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 |
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 |
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 | - |
? |
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 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.1.1.277 | - |
Zea mays |
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 | - |
? |
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 |
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 |
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 |
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 |