bacteriochlorophyllide d C-8(2)-methyltransferase [EC:2.1.1.332]

PMID:17586634

Gomez Maqueo Chew A, Frigaard NU, Bryant DA

Bacteriochlorophyllide c C-8(2) and C-12(1) methyltransferases are essential for  adaptation to low light in Chlorobaculum tepidum.

J Bacteriol 189:6176-84 (2007)
DOI:10.1128/JB.00519-07

[cte:CT1777]

PMID:17506685

Chew AG, Bryant DA

Chlorophyll biosynthesis in bacteria: the origins of structural and functional diversity.

Annu Rev Microbiol 61:113-29 (2007)
DOI:10.1146/annurev.micro.61.080706.093242

Transferases;
Transferring one-carbon groups;
Methyltransferases

S-adenosyl-L-methionine:8,12-diethyl-3-vinylbacteriochlorophyllide-d C-82-methyltransferase

(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]

R11508 R11509

S-adenosyl-L-methionine [CPD:C00019];
8,12-diethyl-3-vinylbacteriochlorophyllide d [CPD:C21427];
12-ethyl-8-propyl-3-vinylbacteriochlorophyllide d [CPD:C21428]

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.

EC 2.1.1.332 created 2016

1  [PMID:17586634]

Gomez Maqueo Chew A, Frigaard NU, Bryant DA.

Bacteriochlorophyllide c C-8(2) and C-12(1) methyltransferases are essential for  adaptation to low light in Chlorobaculum tepidum.

J. Bacteriol. 189 (2007) 6176-84.

[cte:CT1777]