Species: Arabidopsis thaliana col
The farnesoic acid carboxyl methyltransferase (FAMT) identified in Arabidopsis thaliana col is a member of the plant family of SABBATH methyltransferases [Yang06a]. In vitro characterization of this enzyme shows that it can methylate a number of structurally related compounds, but that (2-trans-6-trans)-farnesoate is its preferred substrate.
Atlhough E,E-methyl farnesoate has not been detected in Arabidopsis in in vivo, it has been observed in other plants where the biological importance of it and related compounds remains to be determined [Bede01, Yang06a]. However, the up-regulation of FAMT transcript levels by a fungal elicitor, as well as treatments with jasmonic acid and salicylic acid, suggest a possible involvement for E,E-methyl farnesoate or structurally similar compounds in plant defense [Yang06a].
Enzymatic reaction of: farnesoic acid carboxyl methyltransferase
Synonyms: farnesoate carboxyl methyltransferase
EC Number: 2.1.1.-
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.
The reaction is physiologically favored in the direction shown.
The enzyme accepts two alternative substrates for (2-trans-6-trans)-farnesoate (FA) in vitro, namely laurate (18+/- 6% of the level of activity with FA) and geranate (28+/- 3% of the activity level with FA) [Yang06a].
This enzyme is active over a pH range of 7 to 9.5 [Yang06a]. It is not inhibited by 2.5 mM EDTA. The enzyme loses all of its activity if incubated at 50 °C for 30 min. It retains 50% of its maximum activity if incubated at 40 °C for 30 min, and 90% of its activity if incubated at 30 °C for 30 min [Yang06a].
pH(opt): 8.0-8.5 [Yang06a]
Bede01: Bede JC, Teal PE, Goodman WG, Tobe SS (2001). "Biosynthetic pathway of insect juvenile hormone III in cell suspension cultures of the sedge Cyperus iria." Plant Physiol 127(2);584-93. PMID: 11598232
Yang06a: Yang Y, Yuan JS, Ross J, Noel JP, Pichersky E, Chen F (2006). "An Arabidopsis thaliana methyltransferase capable of methylating farnesoic acid." Arch Biochem Biophys 448(1-2);123-32. PMID: 16165084
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