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Information on EC 4.4.1.11 - methionine gamma-lyase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9SGU9
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4.4.1.11 methionine gamma-lyaseIUBMB 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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Word Map
- 4.4.1.11
- lipase
- monoacylglycerol
-
endocannabinoids
- cannabinoids
- lectin
- putida
-
c-type
- 2-arachidonoylglycerol
- pyridoxal
- medicine
- monoglyceride
-
orthotopic
-
galactose-type
- galnac
- selenomethionine
- anandamide
- freundii
-
2-arachidonoyl
-
citrobacter
- alpha-ketobutyrate
- methylselenol
-
meibomian
-
methionine-dependent
- mercaptan
-
beta-lyase
-
5'-phosphate-dependent
-
dc-sign
-
s-substituted
- synthesis
- nutrition
- environmental protection
- analysis
- drug development
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-methioninase
-
-
-
-
L-methionine gamma-lyase
-
-
-
-
L-methionine-alpha-deamino-gamma-mercaptomethane-lyase
-
-
-
-
lyase, methionine
-
-
-
-
methioninase
-
-
-
-
methionine dethiomethylase
-
-
-
-
methionine gamma-lyase
methionine lyase
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-
-
-
methionine gamma-lyase
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-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -
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
42616-25-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
part of the methanethiol produced can react with an activated form of serine to produce S-methylcysteine. Product 2-oxobutanoate enters the papthway of Ile synthesis in plastids, part of the methanethiol produced can react with an activated form of serine to produce S-methylcysteine
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-methionine + H2O
methanethiol + NH3 + 2-oxobutanoate
-
-
part of the methanethiol produced can react with an activated form of serine to produce S-methylcysteine. Product 2-oxobutanoate enters the papthway of Ile synthesis in plastids
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
isoleucine biosynthesis, sulfur storage, involved in the alternative reverse-transsulfuration pathway, important roe in the resumption process
physiological function
-
under drought conditions and in reproductive tissue enzyme might play significant role as an alternate route to fulfill increased demand for isoleucine
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MGL_ARATH
441
0
47821
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
overexpression in Escherichia coli allows growth on L-methionine as sole nitrogen source and confers a high rate of methanethiol emission. Knock-out of gene significantly increases leaf methionine content and leaf and root S-methylmethionine content in Arabidopsis plants
additional information
-
knockout mutations, increase of S-methylmethionine and methionine accumulation in leaves under sulfate-limiting growth conditions, increase of free methionine in flowers and seeds under normal growth conditions
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
about 50fold induction of enzyme expression in seedlings defective in isocitrate lyase
-
transcription is strongly regulated by exogenous methionine, low sulfate, osmotic stress and availability of threonine or isoleucine
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
environmental protection
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enzyme is not an important source of volatile methanethiol
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Goyer, A.; Collakova, E.; Shachar-Hill, Y.; Hanson, A.D.
Functional characterization of a methionine gamma-lyase in Arabidopsis and its implication in an alternative to the reverse trans-sulfuration pathway
Plant Cell Physiol.
48
232-242
2007
Arabidopsis thaliana
Rebeille, F.; Jabrin, S.; Bligny, R.; Loizeau, K.; Gambonnet, B.; Van Wilder, V.; Douce, R.; Ravanel, S.
Methionine catabolism in Arabidopsis cells is initiated by a gamma-cleavage process and leads to S-methylcysteine and isoleucine syntheses
Proc. Natl. Acad. Sci. USA
103
15687-15692
2006
Arabidopsis thaliana
Joshi, V.; Joung, J.G.; Fei, Z.; Jander, G.
Interdependence of threonine, methionine and isoleucine metabolism in plants: accumulation and transcriptional regulation under abiotic stress
Amino Acids
39
933-947
2010
Arabidopsis thaliana
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)
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