BRENDA - Enzyme Database
show all sequences of 1.3.7.5

Structural basis for hydration dynamics in radical stabilization of bilin reductase mutants

Kohler, A.C.; Gae, D.D.; Richley, M.A.; Stoll, S.; Gunn, A.; Lim, S.; Martin, S.S.; Doukov, T.I.; Britt, R.D.; Ames, J.B.; Lagarias, J.C.; Fisher, A.J.; Biochemistry 49, 6206-6218 (2010)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression of mutant enzymes in Escherichia coli strain BL21(DE3)
Synechocystis sp.
Crystallization (Commentary)
Crystallization
Organism
purified recombinant mutant enzymes, hanging drop vapour diffusion method, dithionite-treated reduced D105N PcyA crystals from 1.45-1.8 M ammonium sulfate, 0.15-0.4 M NaCl, and 0.1 M HEPES, pH 7.0, dithionite-treated reduced H88Q PcyA crystals from 1.7-2.2 M ammonium sulfate, 0.26-0.32 M NaCl, and 0.1 M sodium cacodylate, pH 7.0, 20°C in the dark, cryoprotectant solution is consisting of 30% v/v ethylene glycol in mother liquor, X-ray diffraction structure determination and analysis at 1.5 A resolution
Synechocystis sp.
Engineering
Amino acid exchange
Commentary
Organism
D105N
site-directed mutagenesis
Synechocystis sp.
H88Q
site-directed mutagenesis
Synechocystis sp.
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
biliverdin Ixalpha + reduced ferredoxin
Synechocystis sp.
-
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Synechocystis sp.
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant mutant enzymes from Escherichia coli strain BL21(DE3) by cyanide affinity chromatography
Synechocystis sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
biliverdin Ixalpha + reduced ferredoxin
-
724288
Synechocystis sp.
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
both PcyA D105N and H88Q mutants adopt alpha/beta/alpha sandwich folds possessing a central seven-stranded antiparallel beta-sheet lying between four alpha-helixes on each side
Synechocystis sp.
Cofactor
Cofactor
Commentary
Organism
Structure
Ferredoxin
-
Synechocystis sp.
Cloned(Commentary) (protein specific)
Commentary
Organism
expression of mutant enzymes in Escherichia coli strain BL21(DE3)
Synechocystis sp.
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
Ferredoxin
-
Synechocystis sp.
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant mutant enzymes, hanging drop vapour diffusion method, dithionite-treated reduced D105N PcyA crystals from 1.45-1.8 M ammonium sulfate, 0.15-0.4 M NaCl, and 0.1 M HEPES, pH 7.0, dithionite-treated reduced H88Q PcyA crystals from 1.7-2.2 M ammonium sulfate, 0.26-0.32 M NaCl, and 0.1 M sodium cacodylate, pH 7.0, 20°C in the dark, cryoprotectant solution is consisting of 30% v/v ethylene glycol in mother liquor, X-ray diffraction structure determination and analysis at 1.5 A resolution
Synechocystis sp.
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D105N
site-directed mutagenesis
Synechocystis sp.
H88Q
site-directed mutagenesis
Synechocystis sp.
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
Synechocystis sp.
-
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant mutant enzymes from Escherichia coli strain BL21(DE3) by cyanide affinity chromatography
Synechocystis sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
biliverdin Ixalpha + reduced ferredoxin
-
724288
Synechocystis sp.
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
both PcyA D105N and H88Q mutants adopt alpha/beta/alpha sandwich folds possessing a central seven-stranded antiparallel beta-sheet lying between four alpha-helixes on each side
Synechocystis sp.
General Information
General Information
Commentary
Organism
metabolism
phycocyanobilin:ferredoxin oxidoreductase, PcyA, is a key enzyme in the biogenesis of heme-derived linear tetrapyrroles, phytobilins, it catalyzes the overall four-electron reduction of biliverdin IXalpha to phycocyanobilin, the common chromophore precursor for both classes of biliproteins
Synechocystis sp.
additional information
the interconversion occurs via semireduced bilin radical intermediates that are profoundly stabilized by selected mutations of two critical catalytic residues, Asp105 and His88. Mechanistic scheme for PcyA-mediated reduction of both vinyl groups of biliverdin wherein an axial water molecule, which prematurely binds and ejects from both mutants upon one electron reduction, is required for catalytic turnover of the semireduced state, structure-function relationship, overview
Synechocystis sp.
