1.3.7.15: chlorophyllide a reductase
This is an abbreviated version!
For detailed information about chlorophyllide a reductase, go to the full flat file.
Word Map on EC 1.3.7.15
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1.3.7.15
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nitrogenase-like
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rhodobacter
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protochlorophyllide
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sphaeroides
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nitrogenase
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anoxygenic
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purple
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8-vinyl
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dark-operative
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capsulatus
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b-producing
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two-electron
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methanogenic
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viridis
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blastochloris
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tetrapyrrole
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bchls
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phototrophic
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heterotetrameric
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metalloenzyme
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ethylidene
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heliobacterium
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denitrificans
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six-electron
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subcomplexes
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roseobacter
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modesticaldum
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bacteriochlorin
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light-harvesting
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b-ring
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monovinyl
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molybdenum-containing
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etiochloroplasts
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nickel-containing
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a,c-diamide
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holocomplex
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chlide
- 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
Reaction
+ 2 oxidized ferredoxin [iron-sulfur] cluster + + = + 2 reduced ferredoxin [iron-sulfur] cluster + + + 2 H+
Synonyms
(BchY/BchZ)2 protein, a-COR, BchA, bchB, bchL, bchN, BchX, BchX/Y/Z, BchXYZ, BchY, BchZ, chlorophyllide a oxidoreductase, chlorophyllide oxidoreductase, chlorophyllide reductase, COR, COR 8VR, dark-operative protochlorophyllide oxidoreductase, DPOR, EC 1.3.99.35, light-independent chlorophyllide reductase
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Substrates Products
Substrates Products on EC 1.3.7.15 - chlorophyllide a reductase
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REACTION DIAGRAM
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
-
-
-
-
?
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+
-
-
-
-
?
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
-
-
?
3-deacetyl-3-vinylbacteriochlorophyllide a + A + ADP + phosphate
-
-
-
-
?
chlorophyllide a + AH2 + ATP + H2O
3-deacetyl-3-vinylbacteriochlorophyllide a + A + ADP + phosphate
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the enzyme catalyses trans-reduction of the B-ring of chlorophyllide a. The product has the (7R,8R)-configuration
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-
?
?
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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
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-
?
additional information
?
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-
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
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-
?
additional information
?
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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
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-
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additional information
?
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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
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-
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additional information
?
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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
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-
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additional information
?
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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
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-
-
additional information
?
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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
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-
-
additional information
?
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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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-
-
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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