EC number:2.1.1.300

Enzyme

Download
EC Tree
     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.300
Description:Pavine N-methyltransferase.
Alternative Name: PavNMT.

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.
PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.300
BRENDA Enzyme Link: BRENDA 2.1.1.300
KEGG Enzyme Link: KEGG2.1.1.300
BioCyc Enzyme Link: BioCyc 2.1.1.300
ExPASy Enzyme Link: ExPASy2.1.1.300
EC2PDB Enzyme Link: EC2PDB 2.1.1.300
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.300
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.300
IntEnz Enzyme Link: IntEnz 2.1.1.300
MEDLINE Enzyme Link: MEDLINE 2.1.1.300

EC number:2.1.1.300

MSA:

2.1.1.300;
Phylogenetic Tree:

2.1.1.300;
Uniprot:
M-CSA:
RHEA:39979 (+-)-pavine + S-adenosyl-L-methionine = H(+) + N-methylpavine + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[NH;+0:2]-[*:3].[*:4]-[S+;H0:5](-[*:6])-[CH3;+0:7]>>[*:1]-[N;H0;+0:2](-[*:3])-[CH3;+0:7].[*:4]-[S;H0;+0:5]-[*:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Targeted metabolite and transcript profiling for elucidating enzyme function: isolation of novel N-methyltransferases from three benzylisoquinoline alkaloid-producing species.Liscombe DK, Ziegler J, Schmidt J, Ammer C, Facchini PJ2009 Nov19624470
Purification, crystallization and X-ray diffraction analysis of pavine N-methyltransferase from Thalictrum flavum.Jain A, Ziegler J, Liscombe DK, Facchini PJ, Tucker PA, Panjikar S2008 Nov 118997344