ID: | 2.1.1.140 |
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Description: | (S)-coclaurine-N-methyltransferase. |
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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.UniProtKB Enzyme Link: | UniProtKB 2.1.1.140 |
BRENDA Enzyme Link: | BRENDA 2.1.1.140 |
KEGG Enzyme Link: | KEGG2.1.1.140 |
BioCyc Enzyme Link: | BioCyc 2.1.1.140 |
ExPASy Enzyme Link: | ExPASy2.1.1.140 |
EC2PDB Enzyme Link: | EC2PDB 2.1.1.140 |
ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.140 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.140 |
IntEnz Enzyme Link: | IntEnz 2.1.1.140 |
MEDLINE Enzyme Link: | MEDLINE 2.1.1.140 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:17409 | (S)-coclaurine + S-adenosyl-L-methionine = (S)-N-methylcoclaurine + H(+) + 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 |
Title | Authors | Date | PubMed ID |
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Molecular cloning and characterization of coclaurine N-methyltransferase from cultured cells of Coptis japonica. | Choi KB, Morishige T, Shitan N, Yazaki K, Sato F | 2002 Jan 4 | 11682473 |