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Information on EC 2.1.1.277 - anthranilate O-methyltransferase and Organism(s) Zea mays and UniProt Accession D9J100

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.277 anthranilate O-methyltransferase
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.
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This record set is specific for:
Zea mays
UNIPROT: D9J100
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The taxonomic range for the selected organisms is: Zea mays
The expected taxonomic range for this enzyme is: Zea mays
Synonyms
aamt1, anthranilic acid methyltransferase1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
AAMT1
ANT methyltransferase1
-
anthranilic acid methyltransferase1
-
SYSTEMATIC NAME
IUBMB Comments
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.
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 + O-methyl anthranilate
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + benzoate
S-adenosyl-L-homocysteine + methyl benzoate
show the reaction diagram
26% of the activity with anthanilate, isoenzyme AAMT3
-
-
?
S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + O-methyl anthranilate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL 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 + O-methyl anthranilate
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + anthranilate
S-adenosyl-L-homocysteine + O-methyl anthranilate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.076
S-adenosyl-L-methionine
25°C, pH not specified in the publication, isoenzyme AAMT3
0.311 - 0.641
anthranilate
0.079 - 0.094
S-adenosyl-L-methionine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.37 - 0.45
anthranilate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7 - 1.2
anthranilate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AAMT3_MAIZE
379
0
43220
Swiss-Prot
other Location (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned and expressed with an N-terminal His tag in Escherichia coli
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kllner, 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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team