BRENDA - Enzyme Database
show all sequences of 1.3.7.13

Characterization of BciB a ferredoxin-dependent 8-vinyl-protochlorophyllide reductase from the green sulfur bacterium Chloroherpeton thalassium

Saunders, A.H.; Golbeck, J.H.; Bryant, D.A.; Biochemistry 52, 8442-8451 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene bciB, cloning in Escherichia coli strain JM109, recombinant expression of C-terminally His6-tagged in Escherichia coli strain BL21(DE3). Plasmid pET28-CthaBciB is cotransformed into strain BL21(DE3) along with the plasmid pDB1282, which contains the genes iscS, iscU, iscA, hscA, hscB, and fdx for Fe/S-cluster assembly from Azotobacter vinelandii under the control of an arabinose-inducible promoter to produce Escherichia coli strain AHS-1
Chloroherpeton thalassium
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
Chloroherpeton thalassium
-
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
?
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
Chloroherpeton thalassium ATCC 35110
-
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Chloroherpeton thalassium
B3QYX9
-
-
Chloroherpeton thalassium ATCC 35110
B3QYX9
-
-
Purification (Commentary)
Commentary
Organism
gene bciB, recombinant C-terminally His6-tagged from Escherichia coli strain AHS-1 under anaerobic conditions by cobalt affinity chromatography, ultrafiltration, and desalting gel filtration
Chloroherpeton thalassium
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
-
744314
Chloroherpeton thalassium
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
-
744314
Chloroherpeton thalassium ATCC 35110
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
-
?
additional information
using electrons provided by reduced ferredoxin or dithionite, recombinant BciB is active and reduced the 8-vinyl moiety of the substrate, 8-vinyl protochlorophyllide, producing protochlorophyllide a. BciB requires an additional electron donor, ferredoxin, together with NADPH
744314
Chloroherpeton thalassium
?
-
-
-
-
additional information
using electrons provided by reduced ferredoxin or dithionite, recombinant BciB is active and reduced the 8-vinyl moiety of the substrate, 8-vinyl protochlorophyllide, producing protochlorophyllide a. BciB requires an additional electron donor, ferredoxin, together with NADPH
744314
Chloroherpeton thalassium ATCC 35110
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 47000, recombinant His6-tagged enzyme, SDS-PAGE
Chloroherpeton thalassium
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
-
assay at room temperature
Chloroherpeton thalassium
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Chloroherpeton thalassium
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
recombinant BciB binds a flavin adenine dinucleotide cofactor
Chloroherpeton thalassium
additional information
BciB requires an additional electron donor, ferredoxin, together with NADPH
Chloroherpeton thalassium
NADPH
-
Chloroherpeton thalassium
[4Fe-4S] cluster
recombinant BciB binds two [4Fe-4S] clusters, one of which may not be essential for the activity of the enzyme, determined by EPR spectroscopy as well as quantitative analyses of bound iron and sulfide
Chloroherpeton thalassium
Cloned(Commentary) (protein specific)
Commentary
Organism
gene bciB, cloning in Escherichia coli strain JM109, recombinant expression of C-terminally His6-tagged in Escherichia coli strain BL21(DE3). Plasmid pET28-CthaBciB is cotransformed into strain BL21(DE3) along with the plasmid pDB1282, which contains the genes iscS, iscU, iscA, hscA, hscB, and fdx for Fe/S-cluster assembly from Azotobacter vinelandii under the control of an arabinose-inducible promoter to produce Escherichia coli strain AHS-1
Chloroherpeton thalassium
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
recombinant BciB binds a flavin adenine dinucleotide cofactor
Chloroherpeton thalassium
additional information
BciB requires an additional electron donor, ferredoxin, together with NADPH
Chloroherpeton thalassium
NADPH
-
Chloroherpeton thalassium
[4Fe-4S] cluster
recombinant BciB binds two [4Fe-4S] clusters, one of which may not be essential for the activity of the enzyme, determined by EPR spectroscopy as well as quantitative analyses of bound iron and sulfide
Chloroherpeton thalassium
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
Chloroherpeton thalassium
-
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
?
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
Chloroherpeton thalassium ATCC 35110
-
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
gene bciB, recombinant C-terminally His6-tagged from Escherichia coli strain AHS-1 under anaerobic conditions by cobalt affinity chromatography, ultrafiltration, and desalting gel filtration
Chloroherpeton thalassium
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
-
744314
Chloroherpeton thalassium
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
-
744314
Chloroherpeton thalassium ATCC 35110
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
-
?
additional information
using electrons provided by reduced ferredoxin or dithionite, recombinant BciB is active and reduced the 8-vinyl moiety of the substrate, 8-vinyl protochlorophyllide, producing protochlorophyllide a. BciB requires an additional electron donor, ferredoxin, together with NADPH
744314
Chloroherpeton thalassium
?
-
-
-
-
additional information
using electrons provided by reduced ferredoxin or dithionite, recombinant BciB is active and reduced the 8-vinyl moiety of the substrate, 8-vinyl protochlorophyllide, producing protochlorophyllide a. BciB requires an additional electron donor, ferredoxin, together with NADPH
744314
Chloroherpeton thalassium ATCC 35110
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 47000, recombinant His6-tagged enzyme, SDS-PAGE
Chloroherpeton thalassium
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
22
-
assay at room temperature
Chloroherpeton thalassium
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Chloroherpeton thalassium
General Information
General Information
Commentary
Organism
additional information
structural modeling of BciB based on a structure for the FrhB subunit of F420-reducing [NiFe]-hydrogenase of Methanothermobacter marburgensis, overview
Chloroherpeton thalassium
General Information (protein specific)
General Information
Commentary
Organism
additional information
structural modeling of BciB based on a structure for the FrhB subunit of F420-reducing [NiFe]-hydrogenase of Methanothermobacter marburgensis, overview
Chloroherpeton thalassium
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
1
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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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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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737646
Canniffe
Elucidation of the preferred r ...
Synechocystis sp.
Biochem. J.
462
433-440
2014
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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
-
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1
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4
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1
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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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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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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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