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Literature summary for 2.1.1.116 extracted from

  • Zhu, Q.; Zhu, M.; Fan, G.; Zou, J.; Feng, P.; Liu, Z.; Wang, W.
    Molecular modeling and docking studies of 3-hydroxy-N-methylcoclaurine 4-O-methyltransferase from Coptis chinensis (2014), Bull. Korean Chem. Soc., 35, 62-68.
No PubMed abstract available
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-Adenosyl-L-methionine + 3'-hydroxy-N-methyl-(S)-coclaurine Coptis chinensis
-
 S-Adenosyl-L-homocysteine + (S)-reticuline
-
 ?

Organism

Organism UniProt Comment Textmining
Coptis chinensis B6RJT5
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information no activity with norcoclaurine, coclaurine, N-methylcoclaurine, reticuline, scoulerine, and tetrahydrocolumbamine Coptis chinensis ?
-
 ?
S-Adenosyl-L-methionine + 3'-hydroxy-N-methyl-(S)-coclaurine
-
 Coptis chinensis S-Adenosyl-L-homocysteine + (S)-reticuline
-
 ?

Synonyms

Synonyms Comment Organism
3-hydroxy-N-methylcoclaurine 4-O-methyltransferase
-
 Coptis chinensis
HOMT
-
 Coptis chinensis

General Information

General Information Comment Organism
metabolism essential enzyme in the berberine biosynthetic pathway Coptis chinensis