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Literature summary extracted from

  • 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 (2016), Planta, 244, 725-736 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.B126 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 Rhaphiolepis bibas

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.B126 0.0091
-
 S-adenosyl-L-methionine pH 6.5, 25°C, recombinant enzyme Rhaphiolepis bibas
2.1.1.B126 0.1373
-
 4-Methoxybenzoate pH 6.5, 25°C, recombinant enzyme Rhaphiolepis bibas

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.B126 S-adenosyl-L-methionine + 4-methoxybenzoate Rhaphiolepis bibas
-
 methyl 4-methoxybenzoate + S-adenosyl-L-homocysteine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.B126 Rhaphiolepis bibas A0A1B4Z3V0 flowers and leaves collected in winter at the Uji campus (E135°48', N34°54') of Kyoto University, Japan
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.B126 recombinant His-tagged enzyme EjMT1 from Escherichia coli by nickel affinity chromatography Rhaphiolepis bibas

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.1.B126 flower 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 Rhaphiolepis bibas
-
2.1.1.B126 leaf low enzyme level Rhaphiolepis bibas
-
2.1.1.B126 additional information 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 Rhaphiolepis bibas
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2.1.1.B126 petal
-
 Rhaphiolepis bibas
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.B126 additional information 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 Rhaphiolepis bibas ?
-
-
2.1.1.B126 S-adenosyl-L-methionine + 2-methoxybenzoate low activity Rhaphiolepis bibas methyl 2-methoxybenzoate + S-adenosyl-L-homocysteine
-
 ?
2.1.1.B126 S-adenosyl-L-methionine + 3-methoxybenzoate high activity Rhaphiolepis bibas methyl 3-methoxybenzoate + S-adenosyl-L-homocysteine
-
 ?
2.1.1.B126 S-adenosyl-L-methionine + 4-methoxybenzoate
-
 Rhaphiolepis bibas methyl 4-methoxybenzoate + S-adenosyl-L-homocysteine
-
 ?
2.1.1.B126 S-adenosyl-L-methionine + 4-methoxybenzoate best substrate Rhaphiolepis bibas methyl 4-methoxybenzoate + S-adenosyl-L-homocysteine
-
 ?
2.1.1.B126 S-adenosyl-L-methionine + anthranilate low activity Rhaphiolepis bibas methyl anthranilate + S-adenosyl-L-homocysteine
-
 ?
2.1.1.B126 S-adenosyl-L-methionine + jasmonate low activity Rhaphiolepis bibas methyl jasmonate + S-adenosyl-L-homocysteine
-
 ?
2.1.1.B126 S-adenosyl-L-methionine + vanillate
-
 Rhaphiolepis bibas methyl vanillate + S-adenosyl-L-homocysteine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.B126 EjMBMT
-
 Rhaphiolepis bibas
2.1.1.B126 EjMT1
-
 Rhaphiolepis bibas
2.1.1.B126 MBMT
-
 Rhaphiolepis bibas
2.1.1.B126 p-methoxybenzoic acid carboxyl methyltransferase
-
 Rhaphiolepis bibas

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.B126 25
-
 assay at Rhaphiolepis bibas

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.1.B126 0.018
-
 S-adenosyl-L-methionine pH 6.5, 25°C, recombinant enzyme Rhaphiolepis bibas
2.1.1.B126 0.018
-
 4-Methoxybenzoate pH 6.5, 25°C, recombinant enzyme Rhaphiolepis bibas

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.B126 6 6.5 recombinant enzyme Rhaphiolepis bibas

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.1.1.B126 6 7.5 activity range, recombinant enzyme Rhaphiolepis bibas

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.B126 S-adenosyl-L-methionine
-
 Rhaphiolepis bibas

General Information

EC Number General Information Comment Organism
2.1.1.B126 evolution 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 Rhaphiolepis bibas
2.1.1.B126 metabolism 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 Rhaphiolepis bibas
2.1.1.B126 physiological function 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 Rhaphiolepis bibas

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.1.1.B126 0.131
-
 4-Methoxybenzoate pH 6.5, 25°C, recombinant enzyme Rhaphiolepis bibas
2.1.1.B126 1.98
-
 S-adenosyl-L-methionine pH 6.5, 25°C, recombinant enzyme Rhaphiolepis bibas