Information on EC 2.1.1.111 - anthranilate N-methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.111
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RECOMMENDED NAME
GeneOntology No.
anthranilate N-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + anthranilate = S-adenosyl-L-homocysteine + N-methylanthranilate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acridone alkaloid biosynthesis
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Acridone alkaloid biosynthesis
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Biosynthesis of secondary metabolites
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N-methylanthraniloyl-beta-D-glucopyranose biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:anthranilate N-methyltransferase
Involved in the biosynthesis of acridine alkaloids in plant tissues.
CAS REGISTRY NUMBER
COMMENTARY hide
123779-15-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + N-methylanthranilate
show the reaction diagram
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
S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + N-methylanthranilate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
73% relative enzyme activity in presence of 1.5 mM, significantly reduced
Co2+
activity reduced in presence of 1.5 mM, 25% relative activity retained
Cu2+
activity abolished in presence of 1.5 mM of
Fe2+
activity nearly abolished in presence of 1.5 mM of
Fe3+
activity abolished in presence of 1.5 mM of
Mg2+
activity independent in presence of 1.5 mM of, 90% relative activity retained
Zn2+
activity abolished in presence of 1.5 mM of
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007 - 0.024
anthranilate
0.003
S-adenosyl-L-methionine
N298E mutant; wild-type
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
activity optimum at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
lining the inside of
Manually annotated by BRENDA team
crude extracts of total plants, elicited, 2 years old
Manually annotated by BRENDA team
high mRNA expression and enzyme activity
Manually annotated by BRENDA team
moderate mRNA expression
Manually annotated by BRENDA team
central vascular bundles of, around cup-like structures in the outer ovary wall representing secretory oil glands
Manually annotated by BRENDA team
vascular region of secondary and primary shoots, moderate mRNA expression, high enzyme activity
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62000
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1 * 62000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 62000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gel filtration, SDS-PAGE, wild-type and mutant protein
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli, BL21 cells for induction of recombinant protein expression
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N298E
generated by site-directed mutagenesis