BRENDA - Enzyme Database
show all sequences of 1.3.7.13

Elucidation of the preferred routes of C8-vinyl reduction in chlorophyll and bacteriochlorophyll biosynthesis

Canniffe, D.P.; Chidgey, J.W.; Hunter, C.N.; Biochem. J. 462, 433-440 (2014)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
additional information
generation of an enzyme BciB knockout mutant and recombinant expression of Rhodobacter sphaeroides gene bciA in the mutant
Synechocystis sp. PCC 6803
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Synechocystis sp. PCC 6803
16020
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
Synechocystis sp. PCC 6803
preferred substrate
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
?
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
Synechocystis sp. PCC 6803
is reduced only under conditions in which this pigment accumulates as a result of perturbed formation of chlorophyllide
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
?
additional information
Synechocystis sp. PCC 6803
although the native BciB is able to reduce the 8V group of Pchlide, the preferred substrate for this enzyme is 8V Chlide, with only a small amount of 8E Pchlide detected in the wild-type when grown under pigment accumulating conditions
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Synechocystis sp. PCC 6803
P74473
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
preferred substrate
744270
Synechocystis sp. PCC 6803
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
is reduced only under conditions in which this pigment accumulates as a result of perturbed formation of chlorophyllide
744270
Synechocystis sp. PCC 6803
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
-
?
additional information
although the native BciB is able to reduce the 8V group of Pchlide, the preferred substrate for this enzyme is 8V Chlide, with only a small amount of 8E Pchlide detected in the wild-type when grown under pigment accumulating conditions
744270
Synechocystis sp. PCC 6803
?
-
-
-
-
Cofactor
Cofactor
Commentary
Organism
Structure
ferredoxin [iron-sulfur] cluster
-
Synechocystis sp. PCC 6803
NADPH
-
Synechocystis sp. PCC 6803
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ferredoxin [iron-sulfur] cluster
-
Synechocystis sp. PCC 6803
NADPH
-
Synechocystis sp. PCC 6803
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
generation of an enzyme BciB knockout mutant and recombinant expression of Rhodobacter sphaeroides gene bciA in the mutant
Synechocystis sp. PCC 6803
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
membrane
-
Synechocystis sp. PCC 6803
16020
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
Synechocystis sp. PCC 6803
preferred substrate
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
?
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
Synechocystis sp. PCC 6803
is reduced only under conditions in which this pigment accumulates as a result of perturbed formation of chlorophyllide
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
?
additional information
Synechocystis sp. PCC 6803
although the native BciB is able to reduce the 8V group of Pchlide, the preferred substrate for this enzyme is 8V Chlide, with only a small amount of 8E Pchlide detected in the wild-type when grown under pigment accumulating conditions
?
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
preferred substrate
744270
Synechocystis sp. PCC 6803
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
is reduced only under conditions in which this pigment accumulates as a result of perturbed formation of chlorophyllide
744270
Synechocystis sp. PCC 6803
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
-
?
additional information
although the native BciB is able to reduce the 8V group of Pchlide, the preferred substrate for this enzyme is 8V Chlide, with only a small amount of 8E Pchlide detected in the wild-type when grown under pigment accumulating conditions
744270
Synechocystis sp. PCC 6803
?
-
-
-
-
General Information
General Information
Commentary
Organism
evolution
two unrelated classes of C8-vinyl reductase are known to exist, BciA and BciB
Synechocystis sp. PCC 6803
metabolism
the majority of (B)Chls utilized for light-harvesting carry an ethyl group at the C8 position (8E) of the macrocycle. This group is produced by the reduction of a vinyl group (8V), catalysed by an 8V reductase, 8VR, resulting in the production of an 8E pigment
Synechocystis sp. PCC 6803
additional information
BciB functions as an 8VR and does not require the presence of an additional subunit
Synechocystis sp. PCC 6803
General Information (protein specific)
General Information
Commentary
Organism
evolution
two unrelated classes of C8-vinyl reductase are known to exist, BciA and BciB
Synechocystis sp. PCC 6803
metabolism
the majority of (B)Chls utilized for light-harvesting carry an ethyl group at the C8 position (8E) of the macrocycle. This group is produced by the reduction of a vinyl group (8V), catalysed by an 8V reductase, 8VR, resulting in the production of an 8E pigment
Synechocystis sp. PCC 6803
additional information
BciB functions as an 8VR and does not require the presence of an additional subunit
Synechocystis sp. PCC 6803
Other publictions for EC 1.3.7.13
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
738542
Chen
Two unrelated 8-vinyl reductas ...
Acaryochloris marina
J. Bacteriol.
198
1393-1400
2016
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1
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1
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1
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1
1
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745221
Chen
Two unrelated 8-vinyl reducta ...
Acaryochloris marina, Acaryochloris marina MBIC11017
J. Bacteriol.
198
1393-1400
2016
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1
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2
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2
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2
1
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2
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1
2
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2
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2
1
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4
4
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728467
Ito
Evolution of a new chlorophyll ...
Synechocystis sp.
Plant Cell Physiol.
55
593-603
2014
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-
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1
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1
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1
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1
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736444
Harada
Chlorophyllide a oxidoreductas ...
no activity in Rhodobacter sphaeroides, Rhodopseudomonas palustris, Rhodopseudomonas palustris J1002
J. Biol. Chem.
289
12716-12726
2014
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3
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3
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3
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3
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3
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737646
Canniffe
Elucidation of the preferred r ...
Synechocystis sp.
Biochem. J.
462
433-440
2014
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1
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1
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1
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1
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1
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744270
Canniffe
Elucidation of the preferred ...
Synechocystis sp. PCC 6803
Biochem. J.
462
433-440
2014
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1
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1
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3
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1
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3
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2
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2
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1
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3
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3
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3
3
-
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746037
Ito
Evolution of a new chlorophyl ...
Synechocystis sp. PCC 6803
Plant Cell Physiol.
55
593-603
2014
-
-
1
-
-
-
-
-
-
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-
4
-
1
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5
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1
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1
1
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4
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5
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2
2
-
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-
737687
Saunders
Characterization of BciB: a fe ...
Chloroherpeton thalassium
Biochemistry
52
8442-8451
2013
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1
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1
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8
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1
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1
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2
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1
2
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1
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744314
Saunders
Characterization of BciB a fe ...
Chloroherpeton thalassium, Chloroherpeton thalassium ATCC 35110
Biochemistry
52
8442-8451
2013
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1
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2
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9
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1
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4
1
1
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1
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4
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1
4
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2
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1
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4
1
1
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1
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1
1
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738520
Liu
Multiple types of 8-vinyl redu ...
Chlorobium ferrooxidans, Chlorobium ferrooxidans DSM 13031, Chlorobium limicola, Chlorobium limicola DSM 245, Chlorobium phaeobacteroides, Chlorobium phaeobacteroides DSM 266, Chloroherpeton thalassium, Chloroherpeton thalassium ATCC 35110, Pelodictyon clathratiforme, Pelodictyon clathratiforme DSM 5477, Prosthecochloris aestuarii, Prosthecochloris aestuarii DSM 271
J. Bacteriol.
193
4996-4998
2011
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12
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13
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12
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12
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12
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