SAM:benzoic acid carboxyl methyltransferase; converts benzoic acid to methyl benzoate (floral odor)
BBa_J45002 encodes SAM benzoic acid carboxyl methyltransferase I derived from BAMT from Antirrhinus majus (snapdragon). BAMT catalyzes the conversion of benzoic acid to methyl benzoate. Methyl benzoate has a floral smell.
Usage and Biology
- Enzyme is active as a dimer.
- There are two methionine codons at the begnning of the BAMT cDNA. The BAMT resulting from amplification from the second methionine shows a 2.4 times higher specific activity than from the first methionine in protein purified from cell lysate; on the other hand, BAMT purified from E. coli shows no difference in specific activity (from both Met codons). The Km and kcat are the same from both codons in E. coli.
- Inhibition by SAH was competitive with respect to SAM and noncompetitive with respect to benzoic acid. SAM appears to be the first substrate to bind to the enzyme. Methyl benzoate is released first and SAH last.
- BAMT activity may be regulated by the intracellular SAM/SAH concentration ratio rather than benzoic acid availability.
Sequence and Features
- 10COMPATIBLE WITH RFC
- 12Illegal NheI site found at 970
- 21Illegal XhoI site found at 654
- 23COMPATIBLE WITH RFC
- 25COMPATIBLE WITH RFC
- 1000COMPATIBLE WITH RFC