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Literature summary for 2.1.1.76 extracted from

  • Itoh, N.; Iwata, C.; Toda, H.
    Molecular cloning and characterization of a flavonoid-O-methyltransferase with broad substrate specificity and regioselectivity from Citrus depressa (2016), BMC Plant Biol., 16, 180 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene FOMT5, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of soluble homodimeric His6-tagged enzyme in Escherichia coli strain BL21(DE3) Citrus depressa

Metals/Ions

Metals/Ions Comment Organism Structure
additional information the enzyme is an Mg2+-independent O-methyltransferase Citrus depressa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
88000
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recombinant His6-tagged enzyme, gel filtration Citrus depressa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4 S-adenosyl-L-methionine + quercetin Citrus depressa whole-cell biocatalysis using CdFOMT5 expressed in Escherichia coli cells is performed using quercetin as a substrate, and 3,3',5,7-tetramethylated quercetin is obtained as the final product 4 S-adenosyl-L-homocysteine + 3,3',5,7-tetramethoxyquercetin
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?

Organism

Organism UniProt Comment Textmining
Citrus depressa A0A125T1T5
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-

Source Tissue

Source Tissue Comment Organism Textmining
fruit
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Citrus depressa
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pericarp
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Citrus depressa
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4 S-adenosyl-L-methionine + quercetin whole-cell biocatalysis using CdFOMT5 expressed in Escherichia coli cells is performed using quercetin as a substrate, and 3,3',5,7-tetramethylated quercetin is obtained as the final product Citrus depressa 4 S-adenosyl-L-homocysteine + 3,3',5,7-tetramethoxyquercetin
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?
additional information the flavonoid-O-methyltransferase from Citrus depressa has a broad substrate specificity and regioselectivity. Isozyme CdFOMT5 exhibits O-methyltransferase activity for quercetin, naringenin, (-)-epicatechin, and equol using S-adenosyl-L-methionine (SAM) as a methyl donor. The recombinant CdFOMT5 CdFOMT5 can catalyze the O-methylation of at least three hydroxyl groups of quercetin, and di- or tri-O-methylated quercetin products are obtained by this enzymatic reaction. CdFMOT5 prefers flavonol (3-hydroxyflavone) to other flavonoid structures. Thus, substrate structure, especially the C-ring in flavonoids, may strongly affect the substrate preference, including regioselectivity, of CdFOMT5 Citrus depressa ?
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S-adenosyl-L-methionine + quercetin
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Citrus depressa S-adenosyl-L-homocysteine + 3'-methoxyquercetin
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?
S-adenosyl-L-methionine + quercetin
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Citrus depressa S-adenosyl-L-homocysteine + 3-methoxyquercetin
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?
S-adenosyl-L-methionine + quercetin
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Citrus depressa S-adenosyl-L-homocysteine + 5-methoxyquercetin
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?
S-adenosyl-L-methionine + quercetin
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Citrus depressa S-adenosyl-L-homocysteine + 7-methoxyquercetin
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?

Subunits

Subunits Comment Organism
homodimer 2 * 42030, recombinant His6-tagged enzyme, sequence calculation, 2 * 42000, recombinant His6-tagged enzyme, SDS-PAGE Citrus depressa

Synonyms

Synonyms Comment Organism
CdFOMT5
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Citrus depressa
flavonoid-O-methyltransferase
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Citrus depressa
FOMT5
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Citrus depressa
Mg2+-independent O-methyltransferase
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Citrus depressa
More see also EC 2.1.1.267 Citrus depressa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
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recombinant enzyme Citrus depressa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
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recombinant enzyme Citrus depressa

pH Range

pH Minimum pH Maximum Comment Organism
5.5 9 recombinant enzyme, over 50% activity within this range Citrus depressa

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
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Citrus depressa

pI Value

Organism Comment pI Value Maximum pI Value
Citrus depressa recombinant detagged enzyme, sequence calculation
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5.79