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Literature summary for 2.1.1.277 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)

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

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Zea mays
-
-
-
Zea mays B6SU46
-
-
Zea mays D9J100
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Zea mays

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + anthranilate
-
Zea mays S-adenosyl-L-homocysteine + O-methyl anthranilate
-
?
S-adenosyl-L-methionine + anthranilate no activity with benzoate, isoenzyme AAMT1 Zea mays S-adenosyl-L-homocysteine + O-methyl anthranilate
-
?
S-adenosyl-L-methionine + anthranilate no activity with benzoate, isoenzyme AAMT2 Zea mays S-adenosyl-L-homocysteine + O-methyl anthranilate
-
?
S-adenosyl-L-methionine + benzoate 26% of the activity with anthanilate, isoenzyme AAMT3 Zea mays S-adenosyl-L-homocysteine + methyl benzoate
-
?

Synonyms

Synonyms Comment Organism
AAMT
-
Zea mays
AAMT1
-
Zea mays
AAMT2
-
Zea mays
AAMT3
-
Zea mays

Turnover Number [1/s]

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

General Information

General Information Comment Organism
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]

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