| EC |
2.1.1.300 |
| Accepted name: |
pavine N-methyltransferase |
| Reaction: |
S-adenosyl-L-methionine + (±)-pavine = S-adenosyl-L-homocysteine + N-methylpavine |
| Other name(s): |
PavNMT |
| Systematic name: |
S-adenosyl-L-methionine:(±)-pavine N-methyltransferase |
| Comments: |
The enzyme, isolated from the plant Thalictrum flavum, also methylates (R,S)-stylopine and (S)-scoulerine (11%) with lower activity (14% and 11%, respectively). |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Jain, A., Ziegler, J., Liscombe, D.K., Facchini, P.J., Tucker, P.A. and Panjikar, S. Purification, crystallization and X-ray diffraction analysis of pavine N-methyltransferase from Thalictrum flavum. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64 (2008) 1066–1069. [DOI] [PMID: 18997344] |
| 2. |
Liscombe, D.K., Ziegler, J., Schmidt, J., Ammer, C. and Facchini, P.J. Targeted metabolite and transcript profiling for elucidating enzyme function: isolation of novel N-methyltransferases from three benzylisoquinoline alkaloid-producing species. Plant J. 60 (2009) 729–743. [DOI] [PMID: 19624470] |
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| [EC 2.1.1.300 created 2014] |
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