Information on EC 6.3.4.12 - glutamate-methylamine ligase

Word Map on EC 6.3.4.12
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
6.3.4.12
-
RECOMMENDED NAME
GeneOntology No.
glutamate-methylamine ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-glutamate + methylamine = ADP + phosphate + N5-methyl-L-glutamine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amination
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
methylamine degradation II
-
-
SYSTEMATIC NAME
IUBMB Comments
L-glutamate:methylamine ligase (ADP-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
37318-69-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain FAM5, gene gms
D7R618
UniProt
Manually annotated by BRENDA team
strain FAM5, gene gms
D7R618
UniProt
Manually annotated by BRENDA team
strain No. 9
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-Glu + methylamine
?
show the reaction diagram
-
-
-
-
-
ATP + L-Glu + methylamine
ADP + phosphate + N5-methyl-L-glutamine
show the reaction diagram
ATP + L-glutamate + ethylamine
ADP + phosphate + N5-ethyl-L-glutamine
show the reaction diagram
ATP + L-glutamate + hydroxylamine
ADP + phosphate + N5-hydroxy-L-glutamine
show the reaction diagram
-
30-40% activity of the activity with methylamine for the native and recombinant enzymes
-
-
?
ATP + L-glutamate + methylamine
ADP + phosphate + N5-methyl-L-glutamine
show the reaction diagram
L-glutamic acid + ethylamine
theanine
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-Glu + methylamine
?
show the reaction diagram
-
-
-
-
-
ATP + L-glutamate + ethylamine
ADP + phosphate + N5-ethyl-L-glutamine
show the reaction diagram
ATP + L-glutamate + methylamine
ADP + phosphate + N5-methyl-L-glutamine
show the reaction diagram
L-glutamic acid + ethylamine
theanine
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
ethylamine inhibits yeast sugar fermentation and recombinant theanine production in vivo in a coupled theanine-foorming reaction with Saccharomyces cerevisiae, which can be overcome by potassium phosphate addition, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.022 - 0.205
D7R618
different wild-type and mutant strains
8
-
purified recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
7.5 - 8
-
recombinant and native enzymes
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
40
-
recombinant enzyme
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
freeze-dried cells
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48820
D7R618
x * 48820, sequence calcualtion
49000
-
x * 49000, about, sequence calculation, x * 50000, recombinnat enzyme, SDS-PAGE
50000
-
x * 49000, about, sequence calculation, x * 50000, recombinnat enzyme, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
the native as well as the recombinant enzyme is most stable at pH 6.0
691366
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partially by ammonium sulfate fractionation
D7R618
recombinant enzyme from Escherichia coli strain AD494(DE3) by ammonium sulfate fractionation and anion exchange chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning from a genomic DNA library, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain AD494(DE3), subcloning in Escherichia coli strain JM109
-
expression in Escherichia coli strain AD494(DE3)
-
gene gms, gsIII-like gene, DNA and amino acid sequence determination and analysis, genetic structure
D7R618
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gamma-glutamylmethylamide synthetase is induced during growth on methylated amines
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
assay for the enzymatic synthesis of gamma-glutamylmethylamide
synthesis