Substrates: recombinant MBMT protein expressed in Escherichia coli shows the highest substrate preference toward 4-methoxybenzoic acid. EjMT1 shows high activity with 3-methoxybenzoic acid and vanillic acid. The activity of EjMBMT with benzoic acid, 2-methoxybenzoic acid, anthranilic acid, and jasmonic acid is approximately half of that with p-methoxybenzoic acid. Enzyme EjMBMT displays negligible activity to salicylic acid, shikimic acid, and caffeic acid, no activity with indole-3-acetic acid and cinnamic acid. The enzyme is relatively specific for methoxybenzoic acids and the methoxy group on a benzene ring might be important for either enzyme binding or methyl group transfer from SAM by EjMBMT Products: -
inflorescences of loquat flowers constitute stiff panicles, open flowers are classified as one of four developmental stages, stage 1, stage 2, stage 3, or stage 4. Transcript levels of MBMT continually increase throughout the flower development with peak expression occurring in fully opened flowers
the floral trichomes do not contribute to the production of volatile benzenoids in loquat. EjMT1 is highly expressed in flower petals as compared to the other three EjMT genes. The transcript levels of EjMT1 gene increase as buds matured into flowers and those of EjMT1 are 100 to 300folds higher in flower tissues than in leaves. Quantitative enzyme expression analysis by RT-PCR
in contrast to benzoic acid carboxyl methyltransferase (BAMT) and benzoic acid/salicylic acid carboxyl methyltransferase (EC 2.1.1.274/2.1.1.273), MBMT also displays activity towards both benzoic acid and jasmonic acid. Phylogenetic analysis reveals that loquat MBMT forms a monophyletic group with jasmonic acid carboxyl methyltransferases (JMTs, EC 2.1.1.141) from other plant species. Plant enzymes with same BAMT activity have evolved independently
it appears likely that a para-hydroxyl group of p-hydroxybenzoic acid is first methylated by an yet unidentified O-methyltransferase, then EjMBMT converts the resulting p-methoxybenzoic acid to methyl 4-methoxybenzoate in vivo, but not vice versa
EjMT1 encodes a p-methoxybenzoic acid carboxyl methyltransferase (MBMT), an enzyme capable of converting p-methoxybenzoic acid to methyl p-methoxybenzoate via methylation of the carboxyl group. 4-Methoxybenzaldehyde and methyl 4-methoxybenzoate, along with (2-nitroethyl) benzene, are major components of the floral scent of the Japanese loquat (Eriobotrya japonica). Distribution of volatile benzenoids in different parts of the loquat plant, overview
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene EjMT1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, quantitative RT-PCR enzyme expression analysis, functional recombinant expression of His-tagged enzyme EjMT1 in Escherichia coli
Koeduka, T.; Kajiyama, M.; Suzuki, H.; Furuta, T.; Tsuge, T.; Matsui, K.
Benzenoid biosynthesis in the flowers of Eriobotrya japonica molecular cloning and functional characterization of p-methoxybenzoic acid carboxyl methyltransferase
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