KEGG   ENZYME: 2.1.1.337
Entry
EC 2.1.1.337                Enzyme                                 
Name
reticuline N-methyltransferase;
RNMT
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
Sysname
S-adenosyl-L-methionine:(S)-reticuline N-methyltransferase
Reaction(IUBMB)
(1) S-adenosyl-L-methionine + (S)-reticuline = S-adenosyl-L-homocysteine + (S)-tembetarine [RN:R11595];
(2) S-adenosyl-L-methionine + (S)-corytuberine = S-adenosyl-L-homocysteine + (S)-magnoflorine [RN:R08791]
Reaction(KEGG)
R08791 R11595
Substrate
S-adenosyl-L-methionine [CPD:C00019];
(S)-reticuline [CPD:C02105];
(S)-corytuberine [CPD:C17591]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
(S)-tembetarine [CPD:C21491];
(S)-magnoflorine [CPD:C09581]
Comment
The enzyme from opium poppy (Papaver somniferum) can also methylate (R)-reticuline, tetrahydropapaverine, (S)-glaucine and (S)-bulbocapnine. It is involved in the biosynthesis of the quaternary benzylisoquinoline alkaloid magnoflorine.
History
EC 2.1.1.337 created 2017
Pathway
ec00950  Isoquinoline alkaloid biosynthesis
ec01110  Biosynthesis of secondary metabolites
Orthology
K21580  reticuline N-methyltransferase
Genes
PSOM113277829 113300499 113309783 113319724 113324773 113344288
Reference
1  [PMID:27634038]
  Authors
Morris JS, Facchini PJ
  Title
Isolation and Characterization of Reticuline N-Methyltransferase Involved in Biosynthesis of the Aporphine Alkaloid Magnoflorine in Opium Poppy.
  Journal
J Biol Chem 291:23416-23427 (2016)
DOI:10.1074/jbc.M116.750893
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.337
IUBMB Enzyme Nomenclature: 2.1.1.337
ExPASy - ENZYME nomenclature database: 2.1.1.337
BRENDA, the Enzyme Database: 2.1.1.337

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