Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | 5 mM, slight inhibitory effect, less than 10% inhibition | Antirrhinum majus | |
Cu2+ | 5 mM, strong inhibitory effect, 75100% inhibition | Antirrhinum majus | |
Fe2+ | 5 mM, strong inhibitory effect, 75100% inhibition | Antirrhinum majus | |
Mn2+ | 5 mM, slight inhibitory effect, less than 10% inhibition | Antirrhinum majus | |
Na+ | 5 mM, slight inhibitory effect, less than 10% inhibition | Antirrhinum majus | |
S-adenosyl-L-homocysteine | competitive inhibition with respect to S-adenosyl-L-methionine and noncompetitive inhibition with respect to benzoate | Antirrhinum majus | |
Zn2+ | 5 mM, slight inhibitory effect, less than 10% inhibition | Antirrhinum majus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.028 | - |
S-adenosyl-L-methionine | apparent Km-value of plant-purified protein, pH 7.5, 20°C | Antirrhinum majus | |
0.087 | - |
S-adenosyl-L-methionine | apparent Km-value of recombinant protein, pH 7.5, 20°C | Antirrhinum majus | |
1.1 | - |
benzoate | apparent Km-value of plant-purified protein, pH 7.5, 20°C | Antirrhinum majus | |
1.6 | - |
benzoate | apparent Km-value of recombinant protein, pH 7.5, 20°C | Antirrhinum majus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
K+ | 5 mM, stimulates BAMT activity by a factor of 2 | Antirrhinum majus | |
Mg2+ | BAMT activity not affected by the presence of 5 mM | Antirrhinum majus | |
NH4+ | 5 mM, stimulates BAMT activity by a factor of 2 | Antirrhinum majus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
41000 | - |
calculated molecular mass of the protein encoded by BAMT cDNA | Antirrhinum majus |
49000 | - |
denatured protein, SDSPAGE | Antirrhinum majus |
100000 | - |
native protein, gel filtration chromatography on Superdex 200-HR | Antirrhinum majus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
S-adenosyl-L-methionine + benzoate | Antirrhinum majus | - |
S-adenosyl-L-homocysteine + methyl benzoate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Antirrhinum majus | - |
snapdragon | - |
Purification (Comment) | Organism |
---|---|
enzyme purified from upper and lower petal lobes of 5- to 10-day-old snapdragon flowers using DE53 anion exchange chromatography, hydrophobic interaction chromatography using Phenyl-Sepharose 6FF, and Mono-Q chromatography | Antirrhinum majus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
S-adenosyl-L-methionine + benzoate = S-adenosyl-L-homocysteine + methyl benzoate | ordered bibi mechanism, derived from kinetic analysis, S-adenosyl-L-methionine appears to be the first substrate to bind to the enzyme and methyl benzoate would be the first to be released and S-adenosyl-L-homocysteine the last | Antirrhinum majus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
petal | enzyme is expressed in the upper and lower lobes of petals of snapdragon flowers | Antirrhinum majus | - |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.01962 | - |
purified BAMT protein, pH 7.5, 20°C | Antirrhinum majus |
Storage Stability | Organism |
---|---|
the purified proteins, both from petal tissue and from Escherichia coli, are highly stable for several months when stored at -80°C. When stored in a buffer containing 50 mM BisTrisHCl, pH 6.9, 10% glycerol, and 10 mM beta-mercaptoethanol at 4°C, BAMT protein is stable for 1 week | Antirrhinum majus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | no activity toward other naturally occurring substrates like salicylic acid, trans-cinnamic acid, and their derivatives 3-hydroxybenzoic acid, 4-hydroxybenzoic acid, benzyl alcohol, and 2-coumaric, 3-coumaric, and 4-coumaric acid | Antirrhinum majus | ? | - |
? | |
S-adenosyl-L-methionine + benzoate | - |
Antirrhinum majus | S-adenosyl-L-homocysteine + methyl benzoate | - |
? |
Subunits | Comment | Organism |
---|---|---|
homodimer | 2 * 49000 | Antirrhinum majus |
Synonyms | Comment | Organism |
---|---|---|
BAMT | - |
Antirrhinum majus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | - |
- |
Antirrhinum majus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | 65 | BAMT is 100% stable for 30 min at 20°C and 60% stable for 30 min at 30°C, it is 20% stable for 30 min at 42°C but after 30 min incubation at 65°C, it completely loses activity | Antirrhinum majus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
- |
Antirrhinum majus |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
the enzyme is active in both Tris- and phosphatecitrate-based buffers | Antirrhinum majus |
5.5 | 9.5 | with 65% of maximum activity at both pH 6.5 and 8.5 and at pH 5.5 and 9.5, the enzyme activity falls to about 50% of the optimal value | Antirrhinum majus |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.007 | - |
S-adenosyl-L-homocysteine | for S-adenosyl-L-methionine, pH 7.5, 20°C | Antirrhinum majus | |
0.014 | - |
S-adenosyl-L-homocysteine | for benzoate, pH 7.5, 20°C | Antirrhinum majus |