EC number:2.1.1.331
| ID: | 2.1.1.331 |
|---|---|
| Description: | Bacteriochlorophyllide d C-12(1)-methyltransferase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.1.1.331 |
| BRENDA Enzyme Link: | BRENDA 2.1.1.331 |
| KEGG Enzyme Link: | KEGG2.1.1.331 |
| BioCyc Enzyme Link: | BioCyc 2.1.1.331 |
| ExPASy Enzyme Link: | ExPASy2.1.1.331 |
| EC2PDB Enzyme Link: | EC2PDB 2.1.1.331 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.331 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.331 |
| IntEnz Enzyme Link: | IntEnz 2.1.1.331 |
| MEDLINE Enzyme Link: | MEDLINE 2.1.1.331 |
EC number:2.1.1.331
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:49168 | 8-ethyl-12-methyl-3-vinylbacteriochlorophyllide d + S-adenosyl-L-methionine = 8,12-diethyl-3-vinylbacteriochlorophyllide d + H(+) + S-adenosyl-L-homocysteine |
| RULE(radius=1) | [*:1]-[CH3;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[CH2;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Bacteriochlorophyllide c C-8(2) and C-12(1) methyltransferases are essential for adaptation to low light in Chlorobaculum tepidum. | Gomez Maqueo Chew A, Frigaard NU, Bryant DA | 2007 Sep | 17586634 |