KEGG Orthology (KO) [BR:ko00001]
09100 Metabolism
09108 Metabolism of cofactors and vitamins
00860 Porphyrin metabolism
K11333 bchX; 3,8-divinyl chlorophyllide a/chlorophyllide a reductase subunit X
Enzymes [BR:ko01000]
1. Oxidoreductases
1.3 Acting on the CH-CH group of donors
1.3.7 With an iron-sulfur protein as acceptor
1.3.7.14 3,8-divinyl chlorophyllide a reductase
K11333 bchX; 3,8-divinyl chlorophyllide a/chlorophyllide a reductase subunit X
1.3.7.15 chlorophyllide a reductase
K11333 bchX; 3,8-divinyl chlorophyllide a/chlorophyllide a reductase subunit X
A second nitrogenase-like enzyme for bacteriochlorophyll biosynthesis: reconstitution of chlorophyllide a reductase with purified X-protein (BchX) and YZ-protein (BchY-BchZ) from Rhodobacter capsulatus.
KEGG Orthology (KO) [BR:ko00001]
09100 Metabolism
09108 Metabolism of cofactors and vitamins
00860 Porphyrin metabolism
K11334 bchY; 3,8-divinyl chlorophyllide a/chlorophyllide a reductase subunit Y
Enzymes [BR:ko01000]
1. Oxidoreductases
1.3 Acting on the CH-CH group of donors
1.3.7 With an iron-sulfur protein as acceptor
1.3.7.14 3,8-divinyl chlorophyllide a reductase
K11334 bchY; 3,8-divinyl chlorophyllide a/chlorophyllide a reductase subunit Y
1.3.7.15 chlorophyllide a reductase
K11334 bchY; 3,8-divinyl chlorophyllide a/chlorophyllide a reductase subunit Y
A second nitrogenase-like enzyme for bacteriochlorophyll biosynthesis: reconstitution of chlorophyllide a reductase with purified X-protein (BchX) and YZ-protein (BchY-BchZ) from Rhodobacter capsulatus.
KEGG Orthology (KO) [BR:ko00001]
09100 Metabolism
09108 Metabolism of cofactors and vitamins
00860 Porphyrin metabolism
K11335 bchZ; 3,8-divinyl chlorophyllide a/chlorophyllide a reductase subunit Z
Enzymes [BR:ko01000]
1. Oxidoreductases
1.3 Acting on the CH-CH group of donors
1.3.7 With an iron-sulfur protein as acceptor
1.3.7.14 3,8-divinyl chlorophyllide a reductase
K11335 bchZ; 3,8-divinyl chlorophyllide a/chlorophyllide a reductase subunit Z
1.3.7.15 chlorophyllide a reductase
K11335 bchZ; 3,8-divinyl chlorophyllide a/chlorophyllide a reductase subunit Z
A second nitrogenase-like enzyme for bacteriochlorophyll biosynthesis: reconstitution of chlorophyllide a reductase with purified X-protein (BchX) and YZ-protein (BchY-BchZ) from Rhodobacter capsulatus.
3-deacetyl-3-vinylbacteriochlorophyllide a [CPD:C18152];
oxidized ferredoxin [iron-sulfur] cluster [CPD:C00139];
ADP [CPD:C00008];
phosphate [CPD:C00009];
bacteriochlorophyllide a [CPD:C18155];
3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a [CPD:C18153]
Product
chlorophyllide a [CPD:C02139];
reduced ferredoxin [iron-sulfur] cluster [CPD:C00138];
ATP [CPD:C00002];
H2O [CPD:C00001];
H+ [CPD:C00080];
3-acetyl-3-devinylchlorophyllide a;
3-devinyl-3-(1-hydroxyethyl)chlorophyllide a [CPD:C18154]
Comment
The enzyme, together with EC 1.1.1.396, bacteriochlorophyllide-a dehydrogenase, and EC 4.2.1.165, chlorophyllide-a 31-hydratase, is involved in the conversion of chlorophyllide a to bacteriochlorophyllide a. These enzymes can act in multiple orders, resulting in the formation of different intermediates, but the final product of the cumulative action of the three enzymes is always bacteriochlorophyllide a. This enzyme catalyses a trans-reduction of the B-ring; the product has the (7R,8R)-configuration. In addition, the enzyme has a latent activity of EC 1.3.7.13, 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (ferredoxin) [4]. The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase (EC 1.18.6.1), which catalyses an ATP-driven reduction.
History
EC 1.3.7.15 created 1965 as EC 1.3.99.35, modified 2012, transferred 2016 to EC 1.3.7.15
A second nitrogenase-like enzyme for bacteriochlorophyll biosynthesis: reconstitution of chlorophyllide a reductase with purified X-protein (BchX) and YZ-protein (BchY-BchZ) from Rhodobacter capsulatus.
Broadened Substrate Specificity of 3-Hydroxyethyl Bacteriochlorophyllide a Dehydrogenase (BchC) Indicates a New Route for the Biosynthesis of Bacteriochlorophyll a.
