an anaerobic parasitic protist that lacks forward and reverse trans-sulfuration pathways
J. Biol. Chem.
278
42717-42727
2003
Entamoeba histolytica (Q86D27), Entamoeba histolytica (Q86D28), Entamoeba histolytica
Manually annotated by BRENDA team
Sato, D.; Yamagata, W.; Kamei, K.; Nozaki, T.; Harada, S.
Expression, purification and crystallization of L-methionine gamma -lyase 2 from Entamoeba histolytica
Acta Crystallogr. Sect. F
F62
1034-1036
2006
Entamoeba histolytica (Q86D27), Entamoeba histolytica
Manually annotated by BRENDA team
Sato, D.; Yamagata, W.; Harada, S.; Nozaki, T.
Kinetic characterization of methionine gamma-lyases from the enteric protozoan parasite Entamoeba histolytica against physiological substrates and trifluoromethionine, a promising lead compound against amoebiasis
FEBS J.
275
548-560
2008
Entamoeba histolytica (Q86D27), Entamoeba histolytica (Q86D28), Entamoeba histolytica
Manually annotated by BRENDA team
Sato, D.; Karaki, T.; Shimizu, A.; Kamei, K.; Harada, S.; Nozaki, T.
Crystallization and preliminary X-ray analysis of L-methionine gamma-lyase 1 from Entamoeba histolytica
Acta Crystallogr. Sect. F
64
697-699
2008
Entamoeba histolytica (Q86D28), Entamoeba histolytica
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Sato, D.; Kobayashi, S.; Yasui, H.; Shibata, N.; Toru, T.; Yamamoto, M.; Tokoro, G.; Ali, V.; Soga, T.; Takeuchi, T.; Suematsu, M.; Nozaki, T.
Cytotoxic effect of amide derivatives of trifluoromethionine against the enteric protozoan parasite Entamoeba histolytica
Int. J. Antimicrob. Agents
35
56-61
2010
Entamoeba histolytica
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