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Literature summary extracted from

  • Morishige, T.; Tamakoshi, M.; Takemura, T.; Sato, F.
    Molecular characterization of O-methyltransferases involved in isoquinoline alkaloid biosynthesis in Coptis japonica (2010), Proc. Jpn. Acad. Ser. B, 86, 757-768.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.128 expressed in Escherichia coli BL21(DE3) cells Coptis japonica

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.128 additional information not inhibited by chloromercuribenzenesulfonate and iodoacetamide Coptis japonica
2.1.1.128 S-adenosyl-L-homocysteine
-
 Coptis japonica

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.1.128 additional information the enzyme requires divalent cations for activity Coptis japonica

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.128 Coptis japonica
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.128 Q-Sepharose column chromatography and Bio-Gel HTP column chromatography Coptis japonica

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.128 S-adenosyl-L-methionine + (S)-norcoclaurine
-
 Coptis japonica S-adenosyl-L-homocysteine + (S)-coclaurine
-
 ir
2.1.1.128 S-adenosyl-L-methionine + (S)-norlaudanosoline
-
 Coptis japonica S-adenosyl-L-homocysteine + 6-O-methylnorlaudanosoline
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.128 dimer
-
 Coptis japonica

Synonyms

EC Number Synonyms Comment Organism
2.1.1.128 6-OMT
-
 Coptis japonica
2.1.1.128 S-Adenosyl-L-methionine:norcoclaurine 6-O-methyltransferase
-
 Coptis japonica

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.1.1.128 0.18
-
 using (S)-norlaudanosoline as cosubstrate, in 0.3 M Tris-HCl (pH 7.5), 25mM sodium ascorbate, at 30°C Coptis japonica S-adenosyl-L-homocysteine