BRENDA - Enzyme Database
show all sequences of 1.3.7.4

Electrostatic interaction of phytochromobilin synthase and ferredoxin for biosynthesis of phytochrome chromophore

Chiu, F.Y.; Chen, Y.R.; Tu, S.L.; J. Biol. Chem. 285, 5056-5065 (2010)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
E110Q
site-directed mutagenesis, the mutant shows 321.7% of wild-type activity
Arabidopsis thaliana
E187Q
site-directed mutagenesis, the mutant shows 20.3% of wild-type activity
Arabidopsis thaliana
H259Q
site-directed mutagenesis, the mutant shows 123.4% of wild-type activity
Arabidopsis thaliana
K183Q
site-directed mutagenesis, the mutant shows 24.6% of wild-type activity
Arabidopsis thaliana
K255Q
site-directed mutagenesis, the mutant shows 11.7% of wild-type activity
Arabidopsis thaliana
K263Q
site-directed mutagenesis, the mutant shows 25.8% of wild-type activity
Arabidopsis thaliana
R200Q
site-directed mutagenesis, the mutant shows 12.5% of wild-type activity
Arabidopsis thaliana
R200Q/R264Q
site-directed mutagenesis, the mutant shows 11.9% of wild-type activity
Arabidopsis thaliana
R264Q
site-directed mutagenesis, the mutant shows 18.9% of wild-type activity
Arabidopsis thaliana
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
cofactor ferredoxin
Arabidopsis thaliana
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
biliverdin IXalpha + reduced ferredoxin
Arabidopsis thaliana
-
(3Z)-phytochromobilin + oxidized ferredoxin
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Arabidopsis thaliana
Q9SR43
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
biliverdin IXalpha + reduced ferredoxin
-
712484
Arabidopsis thaliana
(3Z)-phytochromobilin + oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + reduced ferredoxin
conserved surface-charged residues on HY2 and Arabidopsis ferredoxin AtFd2 are important in the protein-protein interaction as well as biliverdin reduction activity of HY2, mutational analysis, overview. The C12 propionate group of biliverdin is important for HY2-catalyzed biliverdin reduction
712484
Arabidopsis thaliana
(3Z)-phytochromobilin + oxidized ferredoxin
-
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Arabidopsis thaliana
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
assay at
Arabidopsis thaliana
Cofactor
Cofactor
Commentary
Organism
Structure
Ferredoxin
one of the six Arabidopsis ferredoxins, AtFd2, is the preferred electron donor for HY2. Activity with ferredoxin AtFd2 mutants D78N, E81Q, E82Q, Y89F, R92Q, and D112N, overview
Arabidopsis thaliana
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
Ferredoxin
one of the six Arabidopsis ferredoxins, AtFd2, is the preferred electron donor for HY2. Activity with ferredoxin AtFd2 mutants D78N, E81Q, E82Q, Y89F, R92Q, and D112N, overview
Arabidopsis thaliana
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
E110Q
site-directed mutagenesis, the mutant shows 321.7% of wild-type activity
Arabidopsis thaliana
E187Q
site-directed mutagenesis, the mutant shows 20.3% of wild-type activity
Arabidopsis thaliana
H259Q
site-directed mutagenesis, the mutant shows 123.4% of wild-type activity
Arabidopsis thaliana
K183Q
site-directed mutagenesis, the mutant shows 24.6% of wild-type activity
Arabidopsis thaliana
K255Q
site-directed mutagenesis, the mutant shows 11.7% of wild-type activity
Arabidopsis thaliana
K263Q
site-directed mutagenesis, the mutant shows 25.8% of wild-type activity
Arabidopsis thaliana
R200Q
site-directed mutagenesis, the mutant shows 12.5% of wild-type activity
Arabidopsis thaliana
R200Q/R264Q
site-directed mutagenesis, the mutant shows 11.9% of wild-type activity
Arabidopsis thaliana
R264Q
site-directed mutagenesis, the mutant shows 18.9% of wild-type activity
Arabidopsis thaliana
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
cofactor ferredoxin
Arabidopsis thaliana
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
biliverdin IXalpha + reduced ferredoxin
Arabidopsis thaliana
-
(3Z)-phytochromobilin + oxidized ferredoxin
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
biliverdin IXalpha + reduced ferredoxin
-
712484
Arabidopsis thaliana
(3Z)-phytochromobilin + oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + reduced ferredoxin
conserved surface-charged residues on HY2 and Arabidopsis ferredoxin AtFd2 are important in the protein-protein interaction as well as biliverdin reduction activity of HY2, mutational analysis, overview. The C12 propionate group of biliverdin is important for HY2-catalyzed biliverdin reduction
712484
Arabidopsis thaliana
(3Z)-phytochromobilin + oxidized ferredoxin
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
25
-
assay at
Arabidopsis thaliana
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
assay at
Arabidopsis thaliana
General Information
General Information
Commentary
Organism
physiological function
HY2 synthesizes the open chain tetrapyrrole chromophore for light-sensing phytochromes. It catalyzes the double bond reduction of a heme-derived tetrapyrrole intermediate biliverdin IXalpha at the A-ring diene system
