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Literature summary for 2.1.1.128 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
Search for more literature for 2.1.1.128

Cloned(Commentary)

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

Inhibitors

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Coptis japonica
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer
-
 Coptis japonica

Synonyms

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

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
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