KEGG   ENZYME: 2.1.1.300Help
Entry
EC 2.1.1.300                Enzyme                                 

Name
pavine N-methyltransferase;
PavNMT
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
BRITE hierarchy
Sysname
S-adenosyl-L-methionine:(+/-)-pavine N-methyltransferase
Reaction(IUBMB)
S-adenosyl-L-methionine + (+/-)-pavine = S-adenosyl-L-homocysteine + N-methylpavine [RN:R10680]
Reaction(KEGG)
Substrate
S-adenosyl-L-methionine [CPD:C00019];
(+/-)-pavine [CPD:C20771]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
N-methylpavine [CPD:C20770]
Comment
The enzyme, isolated from the plant Thalictrum flavum, also methylates (R,S)-stylopine and (S)-scoulerine (11%) with lower activity (14% and 11%, respectively).
History
EC 2.1.1.300 created 2014
Reference
1  [PMID:18997344]
  Authors
Jain A, Ziegler J, Liscombe DK, Facchini PJ, Tucker PA, Panjikar S
  Title
Purification, crystallization and X-ray diffraction analysis of pavine N-methyltransferase from Thalictrum flavum.
  Journal
Acta. Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. 64 (2008) 1066-9.
Reference
2  [PMID:19624470]
  Authors
Liscombe DK, Ziegler J, Schmidt J, Ammer C, Facchini PJ
  Title
Targeted metabolite and transcript profiling for elucidating enzyme function: isolation of novel N-methyltransferases from three benzylisoquinoline alkaloid-producing species.
  Journal
Plant. J. 60 (2009) 729-43.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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