EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.1.1.B126 | more |
recombinant MBMT protein expressed in Escherichia coli shows the highest substrate preference toward 4-methoxybenzoic acid. EjMT1 shows high activity with 3-methoxybenzoic acid and vanillic acid. The activity of EjMBMT with benzoic acid, 2-methoxybenzoic acid, anthranilic acid, and jasmonic acid is approximately half of that with p-methoxybenzoic acid. Enzyme EjMBMT displays negligible activity to salicylic acid, shikimic acid, and caffeic acid, no activity with indole-3-acetic acid and cinnamic acid. The enzyme is relatively specific for methoxybenzoic acids and the methoxy group on a benzene ring might be important for either enzyme binding or methyl group transfer from SAM by EjMBMT |
Rhaphiolepis bibas |
? |
- |
- |
2.1.1.B126 | S-adenosyl-L-methionine + 2-methoxybenzoate |
low activity |
Rhaphiolepis bibas |
methyl 2-methoxybenzoate + S-adenosyl-L-homocysteine |
- |
? |
2.1.1.B126 | S-adenosyl-L-methionine + 3-methoxybenzoate |
high activity |
Rhaphiolepis bibas |
methyl 3-methoxybenzoate + S-adenosyl-L-homocysteine |
- |
? |
2.1.1.B126 | S-adenosyl-L-methionine + 4-methoxybenzoate |
- |
Rhaphiolepis bibas |
methyl 4-methoxybenzoate + S-adenosyl-L-homocysteine |
- |
? |
2.1.1.B126 | S-adenosyl-L-methionine + 4-methoxybenzoate |
best substrate |
Rhaphiolepis bibas |
methyl 4-methoxybenzoate + S-adenosyl-L-homocysteine |
- |
? |
2.1.1.B126 | S-adenosyl-L-methionine + anthranilate |
low activity |
Rhaphiolepis bibas |
methyl anthranilate + S-adenosyl-L-homocysteine |
- |
? |
2.1.1.B126 | S-adenosyl-L-methionine + jasmonate |
low activity |
Rhaphiolepis bibas |
methyl jasmonate + S-adenosyl-L-homocysteine |
- |
? |
2.1.1.B126 | S-adenosyl-L-methionine + vanillate |
- |
Rhaphiolepis bibas |
methyl vanillate + S-adenosyl-L-homocysteine |
- |
? |