| Entry |
|
| Name |
bacteriochlorophyllide d C-121-methyltransferase;
bchR (gene name)
|
| Class |
Transferases;
Transferring one-carbon groups;
Methyltransferases
 |
| Sysname |
S-adenosyl-L-methionine:8-ethyl-12-methyl-3-vinylbacteriochlorophyllide-d C-121-methyltransferase
|
| Reaction(IUBMB) |
S-adenosyl-L-methionine + 8-ethyl-12-methyl-3-vinylbacteriochlorophyllide d = S-adenosyl-L-homocysteine + 8,12-diethyl-3-vinylbacteriochlorophyllide d [RN: R11507]
|
| Reaction(KEGG) |
|
| Substrate |
S-adenosyl-L-methionine [CPD: C00019];
8-ethyl-12-methyl-3-vinylbacteriochlorophyllide d [CPD: C18157]
|
| Product |
S-adenosyl-L-homocysteine [CPD: C00021];
8,12-diethyl-3-vinylbacteriochlorophyllide d [CPD: C21427]
|
| Comment |
This enzyme, found in green sulfur bacteria (Chlorobiaceae) and green flimentous bacteria (Chloroflexaceae), is a radical S-adenosyl-L-methionine (AdoMet) enzyme and contains a [4Fe-4S] cluster. It adds a methyl group at the C-121 position of bacteriochlorophylls of the c, d and e types. This methylation plays a role in fine-tuning the structural arrangement of the bacteriochlorophyll aggregates in chlorosomes and therefore directly influences the chlorosomes absorption properties.
|
| History |
EC 2.1.1.331 created 2016
|
| Pathway |
| Porphyrin and chlorophyll metabolism | | Biosynthesis of secondary metabolites |
|
| Orthology |
| bacteriochlorophyllide d C-12(1)-methyltransferase |
|
| Genes |
CTE: | | CPC: | | CLZ: | | CCH: | | CPH: | | CPB: | | CLI: | | PVI: | | PLT: | | PPH: | | PAA: | | PROC: | | CTS: | | » show all
 |
| Reference |
|
| Authors |
Gomez Maqueo Chew A, Frigaard NU, Bryant DA. |
| Title |
Bacteriochlorophyllide c C-8(2) and C-12(1) methyltransferases are essential for adaptation to low light in Chlorobaculum tepidum. |
| Journal |
J. Bacteriol. 189 (2007) 6176-84. |
| Sequence |
|
| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: |