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Literature summary for 2.1.1.104 extracted from

  • Naaz, H.; Pandey, V.P.; Singh, S.; Dwivedi, U.N.
    Structure-function analyses and molecular modeling of caffeic acid-O-methyltransferase and caffeoyl-CoA-O-methyltransferase: revisiting the basis of alternate methylation pathways during monolignol biosynthesis (2013), Biotechnol. Appl. Biochem., 60, 170-189.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular docking of 16 putative substrates (intermediates of monolignol biosynthesis pathway). Both caffeic acid-O-methyltransferase, EC 2.1.1.68, and caffeoyl-coenzyme A-O-methyltransferase interact with all 16 substrates in a similar manner, with thiol esters being the most potent and binding of these putative substrates to caffeoyl-coenzyme A-O-methyltransferase being more efficient Medicago sativa

Organism

Organism UniProt Comment Textmining
Medicago sativa Q40313
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information in silico studies suggest that alcoholic and aldehydic substrates are preferred to those of caffeic, sinapic, and ferulic acid by both caffeic acid-O-methyltransferase, EC 2.1.1.68, and caffeoyl-coenzyme A-O-methyltransferase with a marked preference for CoA ester substrates over free acids, aldehydes, and alcohols Medicago sativa ?
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Synonyms

Synonyms Comment Organism
CCOMT
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Medicago sativa