Difference between revisions of "Part:BBa J45002"

Revision as of 23:38, 13 June 2006

SAM:benzoic acid carboxyl methyltransferase; converts benzoic acid to methyl benzoate (floral odor)

This is the cDNA sequence of 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.

Usage and Biology

Enzyme is active as a dimer.
There are two Met codons at the begnning of the BAMT cDNA. The BAMT resulting from amplification from the second Met shows a 2.4 times higher specific activity than from the first Met 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_m and k_cat are the same from both codons in E. coli.
Inhibition by SAH was competitive with respect to SAM and noncompetitive with respect to BA. The K_i value of SAH was determined to be 7 μM for SAM and 14 μM for BA. SAM appears to be the first substrate to bind to the enzyme. Methyl benzoate, would be the first to be released and SAH the last.
BAMT activity may be regulated by the intracellular SAM/SAH concentration ratio rather than BA 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_num	2.1.1.-
kegg	none
protein	BAMT
swisspro	Q9FYZ9

@@ Line 6: / Line 6: @@
 ===Usage and Biology===
-#*Enzyme is active as a dimer.
+*Enzyme is active as a dimer.
-#*There are two Met codons at the begnning of the BAMT cDNA.  The BAMT resulting from amplification from the second Met shows a 2.4 times higher specific activity than from the first Met 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''.
+*There are two Met codons at the begnning of the BAMT cDNA.  The BAMT resulting from amplification from the second Met shows a 2.4 times higher specific activity than from the first Met 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''.
-#*Inhibition by SAH was competitive with respect to SAM and noncompetitive with respect to BA. The K<sub>i</sub> value of SAH was determined to be 7 μM for SAM and 14 μM for BA. SAM appears to be the first substrate to bind to the enzyme. Methyl benzoate, would be the first to be released and SAH the last.
+*Inhibition by SAH was competitive with respect to SAM and noncompetitive with respect to BA. The K<sub>i</sub> value of SAH was determined to be 7 μM for SAM and 14 μM for BA. SAM appears to be the first substrate to bind to the enzyme. Methyl benzoate, would be the first to be released and SAH the last.
-#*BAMT activity may be regulated by the intracellular SAM/SAH concentration ratio rather than BA availability.
+*BAMT activity may be regulated by the intracellular SAM/SAH concentration ratio rather than BA availability.
 <span class='h3bb'>Sequence and Features</span>