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EC Tree
IUBMB Comments In the plant maize (Zea mays), the isoforms AAMT1 and AAMT2 are specific for anthranilate while AAMT3 also has the activity of EC 2.1.1.273, benzoate methyltransferase.
The expected taxonomic range for this enzyme is: Zea mays
Synonyms
AAMT,
AAMT1 , AAMT2, AAMT3, ANT methyltransferase1, anthranilic acid methyltransferase1,
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anthranilic acid methyltransferase1
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AAMT1
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-
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S-adenosyl-L-methionine + anthranilate = S-adenosyl-L-homocysteine + O-methyl anthranilate
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-
-
-
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S-adenosyl-L-methionine:anthranilate O-methyltransferase
In the plant maize (Zea mays), the isoforms AAMT1 and AAMT2 are specific for anthranilate while AAMT3 also has the activity of EC 2.1.1.273, benzoate methyltransferase.
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S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + O-methyl anthranilate
S-adenosyl-L-methionine + benzoate
S-adenosyl-L-homocysteine + methyl benzoate
26% of the activity with anthanilate, isoenzyme AAMT3
-
-
?
S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + O-methyl anthranilate
-
-
-
?
S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + O-methyl anthranilate
-
-
-
?
S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + O-methyl anthranilate
no activity with benzoate, isoenzyme AAMT1
-
-
?
S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + O-methyl anthranilate
no activity with benzoate, isoenzyme AAMT2
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-
?
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S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + O-methyl anthranilate
S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + O-methyl anthranilate
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-
-
?
S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + O-methyl anthranilate
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-
-
?
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S-adenosyl-L-methionine
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0.311 - 0.641
anthranilate
0.076 - 0.094
S-adenosyl-L-methionine
0.311
anthranilate
25°C, pH not specified in the publication, isoenzyme AAMT2
0.641
anthranilate
25°C, pH not specified in the publication, isoenzyme AAMT1
0.076
S-adenosyl-L-methionine
25°C, pH not specified in the publication, isoenzyme AAMT3
0.079
S-adenosyl-L-methionine
25°C, pH not specified in the publication, isoenzyme AAMT1
0.094
S-adenosyl-L-methionine
25°C, pH not specified in the publication, isoenzyme AAMT2
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0.37
anthranilate
25°C, pH not specified in the publication, isoenzyme AAMT2
0.45
anthranilate
25°C, pH not specified in the publication, isoenzyme AAMT1
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0.7
anthranilate
25°C, pH not specified in the publication, isoenzyme AAMT1
1.2
anthranilate
25°C, pH not specified in the publication, isoenzyme AAMT2
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brenda
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UniProt
brenda
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UniProt
brenda
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physiological function
isoenzyme AAMT1 is responsible for most of the S-adenosyl-L-methionine-dependent methyltransferase activity and methyl anthranilate formation observed in maize after herbivore damage
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AAMT1_MAIZE
382
0
43588
Swiss-Prot
other Location (Reliability: 1 )
AAMT2_MAIZE
374
0
42666
Swiss-Prot
other Location (Reliability: 2 )
AAMT3_MAIZE
379
0
43220
Swiss-Prot
other Location (Reliability: 2 )
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additional information
metabolic engineering of Escherichia coli and Corynebacterium glutamicum strains by expression of plant enzyme anthranilic acid methyltransferase1 (AAMT1). Optimizing the key enzyme anthranilic acid (ANT) methyltransferase1 (AAMT1) expression, increasing the direct precursor ANT supply, and enhancing the intracellular availability and salvage of the cofactor S-adenosyl-L-methionine required by AAMT1, results in improved methyl anthranilate (MANT) production in both engineered microorganisms. In situ two-phase extractive fermentation using tributyrin as an extractant is developed to overcome MANT toxicity. Fed-batch cultures of the final engineered Escherichia coli and Corynebacterium glutamicum strains in two-phase cultivation mode lead to the production of 4.47 and 5.74 g/l MANT, respectively, in minimal media containing glucose. Metabolic network related to MANT biosynthesis from glucose in Escherichia coli and Corynebacterium glutamicum, as well as metabolic engineering strategies, methods, overview
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cloned and expressed with an N-terminal His tag in Escherichia coli
gene aamt1, recombinant expresion in Escherichia coli strain W3110 trpD9923 and Corynebacterium glutamicum strain ATCC 13032
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Köllner, T.G.; Lenk, C.; Zhao, N.; Seidl-Adams, I.; Gershenzon, J.; Chen, F.; Degenhardt, J.
Herbivore-induced SABATH methyltransferases of maize that methylate anthranilic acid using s-adenosyl-L-methionine
Plant Physiol.
153
1795-1807
2010
Zea mays, Zea mays (B6SU46), Zea mays (D9J100)
brenda
Luo, Z.W.; Cho, J.S.; Lee, S.Y.
Microbial production of methyl anthranilate, a grape flavor compound
Proc. Natl. Acad. Sci. USA
116
10749-10756
2019
Zea mays (D9J0Z7)
brenda
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2.1.1.277 anthranilate O-methyltransferase
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