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Information on EC 2.1.1.111 - anthranilate N-methyltransferase for references in articles please use BRENDA:EC2.1.1.111
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EC Tree
IUBMB Comments Involved in the biosynthesis of acridine alkaloids in plant tissues.
The enzyme appears in viruses and cellular organisms
Synonyms
ANMT, anthranilic acid N-methyltransferase,
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anthranilic acid N-methyltransferase
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S-adenosyl-L-methionine + anthranilate = S-adenosyl-L-homocysteine + N-methylanthranilate
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methyl group transfer
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S-adenosyl-L-methionine:anthranilate N-methyltransferase
Involved in the biosynthesis of acridine alkaloids in plant tissues.
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S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + N-methylanthranilate
S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + N-methylanthranilate
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?
S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + N-methylanthranilate
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first specific step in quinoline alkaloid biosynthesis
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S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + N-methylanthranilate
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S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + N-methylanthranilate
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first specific step in acridone alkaloid biosynthesis
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S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + N-methylanthranilate
first specific step in acridone alkaloid biosynthesis
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S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + N-methylanthranilate
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first specific step in quinoline alkaloid biosynthesis
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S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + N-methylanthranilate
first specific step in alkaloid biosynthesis, substrate specificity determines the course of acridone biosynthesis
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S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + N-methylanthranilate
S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + N-methylanthranilate
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first specific step in quinoline alkaloid biosynthesis
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S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + N-methylanthranilate
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first specific step in acridone alkaloid biosynthesis
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S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + N-methylanthranilate
A9X7L0
first specific step in acridone alkaloid biosynthesis
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S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + N-methylanthranilate
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first specific step in quinoline alkaloid biosynthesis
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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
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0.007 - 0.024
anthranilate
0.003
S-adenosyl-L-methionine
N298E mutant; wild-type
0.007
anthranilate
wild-type
0.024
anthranilate
N298E mutant
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additional information
in-gel digestion and peptide sequencing by mass spectrometry, Western Blot and phylogenetic analysis, assays conducted at 32°C in 73.5 mM glycine-NaOH buffer at pH 8.9, HPLC separation of assay extracts, list of compounds that are not accepted as substrate in assay
additional information
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in-gel digestion and peptide sequencing by mass spectrometry, Western Blot and phylogenetic analysis, assays conducted at 32°C in 73.5 mM glycine-NaOH buffer at pH 8.9, HPLC separation of assay extracts, list of compounds that are not accepted as substrate in assay
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8.2
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assay at
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32
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assay at
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line R-20
SwissProt
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lining the inside of
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crude extracts of total plants, elicited, 2 years old
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high mRNA expression and enzyme activity
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moderate mRNA expression
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central vascular bundles of, around cup-like structures in the outer ovary wall representing secretory oil glands
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vascular region of secondary and primary shoots, moderate mRNA expression, high enzyme activity
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rhizodermis of older root parts, endodermis of younger root parts, high mRNA expression and enzyme activity
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ANMT_RUTGR
364
0
40059
Swiss-Prot
Q2HTB5_MEDTR
375
0
41406
TrEMBL
A0A396GSA2_MEDTR
125
0
14684
TrEMBL
A0A396HGZ5_MEDTR
176
0
20120
TrEMBL
M4HXR6_9POAL
354
0
38657
TrEMBL
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62000
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1 * 62000, SDS-PAGE
70000
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gel filtration
70000
gel filtration, SDS-PAGE
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monomer
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1 * 62000, SDS-PAGE
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N298E
generated by site-directed mutagenesis
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gel filtration, SDS-PAGE, wild-type and mutant protein
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expressed in Escherichia coli, BL21 cells for induction of recombinant protein expression
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Eilert, U.; Wolters B.
Elicitor induction of S-adenosyl-L-methionine: anthranilic acid N-methyltransferase activity in cell suspension and organ cultures of Ruta graveolens L.
Plant Cell Tissue Organ Cult.
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1-18
1989
Ruta graveolens
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brenda
Baumert, A.; Creche, J.; Rideau, M.; Chenieux, J.C.; Groeger, D.
Anthranilic acid-specific enzymes in alkaloid-producing tissue cultures of Choisya ternata and Ruta graveolens
Plant Physiol. Biochem.
28
587-592
1990
Choisya ternata, Ruta graveolens
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Baumert, A.; Maier, W.; Schumann, B.; Gröger, D.
Increased accumulation of Acridone alkaloids by cell suspension cultures of Ruta graveolens in response to elicitors
J. Plant Physiol.
139
224-228
1991
Ruta graveolens
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brenda
Maier, W; Baumert, A.; Groeger, D.
Partial purification and characterization of S-adenosyl-L-methionine:anthranilic acid N-methyltransferase from Ruta cell suspension cultures
J. Plant Physiol.
145
1-6
1995
Ruta graveolens
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brenda
Rohde, B.; Hans, J.; Martens, S.; Baumert, A.; Hunziker, P.; Matern, U.
Anthranilate N-methyltransferase, a branch-point enzyme of acridone biosynthesis
Plant J.
53
541-553
2008
Ruta graveolens (A9X7L0), Ruta graveolens
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