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Information on EC 4.4.1.11 - methionine gamma-lyase and Organism(s) Streptomyces avermitilis and UniProt Accession Q826W3

for references in articles please use BRENDA:EC4.4.1.11
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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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Streptomyces avermitilis
UNIPROT: Q826W3
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The taxonomic range for the selected organisms is: Streptomyces avermitilis
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
L-methioninase
-
-
-
-
L-methionine gamma-lyase
-
-
-
-
L-methionine-alpha-deamino-gamma-mercaptomethane-lyase
-
-
-
-
lyase, methionine
-
-
-
-
methioninase
-
-
-
-
methionine dethiomethylase
-
-
-
-
methionine gamma-lyase
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-
-
-
methionine lyase
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-
-
-
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-homocysteine + H2O
sulfide + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2
L-cysteine
pH 8.0, 37°C
1.78
L-homocysteine
pH 8.0, 37°C
1.6
L-methionine
pH 8.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
L-cysteine
pH 8.0, 37°C
1.7
L-homocysteine
pH 8.0, 37°C
2.9
L-methionine
pH 8.0, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
L-cysteine
pH 8.0, 37°C
0.94
L-homocysteine
pH 8.0, 37°C
1.81
L-methionine
pH 8.0, 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 42994, calculated from sequence
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kudou, D.; Yasuda, E.; Hirai, Y.; Tamura, T.; Inagaki, K.
Molecular cloning and characterization of L-methionine gamma-lyase from Streptomyces avermitilis
J. Biosci. Bioeng.
120
380-383
2015
Streptomyces avermitilis (Q826W3), Streptomyces avermitilis, Streptomyces avermitilis DSM 46492 (Q826W3)
Manually annotated by BRENDA team