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Information on EC 1.3.7.15 - chlorophyllide a reductase
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EC Tree
1.3.7.15 chlorophyllide a reductaseIUBMB Comments
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) . 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.
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Word Map
- 1.3.7.15
-
nitrogenase-like
- rhodobacter
- protochlorophyllide
- sphaeroides
- nitrogenase
-
anoxygenic
-
purple
-
8-vinyl
-
dark-operative
- capsulatus
-
b-producing
-
two-electron
-
methanogenic
- viridis
-
blastochloris
- tetrapyrrole
-
bchls
-
phototrophic
-
heterotetrameric
-
metalloenzyme
-
ethylidene
-
heliobacterium
- denitrificans
-
six-electron
-
subcomplexes
-
roseobacter
- modesticaldum
-
bacteriochlorin
-
light-harvesting
-
b-ring
-
monovinyl
-
molybdenum-containing
-
etiochloroplasts
-
nickel-containing
- a,c-diamide
-
holocomplex
-
chlide
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
2
+
+
=
+
2
+
+
+
2
+
2
oxidized ferredoxin [iron-sulfur] cluster
+
+
=
+
2
reduced ferredoxin [iron-sulfur] cluster
+
+
+
2
+
2
+
+
=
+
2
+
+
+
2
+
2
oxidized ferredoxin [iron-sulfur] cluster
+
+
=
+
2
reduced ferredoxin [iron-sulfur] cluster
+
+
+
2
+
2
+
+
=
+
2
+
+
+
2
+
2
oxidized ferredoxin [iron-sulfur] cluster
+
+
=
+
2
reduced ferredoxin [iron-sulfur] cluster
+
+
+
2
Synonyms
chlorophyllide a reductase, chlorophyllide oxidoreductase, chlorophyllide a oxidoreductase, cor 8vr, (bchy/bchz)2 protein, light-independent chlorophyllide reductase, bchxyz, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
a-COR
BchA
BchX
BchXYZ
BchY
BchZ
chlorophyllide a oxidoreductase
chlorophyllide oxidoreductase
chlorophyllide reductase
COR
COR 8VR
EC 1.3.99.35
-
-
formerly
-
light-independent chlorophyllide reductase
light-independent chlorophyllide reductase
A0A143BJ63; A0A143BQ39
-
light-independent chlorophyllide reductase
B0TBQ4; B0TBQ9; B0TBQ8
-
light-independent chlorophyllide reductase
Heliomicrobium modesticaldum ATCC 51547
B0TBQ4; B0TBQ9; B0TBQ8
-
-
light-independent chlorophyllide reductase
B0TBQ4; B0TBQ9; B0TBQ8
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-deacetyl-3-(1-hydroxyethyl)bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = 3-devinyl-3-(1-hydroxyethyl)chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
(3)
-
-
-
3-deacetyl-3-vinylbacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = 3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
(2)
-
-
-
3-deacetyl-3-vinylbacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
(1)
-
-
-
3-deacetyl-3-vinylbacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
binding of the substrate to (BchY/BchZ)2 is the initial step of COR catalysis, which is followed by formation of the ternary complex between (BchY/BchZ)2 and (BchX)2
P26277; Q16DU8; Q16DU7
3-deacetyl-3-vinylbacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate = chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
binding of the substrate to (BchY/BchZ)2 is the initial step of COR catalysis, which is followed by formation of the ternary complex between (BchY/BchZ)2 and (BchX)2
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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SYSTEMATIC NAME
IUBMB Comments
bacteriochlorophyllide-a:ferredoxin 7,8-oxidoreductase
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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
3-deacetyl-3-vinylbacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
bacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
3-acetyl-3-devinylchlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
-
-
-
-
?
chlorophyllide a + AH2 + ATP + H2O
3-deacetyl-3-vinylbacteriochlorophyllide a + A + ADP + phosphate
protochlorophyllide + reduced dithionite + ATP + H2O + H+
chlorophyllide a + oxidized dithionite + ADP + phosphate
-
-
-
-
?
protochlorophyllide + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
P26277; Q16DU8; Q16DU7
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
P26277; Q16DU8; Q16DU7
-
-
-
?
3-deacetyl-3-vinylbacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
-
-
-
-
?
3-deacetyl-3-vinylbacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
-
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
P26277; Q16DU8; Q16DU7
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
P26277; Q16DU8; Q16DU7
the substrate is purified from the Rhodobacter capsulatus strain CB1200
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
P26277; Q16DU8; Q16DU7
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
P26277; Q16DU8; Q16DU7
the substrate is purified from the Rhodobacter capsulatus strain CB1200
-
-
?
chlorophyllide a + AH2 + ATP + H2O
3-deacetyl-3-vinylbacteriochlorophyllide a + A + ADP + phosphate
-
-
-
-
?
chlorophyllide a + AH2 + ATP + H2O
3-deacetyl-3-vinylbacteriochlorophyllide a + A + ADP + phosphate
-
the enzyme catalyses trans-reduction of the B-ring of chlorophyllide a. The product has the (7R,8R)-configuration
-
-
?
additional information
?
-
holoenzyme is composed of subunits BchX, BchY, and BchZ, and reduces ring B of chlorophyllide a using NADH under anaerobic conditions. It generates superoxide at low O2 concentrations. Superoxide is generated not from FMN of reductase subunit BchX but from heme of subunit BchZ
-
-
?
additional information
?
-
-
holoenzyme is composed of subunits BchX, BchY, and BchZ, and reduces ring B of chlorophyllide a using NADH under anaerobic conditions. It generates superoxide at low O2 concentrations. Superoxide is generated not from FMN of reductase subunit BchX but from heme of subunit BchZ
-
-
?
additional information
?
