Entry |
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Name |
bacteriochlorophyllide d C-82-methyltransferase;
bchQ (gene name)
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Class |
Transferases;
Transferring one-carbon groups;
Methyltransferases
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Sysname |
S-adenosyl-L-methionine:8,12-diethyl-3-vinylbacteriochlorophyllide-d C-82-methyltransferase
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Reaction(IUBMB) |
(1) S-adenosyl-L-methionine + 8,12-diethyl-3-vinylbacteriochlorophyllide d = S-adenosyl-L-homocysteine + 12-ethyl-8-propyl-3-vinylbacteriochlorophyllide d [RN: R11508];
(2) S-adenosyl-L-methionine + 12-ethyl-8-propyl-3-vinylbacteriochlorophyllide d = S-adenosyl-L-homocysteine + 12-ethyl-8-isobutyl-3-vinylbacteriochlorophyllide d [RN: R11509]
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Reaction(KEGG) |
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Substrate |
S-adenosyl-L-methionine [CPD: C00019];
8,12-diethyl-3-vinylbacteriochlorophyllide d [CPD: C21427];
12-ethyl-8-propyl-3-vinylbacteriochlorophyllide d [CPD: C21428]
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Product |
S-adenosyl-L-homocysteine [CPD: C00021];
12-ethyl-8-propyl-3-vinylbacteriochlorophyllide d [CPD: C21428];
12-ethyl-8-isobutyl-3-vinylbacteriochlorophyllide d [CPD: C21429]
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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 one or two methyl groups at the C-82 position of bacteriochlorophylls of the c, d, and e types. These methylations play a role in fine-tuning the structural arrangement of the bacteriochlorophyll aggregates in chlorosomes and therefore directly influence chlorosomal absorption properties.
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History |
EC 2.1.1.332 created 2016
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Pathway |
ec00860 | Porphyrin and chlorophyll metabolism |
ec01110 | Biosynthesis of secondary metabolites |
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Orthology |
K13601 | bacteriochlorophyllide d C-8(2)-methyltransferase |
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Genes |
» show all
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Reference |
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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 |
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Sequence |
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Other DBs |
ExPASy - ENZYME nomenclature database: | 2.1.1.332 |
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