BRENDA - Enzyme Database
show all sequences of 1.3.7.5

Attachment of noncognate chromophores to CpcA of Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002 by heterologous expression in Escherichia coli

Alvey, R.M.; Biswas, A.; Schluchter, W.M.; Bryant, D.A.; Biochemistry 50, 4890-4902 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
recombinant functional expression of PcyA in Escherichia coli with production of phycocyanobilin, functional co-expression with cyanobacterial heme oxygenase, and the phycocyanin alpha-subunit, CpcA, from Synechocystis sp. PCC 6803 or Synechococcus sp. PCC 7002, and with the phycocyanin alpha-subunit phycocyanobilin lyase, CpcE/CpcF, or the phycoerythrocyanin alpha-subunit phycocyanobilin isomerizing lyase, PecE/PecF, from Noctoc sp. PCC 7120. Production levels of fluorescent pigments and chromophore analysis, overview
Synechococcus sp.
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
biliverdin Ixalpha + reduced ferredoxin
Synechococcus sp.
-
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
?
biliverdin Ixalpha + reduced ferredoxin
Synechococcus sp. 7002
-
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Synechococcus sp.
-
-
-
Synechococcus sp. 7002
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
biliverdin Ixalpha + reduced ferredoxin
-
724317
Synechococcus sp.
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
?
biliverdin Ixalpha + reduced ferredoxin
-
724317
Synechococcus sp. 7002
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
Ferredoxin
-
Synechococcus sp.
Cloned(Commentary) (protein specific)
Commentary
Organism
recombinant functional expression of PcyA in Escherichia coli with production of phycocyanobilin, functional co-expression with cyanobacterial heme oxygenase, and the phycocyanin alpha-subunit, CpcA, from Synechocystis sp. PCC 6803 or Synechococcus sp. PCC 7002, and with the phycocyanin alpha-subunit phycocyanobilin lyase, CpcE/CpcF, or the phycoerythrocyanin alpha-subunit phycocyanobilin isomerizing lyase, PecE/PecF, from Noctoc sp. PCC 7120. Production levels of fluorescent pigments and chromophore analysis, overview
Synechococcus sp.
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
Ferredoxin
-
Synechococcus 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
Synechococcus sp.
-
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
?
biliverdin Ixalpha + reduced ferredoxin
Synechococcus sp. 7002
-
(3Z)-phycocyanobilin + 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
-
724317
Synechococcus sp.
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
?
biliverdin Ixalpha + reduced ferredoxin
-
724317
Synechococcus sp. 7002
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
?
General Information
General Information
Commentary
Organism
additional information
cyanobacteria utilize phycocyanobilin:ferredoxin oxidoreductase (PcyA) to perform a two-step reaction, the enzyme first reduces the 18-vinyl side chain of the D-ring and subsequently reduces the vinyl side chain of the pyrrole A ring to yield phycocyanobilin
Synechococcus sp.
General Information (protein specific)
General Information
Commentary
Organism
additional information
cyanobacteria utilize phycocyanobilin:ferredoxin oxidoreductase (PcyA) to perform a two-step reaction, the enzyme first reduces the 18-vinyl side chain of the D-ring and subsequently reduces the vinyl side chain of the pyrrole A ring to yield phycocyanobilin
Synechococcus 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
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First computational step towa ...
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742524
Hagiwara
Atomic-resolution structure o ...
Synechocystis sp. PCC 6803
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Synechocystis sp.
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1
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2
1
1
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1
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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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2
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10
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1
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2
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1
1
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725252
Alvey
Effects of modified phycobilin ...
Synechococcus sp.
J. Bacteriol.
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1663-1671
2011
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4
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3
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711117
Wada
One residue substitution in Pc ...
Synechocystis sp.
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402
373-377
2010
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1
1
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1
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712411
Hagiwara
Structural insights into vinyl ...
Synechocystis sp.
J. Biol. Chem.
285
1000-1007
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5
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3
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1
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1
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1
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3
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1
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1
1
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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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1
-
-
-
-
-
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2
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20
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1
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13
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2
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1
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1
1
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2
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1
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13
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2
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2
2
-
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-
724288
Kohler
Structural basis for hydration ...
Synechocystis sp.
Biochemistry
49
6206-6218
2010
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1
1
2
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1
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3
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1
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1
1
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2
2
-
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-
696870
Zhang
Biosynthesis of fluorescent al ...
Synechocystis sp.
Biotechnol. Appl. Biochem.
52
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2009
-
1
1
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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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2
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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1
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1
1
1
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1
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1
1
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685125
Tu
Insight into the radical mecha ...
Nostoc sp. PCC 7120
Biochemistry
46
1484-1494
2007
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1
5
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4
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1
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1
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1
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673636
Mukougawa
Metabolic engineering to produ ...
Synechococcus sp., Synechococcus sp. W8020
FEBS Lett.
580
1333-1338
2006
-
1
1
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2
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673657
Hagiwara
Induced-fitting and electrosta ...
Synechocystis sp.
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580
3823-3828
2006
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1
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674669
Tu
A conserved histidine-aspartat ...
Nostoc sp.
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281
3127-3136
2006
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1
1
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16
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1
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1
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1
1
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1
1
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16
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1
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1
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1
1
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674771
Zhao
Chromophore attachment to phyc ...
Anabaena sp., Anabaena sp. PCC 7120
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281
8573-8581
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1
1
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2
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676847
Hagiwara
Crystal structure of phycocyan ...
Synechocystis sp.
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103
27-32
2006
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1
1
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3
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1
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655796
Tu
Biliverdin reduction by cyanob ...
Anabaena sp.
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126
8682-8693
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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-
-
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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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1
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3
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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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1
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2
1
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5
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1
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1
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4
1
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437763
Tooley
Biosynthesis of the cyanobacte ...
Anabaena sp.
J. Bacteriol.
184
4666-4671
2002
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1
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1
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1
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437673
Frankenberg
Functional genomic analysis of ...
Anabaena sp., Nostoc punctiforme, Prochlorococcus sp., Prochlorococcus sp. CCMP1378 / MED4, Synechococcus sp., Synechococcus sp. WH8102, Synechocystis sp.
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965-978
2001
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5
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7
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437764
Tooley
Biosynthesis of a fluorescent ...
Synechocystis sp.
Proc. Natl. Acad. Sci. USA
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10560-10565
2001
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1
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4
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437765
Wu
Phycocyanobilin is the natural ...
Mesotaenium caldariorum
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25700-25705
1997
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