-
holoenzyme is composed of subunits BchX, BchY, and BchZ, and reduces ring B of chlorophyllide a using NADH under anaerobic conditions. It generates superoxide at low O2 concentrations. Superoxide is generated not from FMN of reductase subunit BchX but from heme of subunit BchZ
-
-
?
additional information
?
-
enzyme COR has an alternative 8VR activity in addition to the B-ring C7=C8 double bond reduction activity, cf. EC 1.3.7.13 or EC 1.3.1.75
-
-
-
additional information
?
-
-
enzyme COR has an alternative 8VR activity in addition to the B-ring C7=C8 double bond reduction activity, cf. EC 1.3.7.13 or EC 1.3.1.75
-
-
-
additional information
?
-
enzyme COR has an alternative 8VR activity in addition to the B-ring C7=C8 double bond reduction activity, cf. EC 1.3.7.13 or EC 1.3.1.75
-
-
-
additional information
?
-
enzyme COR has an alternative 8VR activity in addition to the B-ring C7=C8 double bond reduction activity, cf. EC 1.3.7.13 or EC 1.3.1.75
-
-
-
additional information
?
-
enzyme COR has an alternative 8VR activity in addition to the B-ring C7=C8 double bond reduction activity, cf. EC 1.3.7.13 or EC 1.3.1.75
-
-
-
additional information
?
-
P26277; Q16DU8; Q16DU7
for the standard DPOR/COR activity assay, a cell-free Escherichia coli extract containing overproduced Chlorobaculum tepidum DPOR subunits, BchN, BchB and BchL, is used in combination with purified recombinant COR subcomplexes, BchX2 and (BchY/BchZ)2. When using the chemical reducing agent, dithionite, instead of the natural electron donor (which might be a ferredoxin), it is essential to conduct control reactions in the absence of BchX2 and (BchY/BchZ)2 to ensure the dependence of the observed COR activity on both protein subcomplexes. The maximum COR activity is only achieved using an optimal ratio between BchX2 and (BchY/BchZ)2. Protein-protein interaction of BchX2 and (BchY/BchZ)2 is investigated in the presence of an analogue of the cosubstrate ATP, MgADP-AlF4-. Assay method evaluation, overview
-
-
-
additional information
?
-
P26277; Q16DU8; Q16DU7
for the standard DPOR/COR activity assay, a cell-free Escherichia coli extract containing overproduced Chlorobaculum tepidum DPOR subunits, BchN, BchB and BchL, is used in combination with purified recombinant COR subcomplexes, BchX2 and (BchY/BchZ)2. When using the chemical reducing agent, dithionite, instead of the natural electron donor (which might be a ferredoxin), it is essential to conduct control reactions in the absence of BchX2 and (BchY/BchZ)2 to ensure the dependence of the observed COR activity on both protein subcomplexes. The maximum COR activity is only achieved using an optimal ratio between BchX2 and (BchY/BchZ)2. Protein-protein interaction of BchX2 and (BchY/BchZ)2 is investigated in the presence of an analogue of the cosubstrate ATP, MgADP-AlF4-. Assay method evaluation, overview
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
3-deacetyl-3-vinylbacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
bacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
3-acetyl-3-devinylchlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
-
-
-
-
?
chlorophyllide a + AH2 + ATP + H2O
3-deacetyl-3-vinylbacteriochlorophyllide a + A + ADP + phosphate
-
-
-
-
?
protochlorophyllide + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
P26277; Q16DU8; Q16DU7
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
P26277; Q16DU8; Q16DU7
-
-
-
?
3-deacetyl-3-vinylbacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
-
-
-
-
?
3-deacetyl-3-vinylbacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
-
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
P26277; Q16DU8; Q16DU7
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
P26277; Q16DU8; Q16DU7
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
P26277; Q16DU8; Q16DU7
sodium dithionite can substitute for ferredoxin as electron donor
-
Fe-S center
a [4Fe-4S] cluster is bound at the interface between the BchX homodimer and the YZ protein of the COR enzyme complex
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8-vinyl chlorophyllide a
inhibitory effect of 8 V-Chlide on 3 V-BChlide production inhibitory effect of 8 V-Chlide on the C7=C8 reduction of COR
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
oligomeric BciA provides a kcat/Km value of 0.029/s * microM, which is 15fold higher than the value of a-COR towards Chlide a (0.0019/s * microM when the ratio of BchX:BchYZ is 4:1)
-
0.0014
8-vinyl chlorophyllide a
recombinant enzyme BchX/BchY, pH and temperature not specified in the publication
-
0.0059
8-vinyl chlorophyllide a
pH 8.0, 22°C, recombinant BchYZ heterodimer
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00027
8-vinyl chlorophyllide a
recombinant enzyme BchX/BchY, pH and temperature not specified in the publication
-
0.011
8-vinyl chlorophyllide a
pH 8.0, 22°C, recombinant BchYZ heterodimer
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.864
8-vinyl chlorophyllide a
pH 8.0, 22°C, recombinant BchYZ heterodimer
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
34
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
genes bchX, bchY, and bchZ
B0TBQ4; B0TBQ9; B0TBQ8
UniProt
brenda
Heliomicrobium modesticaldum ATCC 51547
genes bchX, bchY, and bchZ
B0TBQ4; B0TBQ9; B0TBQ8
UniProt
brenda
genes bchX, bchY, and bchZ
B0TBQ4; B0TBQ9; B0TBQ8
UniProt
brenda
genes bchX, bchY, and bchZ encoding the three subunits of the enzyme
UniProt
brenda
genes bchX, bchY, and bchZ encoding the three subunits of the enzyme
UniProt
brenda
genes bchX, bchY, and bchZ encoding the three subunits of the enzyme
UniProt
brenda
genes bchX, bchY, and bchZ encoding the three subunits of the enzyme
UniProt
brenda