Arabidopsis thaliana
General Information (protein specific)
General Information
Commentary
Organism
physiological function
HY2 synthesizes the open chain tetrapyrrole chromophore for light-sensing phytochromes. It catalyzes the double bond reduction of a heme-derived tetrapyrrole intermediate biliverdin IXalpha at the A-ring diene system
Arabidopsis thaliana
Other publictions for EC 1.3.7.4
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)
742513
Shin
Expression of recombinant ful ...
Arabidopsis thaliana
FEBS Lett.
588
2964-2970
2014
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1
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724317
Alvey
Attachment of noncognate chrom ...
Arabidopsis thaliana
Biochemistry
50
4890-4902
2011
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1
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8
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1
1
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725252
Alvey
Effects of modified phycobilin ...
Arabidopsis thaliana
J. Bacteriol.
193
1663-1671
2011
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1
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712484
Chiu
Electrostatic interaction of p ...
Arabidopsis thaliana
J. Biol. Chem.
285
5056-5065
2010
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9
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1
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4
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9
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1
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687760
Tu
Mechanistic studies of the phy ...
Arabidopsis thaliana
J. Biol. Chem.
283
27555-27564
2008
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1
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5
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2
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1
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1
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1
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5
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1
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685125
Tu
Insight into the radical mecha ...
Arabidopsis thaliana
Biochemistry
46
1484-1494
2007
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1
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1
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673636
Mukougawa
Metabolic engineering to produ ...
Escherichia coli
FEBS Lett.
580
1333-1338
2006
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1
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743476
Creff
Targeted Ds-tagging strategy ...
Arabidopsis thaliana
Plant Mol. Biol.
61
603-613
2006
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1
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1
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676460
Muramoto
The tomato photomorphogenetic ...
Solanum lycopersicum
Plant Cell Physiol.
46
661-665
2005
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657069
Sawers
The Elm1 (ZmHy2) gene of maize ...
Zea mays
Plant Physiol.
136
2771-2781
2004
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1
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1
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1
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5
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1
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437673
Frankenberg
Functional genomic analysis of ...
Arabidopsis thaliana
Plant Cell
13
965-978
2001
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1
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1
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6
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2
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437767
Kohchi
The Arabidopsis hy2 gene encod ...
Arabidopsis thaliana
Plant Cell
13
425-436
2001
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1
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2
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4
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437768
McDowell
Purification and biochemical p ...
Avena sativa
Plant Physiol.
126
1546-1554
2001
-
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3
1
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1
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4
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1
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1
1
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1
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1
1
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1
1
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437769
Terry
Holophytochrome assembly. Coup ...
Cucumis sativus
J. Biol. Chem.
266
22215-22221
1991
4
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3
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