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Literature summary extracted from

  • 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 (2010), Plant Physiol., 153, 1795-1807.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.273 expressed with an N-terminal His tag in Escherichia coli Zea mays
2.1.1.277 cloned and expressed with an N-terminal His tag in Escherichia coli Zea mays

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.277 0.076
-
S-adenosyl-L-methionine 25°C, pH not specified in the publication, isoenzyme AAMT3 Zea mays
2.1.1.277 0.079
-
S-adenosyl-L-methionine 25°C, pH not specified in the publication, isoenzyme AAMT1 Zea mays
2.1.1.277 0.094
-
S-adenosyl-L-methionine 25°C, pH not specified in the publication, isoenzyme AAMT2 Zea mays
2.1.1.277 0.311
-
anthranilate 25°C, pH not specified in the publication, isoenzyme AAMT2 Zea mays
2.1.1.277 0.641
-
anthranilate 25°C, pH not specified in the publication, isoenzyme AAMT1 Zea mays

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.277 S-adenosyl-L-methionine + anthranilate Zea mays
-
S-adenosyl-L-homocysteine + O-methyl anthranilate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.273 Zea mays
-
cv. Delprim
-
2.1.1.277 Zea mays
-
-
-
2.1.1.277 Zea mays B6SU46
-
-
2.1.1.277 Zea mays D9J100
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.277
-
Zea mays

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.273 additional information no activity with anthranilic acid, salicylic acid, cinnamic acid, and coumaric acid Zea mays ?
-
?
2.1.1.273 S-adenosyl-L-methionine + benzoate
-
Zea mays S-adenosyl-L-homocysteine + methyl benzoate
-
?
2.1.1.277 S-adenosyl-L-methionine + anthranilate
-
Zea mays S-adenosyl-L-homocysteine + O-methyl anthranilate
-
?
2.1.1.277 S-adenosyl-L-methionine + anthranilate no activity with benzoate, isoenzyme AAMT1 Zea mays S-adenosyl-L-homocysteine + O-methyl anthranilate
-
?
2.1.1.277 S-adenosyl-L-methionine + anthranilate no activity with benzoate, isoenzyme AAMT2 Zea mays S-adenosyl-L-homocysteine + O-methyl anthranilate
-
?
2.1.1.277 S-adenosyl-L-methionine + benzoate 26% of the activity with anthanilate, isoenzyme AAMT3 Zea mays S-adenosyl-L-homocysteine + methyl benzoate
-
?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.273 OMT8
-
Zea mays
2.1.1.277 AAMT
-
Zea mays
2.1.1.277 AAMT1
-
Zea mays
2.1.1.277 AAMT2
-
Zea mays
2.1.1.277 AAMT3
-
Zea mays

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.1.277 0.37
-
anthranilate 25°C, pH not specified in the publication, isoenzyme AAMT2 Zea mays
2.1.1.277 0.45
-
anthranilate 25°C, pH not specified in the publication, isoenzyme AAMT1 Zea mays

General Information

EC Number General Information Comment Organism
2.1.1.277 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 Zea mays

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.1.1.277 0.7
-
anthranilate 25°C, pH not specified in the publication, isoenzyme AAMT1 Zea mays
2.1.1.277 1.2
-
anthranilate 25°C, pH not specified in the publication, isoenzyme AAMT2 Zea mays