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Literature summary for 2.1.1.267 extracted from

  • Jeong, K.; Lee, J.; Kang, D.; Lee, J.; Hwang, Y.; Kim, Y.
    Flavonoids as substrates of Bacillus halodurans O-methyltransferase (2008), Bull. Korean Chem. Soc., 29, 1311-1314.
No PubMed abstract available
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Cloned(Commentary)

Cloned (Comment) Organism
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 Halalkalibacterium halodurans

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ interactions between flavonoid and enzyme are enhanced by metal-mediated electrostatic interactions in substrate binding site. Ca2+ and Mg2+ show similar effects Halalkalibacterium halodurans
Mg2+ interactions between flavonoid and enzyme are enhanced by metal-mediated electrostatic interactions in substrate binding site. Ca2+ and Mg2+ show similar effects Halalkalibacterium halodurans

Organism

Organism UniProt Comment Textmining
Halalkalibacterium halodurans
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + fisetin analysis of binding constant and docking energy Halalkalibacterium halodurans S-adenosyl-L-homocysteine + ?
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 ?
S-adenosyl-L-methionine + luteolin analysis of binding constant and docking energy Halalkalibacterium halodurans S-adenosyl-L-homocysteine + ?
-
 ?
S-adenosyl-L-methionine + myricetin analysis of binding constant and docking energy Halalkalibacterium halodurans S-adenosyl-L-homocysteine + ?
-
 ?
S-adenosyl-L-methionine + quercetin analysis of binding constant and docking energy Halalkalibacterium halodurans S-adenosyl-L-homocysteine + ?
-
 ?