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Information on EC 4.4.1.11 - methionine gamma-lyase and Organism(s) Fusobacterium nucleatum and UniProt Accession Q8RDT4

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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This record set is specific for:
Fusobacterium nucleatum
UNIPROT: Q8RDT4
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Word Map
The taxonomic range for the selected organisms is: Fusobacterium nucleatum
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
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L-methionine gamma-lyase
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L-methionine-alpha-deamino-gamma-mercaptomethane-lyase
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L-methionine-gamma-lyase
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lyase, methionine
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methioninase
methionine dethiomethylase
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methionine gamma-lyase
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
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SUBSTRATE
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
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
myrsinoic acid B
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000389 - 0.0105
myrsinoic acid B
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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utilization for the treatment of cancers
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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