(S)-scoulerine 9-O-methyltransferase

(S)-scoulerine 9-O-methyltransferase (EC 2.1.1.117) is an enzyme that catalyzes the chemical reaction

(S)-scoulerine 9-O-methyltransferase
Identifiers
EC no.2.1.1.117
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
+ SAM
 
 
 
 
Rightward reaction arrow
 
 
 
+ SAH
 

This is a methylation reaction in which the benzylisoquinoline alkaloid, (S)-scoulerine, is converted to (S)-isocorypalmine. The methyl group comes from the cofactor, S-adenosyl methionine (SAM), which becomes S-adenosyl-L-homocysteine (SAH). The enzyme was characterised from Berberis wilsoniae.[1]

This enzyme belongs to the family of transferases, specifically those transferring one-carbon group methyltransferases. The systematic name of this enzyme class is S-adenosyl-L-methionine:(S)-scoulerine 9-O-methyltransferase. It is part of the alkaloid biosynthesis pathway.[2]

References

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  1. Muemmler S, Rueffer M, Nagakura N, Zenk MH (1985). "S-Adenosyl-L-methionine:(S)-scoulerine 9-O-methyltransferase, a highly stereo- and regiospecific enzyme in tetrahydroberberine biosynthesis". Plant Cell Reports. 4 (1): 36–39. doi:10.1007/BF00285501. PMID 24253642.
  2. Enzyme 2.1.1.117 at KEGG Pathway Database.