Difference between revisions of "Part:BBa J45002"
 
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<partinfo>BBa_J45002 short</partinfo>
 
<partinfo>BBa_J45002 short</partinfo>
  
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This is the BAMT enzyme from ''Antirrhinus majus'' (snapdragon). BAMT catalyzes the transfer of a methyl group from SAM (S-adenosyl methyltransferase) to benzoic acid, creating methyl benzoate.  Methyl benzoate produces a "pleasant" smell.  Genbank accession number(s): AF198492.
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<partinfo>BBa_J45002</partinfo> 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===
 
===Usage and Biology===
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*Enzyme is active as a dimer.
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*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 K<sub>m</sub> and k<sub>cat</sub> are the same from both codons in ''E. coli''.
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*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.
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*BAMT activity may be regulated by the intracellular SAM/SAH concentration ratio rather than benzoic acid availability.
  
 
<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
 
<partinfo>BBa_J45002 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_J45002 SequenceAndFeatures</partinfo>
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===Functional Parameters===
 
===Functional Parameters===
 
<partinfo>BBa_J45002 parameters</partinfo>
 
<partinfo>BBa_J45002 parameters</partinfo>

Latest revision as of 21:35, 9 March 2008

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


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NheI site found at 970
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal XhoI site found at 654
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]

Functional Parameters

ec_num2.1.1.-
keggnone
proteinBAMT
swissproQ9FYZ9