BRENDA - Enzyme Database
show all sequences of 1.14.15.20

Phycobilin biosynthesis: Reductant requirements and product identification for heme oxygenase from Cyanidium caldarium

Rhie, G.; Beale, S.; Arch. Biochem. Biophys. 320, 182-194 (1995)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
D-ascorbate
99% activity with D-ascorbate as compared to L-ascorbate
Cyanidium caldarium
desferrioxamine
6fold increase of activity in the presence of 2.5 mM desferrioxamine
Cyanidium caldarium
HClO4
134% activity at 5% (v/v) HClO4
Cyanidium caldarium
L-ascorbate
required for activity
Cyanidium caldarium
additional information
not activated by EDTA, dehydroascorbate, and phenyledediamine
Cyanidium caldarium
Tiron
almost as effective as desferrioxamine
Cyanidium caldarium
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
soluble
-
Cyanidium caldarium
-
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
Cyanidium caldarium
-
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Cyanidium caldarium
-
-
-
Purification (Commentary)
Commentary
Organism
ammonium sulfate precipitation, Blue 2-Sepharose column chromatography, DEAE column chromatography, ferredoxin-Sepharose column chromatography, and Sephadex G-75 gel filtration
Cyanidium caldarium
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.00069
-
unpurified enzyme, at pH 7.6 and 42C
Cyanidium caldarium
0.1403
-
after 203fold purification, at pH 7.6 and 42C
Cyanidium caldarium
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
-
737548
Cyanidium caldarium
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
D-ascorbate
99% activity with D-ascorbate as compared to L-ascorbate
Cyanidium caldarium
desferrioxamine
6fold increase of activity in the presence of 2.5 mM desferrioxamine
Cyanidium caldarium
HClO4
134% activity at 5% (v/v) HClO4
Cyanidium caldarium
L-ascorbate
required for activity
Cyanidium caldarium
additional information
not activated by EDTA, dehydroascorbate, and phenyledediamine
Cyanidium caldarium
Tiron
almost as effective as desferrioxamine
Cyanidium caldarium
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
soluble
-
Cyanidium caldarium
-
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
Cyanidium caldarium
-
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
ammonium sulfate precipitation, Blue 2-Sepharose column chromatography, DEAE column chromatography, ferredoxin-Sepharose column chromatography, and Sephadex G-75 gel filtration
Cyanidium caldarium
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.00069
-
unpurified enzyme, at pH 7.6 and 42C
Cyanidium caldarium
0.1403
-
after 203fold purification, at pH 7.6 and 42C
Cyanidium caldarium
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
-
737548
Cyanidium caldarium
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
-
-
-
?
Other publictions for EC 1.14.15.20
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)
725252
Alvey
Effects of modified phycobilin ...
Synechococcus sp.
J. Bacteriol.
193
1663-1671
2011
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702147
Gisk
Characterization of the heme o ...
Arabidopsis thaliana
Biochem. J.
425
425-434
2010
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1
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3
3
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737588
Gohya
Variation of the oxidation sta ...
Glycine max
Biochem. Biophys. Res. Commun.
376
293-298
2008
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739250
Dammeyer
Function and distribution of b ...
Synechocystis sp. PCC 6803
Photochem. Photobiol. Sci.
7
1121-1130
2008
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673571
Gohya
Spectroscopic characterization ...
Glycine max
FEBS J.
273
5384-5399
2006
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738200
Zhang
Protein expressed by the ho2 g ...
Synechocystis sp.
FEBS J.
272
1012-1022
2005
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1
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658647
Sugishima
Crystal structure of heme oxyg ...
Synechocystis sp.
Eur. J. Biochem.
271
4517-4525
2004
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739342
Muramoto
Expression and biochemical pro ...
Arabidopsis thaliana
Plant Physiol.
130
1958-1966
2002
8
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1
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6
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739736
Montgomery
Phytochrome ancestry: sensors ...
Agrobacterium tumefaciens, Anabaena sp., Anabaena sp. PCC 7120, Deinococcus radiodurans, Magnetospirillum magnetotacticum, no activity in Cytophaga hutchinsonii, Nostoc punctiforme, Prochlorococcus marinus subsp. pastoris str. CCMP1986, Prochlorococcus sp. MIT9319, Pseudomonas aeruginosa, Pseudomonas fluorescens, Pseudomonas putida, Pseudomonas putida KT 2240, Pseudomonas putida PRS1, Pseudomonas syringae, Rhodobacter sphaeroides, Rhodopseudomonas palustris, Synechocystis sp.
Trends Plant Sci.
7
357-366
2002
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739326
Willows
Phytobilin biosynthesis: The S ...
Synechocystis sp.
Plant Mol. Biol.
43
113-120
2000
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739302
Cornejo
Phytobilin biosynthesis: Cloni ...
Synechocystis sp. PCC 6803
Plant J.
15
99-107
1998
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737548
Rhie
Phycobilin biosynthesis: Reduc ...
Cyanidium caldarium
Arch. Biochem. Biophys.
320
182-194
1995
6
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738561
Beale
Biosynthesis of phycobilins. F ...
Cyanidium caldarium
J. Biol. Chem.
266
22328-22332
1991
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