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Information on EC 4.4.1.11 - methionine gamma-lyase and Organism(s) Trichomonas vaginalis and UniProt Accession O15565

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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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Trichomonas vaginalis
UNIPROT: O15565
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The taxonomic range for the selected organisms is: Trichomonas vaginalis
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
methionine gamma-lyase
-
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-homocysteic acid + H2O
?
show the reaction diagram
-
-
-
-
?
DL-homocysteine + H2O
?
show the reaction diagram
-
-
-
-
?
L-cysteine + H2O
?
show the reaction diagram
-
-
-
-
?
L-ethionine + H2O
?
show the reaction diagram
-
-
-
-
?
L-methionine + H2O
?
show the reaction diagram
-
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-selenomethionine + H2O
?
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
-
-
-
?
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
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
5-5'-dithiobis-(2-nitrobenzoic acid)
-
-
aminoethyloxyvinylglycine
-
-
cycloserine
-
-
DL-Penicillamine
-
-
DL-propargylglycine
-
-
hydroxylamine
-
-
iodacetamide
-
-
iodoacetamide
-
-
L-Cycloserine
-
-
p-chloromercuri-benzoic acid
-
-
p-chloromercuribenzoate
-
-
Penicillamine
-
-
propargylglycine
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.6 - 22.3
cysteine
0.5
DL-homocysteine
-
-
3.6
L-cysteine
-
-
0.5 - 37.2
L-ethionine
4.3
L-methionine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
value is 3.17 U/mg protein
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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?
O15565_TRIVA
398
0
43112
TrEMBL
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
160000
-
gel filtration
44000
-
4 * 44000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor-diffusion method
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C113G
-
MGL1, reduced activity towards methionine and homocysteine
C116G
-
MGL2, reduced activity towards methionine and homocysteine
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
-
-
701880
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ion exchange and gel filtration chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
utilization for the treatment of cancers
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lockwood, B.C.; Coombs, G.H.
Purification and characterization of methionine gamma-lyase from Trichomonas vaginalis
Biochem. J.
279
675-682
1991
Trichomonas vaginalis
Manually annotated by BRENDA team
McKie, A.E.; Edlind, T.; Walker, J.; Mottram, J.C.; Coombs, G.H.
The primitive protozoon Trichomonas vaginalis contains two methionine gamma-lyase genes that encode members of the gamma-family of pyridoxal 5 -phosphate-dependent enzymes
J. Biol. Chem.
273
5549-5556
1998
Trichomonas vaginalis
Manually annotated by BRENDA team
Spallholz, J.E.; Palace, V.P.; Reid, T.W.
Methioninase and selenomethionine but not Se-methylselenocysteine generate methylselenol and superoxide in an in vitro chemiluminescent assay: implications for the nutritional carcinostatic activity of selenoamino acids
Biochem. Pharmacol.
67
547-554
2004
Trichomonas vaginalis
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.; 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