General Information (protein specific)
General Information
Commentary
Organism
metabolism
phycocyanobilin:ferredoxin oxidoreductase, PcyA, is a key enzyme in the biogenesis of heme-derived linear tetrapyrroles, phytobilins, it catalyzes the overall four-electron reduction of biliverdin IXalpha to phycocyanobilin, the common chromophore precursor for both classes of biliproteins
Synechocystis sp.
additional information
the interconversion occurs via semireduced bilin radical intermediates that are profoundly stabilized by selected mutations of two critical catalytic residues, Asp105 and His88. Mechanistic scheme for PcyA-mediated reduction of both vinyl groups of biliverdin wherein an axial water molecule, which prematurely binds and ejects from both mutants upon one electron reduction, is required for catalytic turnover of the semireduced state, structure-function relationship, overview
Synechocystis sp.
Other publictions for EC 1.3.7.5
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)
742318
Ceron-Carrasco
-
First computational step towa ...
Synechocystis sp. PCC 6803
Comput. Theoret. Chem.
1077
58-64
2016
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742524
Hagiwara
Atomic-resolution structure o ...
Synechocystis sp. PCC 6803
FEBS Lett.
590
3425-3434
2016
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1
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724131
Kabasakal
His74 conservation in the bili ...
Synechocystis sp.
Arch. Biochem. Biophys.
537
233-242
2013
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1
1
3
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3
3
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724317
Alvey
Attachment of noncognate chrom ...
Synechococcus sp., Synechococcus sp. 7002
Biochemistry
50
4890-4902
2011
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1
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10
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725252
Alvey
Effects of modified phycobilin ...
Synechococcus sp.
J. Bacteriol.
193
1663-1671
2011
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3
3
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711117
Wada
One residue substitution in Pc ...
Synechocystis sp.
Biochem. Biophys. Res. Commun.
402
373-377
2010
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1
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712411
Hagiwara
Structural insights into vinyl ...
Synechocystis sp.
J. Biol. Chem.
285
1000-1007
2010
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724287
Shang
Biliverdin amides reveal roles ...
Anabaena sp., Anabaena sp. PCC 7120
Biochemistry
49
6070-6082
2010
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724288
Kohler
Structural basis for hydration ...
Synechocystis sp.
Biochemistry
49
6206-6218
2010
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2
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696870
Zhang
Biosynthesis of fluorescent al ...
Synechocystis sp.
Biotechnol. Appl. Biochem.
52
135-140
2009
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1
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1
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698489
Stoll
Structure of the biliverdin ra ...
Nostoc sp. PCC 7120, Synechocystis sp.
J. Am. Chem. Soc.
131
1986-1995
2009
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3
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7
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712008
Okada
HO1 and PcyA proteins involved ...
Thermosynechococcus elongatus
FEBS Lett.
583
1251-1256
2009
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685125
Tu
Insight into the radical mecha ...
Nostoc sp. PCC 7120
Biochemistry
46
1484-1494
2007
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673636
Mukougawa
Metabolic engineering to produ ...
Synechococcus sp., Synechococcus sp. W8020
FEBS Lett.
580
1333-1338
2006
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1
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673657
Hagiwara
Induced-fitting and electrosta ...
Synechocystis sp.
FEBS Lett.
580
3823-3828
2006
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674669
Tu
A conserved histidine-aspartat ...
Nostoc sp.
J. Biol. Chem.
281
3127-3136
2006
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1
1
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16
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674771
Zhao
Chromophore attachment to phyc ...
Anabaena sp., Anabaena sp. PCC 7120
J. Biol. Chem.
281
8573-8581
2006
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676847
Hagiwara
Crystal structure of phycocyan ...
Synechocystis sp.
Proc. Natl. Acad. Sci. USA
103
27-32
2006
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1
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655796
Tu
Biliverdin reduction by cyanob ...
Anabaena sp.
J. Am. Chem. Soc.
126
8682-8693
2004
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1
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1
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657164
Kami
Complementation of phytochrome ...
Synechocystis sp.
Proc. Natl. Acad. Sci. USA
101
1099-1104
2004
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1
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656197
Frankenberg
Phycocyanobilin:ferredoxin oxi ...
Anabaena sp.
J. Biol. Chem.
278
9219-9226
2003
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Phycocyanobilin is the natural ...
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