Information on EC 1.14.15.20 - heme oxygenase (biliverdin-producing, ferredoxin)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

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EC NUMBER
COMMENTARY hide
1.14.15.20
-
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RECOMMENDED NAME
GeneOntology No.
heme oxygenase (biliverdin-producing, ferredoxin)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
protoheme + 6 reduced ferredoxin [iron-sulfur] cluster + 3 O2 + 6 H+ = biliverdin + Fe2+ + CO + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
show the reaction diagram
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
heme degradation II
-
-
Metabolic pathways
-
-
phycocyanobilin biosynthesis
-
-
phycoerythrobilin biosynthesis I
-
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phycoerythrobilin biosynthesis II
-
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phycourobilin biosynthesis
-
-
phycoviolobilin biosynthesis
-
-
phytochromobilin biosynthesis
-
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Porphyrin and chlorophyll metabolism
-
-
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SYSTEMATIC NAME
IUBMB Comments
protoheme,reduced ferredoxin:oxygen oxidoreductase (alpha-methene-oxidizing, hydroxylating)
The enzyme, found in plants, algae, and cyanobacteria, participates in the biosynthesis of phytochromobilin and phytobilins. The terminal oxygen atoms that are incorporated into the carbonyl groups of pyrrole rings A and B of biliverdin are derived from two separate oxygen molecules. The third oxygen molecule provides the oxygen atom that converts the alpha-carbon to CO. Unlike this enzyme, which uses ferredoxin as its electron donor, the electron source for the related mammalian enzyme (EC 1.14.14.18) is EC 1.6.2.4, NADPH---hemoprotein reductase.
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
initial step in the biosynthesis of functional open-chain tetrapyrroles
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
hemin + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
-
-
-
-
?
mesoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
mesobiliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
-
-
-
-
?
protoheme + 6 reduced ferredoxin [iron-sulfur] cluster + 3 O2 + 6 H+
biliverdin + Fe2+ + CO + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
show the reaction diagram
-
-
-
?
protoheme + reduced ferredoxin [iron-sulfur] cluster + H2O2 + H+
verdomheme + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
-
-
-
-
?
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
-
-
-
-
?
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
hemin + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
-
-
-
-
?
mesoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
mesobiliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
-
-
-
-
?
protoheme + 6 reduced ferredoxin [iron-sulfur] cluster + 3 O2 + 6 H+
biliverdin + Fe2+ + CO + 6 oxidized ferredoxin [iron-sulfur] cluster + 3 H2O
show the reaction diagram
P72849
-
-
-
?
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
-
-
-
-
?
protoheme + reduced ferredoxin [iron-sulfur] cluster + O2 + H+
biliverdin IXalpha + Fe2+ + CO + oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
heme
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the enzyme forms a 1:1 complex with heme
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Sn-protoporphyrin IX
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25% inhibition at 0.02 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4,5-dihydroxy-1,3-benzene disulfonic acid
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6-hydroxy-2,5,7,8-tetramethylchroman-2-carboxylic acid
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significantly increases enzyme activity
D-ascorbate
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99% activity with D-ascorbate as compared to L-ascorbate
dehydroascorbate
-
-
desferrioxamine
HClO4
-
134% activity at 5% (v/v) HClO4
isoascorbate
-
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L-ascorbate
o-phenanthroline
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-
Tiron
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almost as effective as desferrioxamine
additional information
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not activated by EDTA, dehydroascorbate, and phenyledediamine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0013
Hemin
-
at pH 7.2 and 25°C
0.0013 - 0.0057
protoheme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00069
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unpurified enzyme, at pH 7.6 and 42°C
0.1403
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after 203fold purification, at pH 7.6 and 42°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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isoform HO3
7.3
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isoforms HO4 and HY1
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 45
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the relative enzyme activity increases between 10°C and 45°C
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
isoforms HY1, HO3 and HO4
Manually annotated by BRENDA team
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53000
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-30°C, in 50 mM HEPES-NaOH (pH 7.2) with 40% (v/v) glycerol, at least 3 months, no loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Blue 2-Sepharose column chromatography, DEAE column chromatography, ferredoxin-Sepharose column chromatography, and Sephadex G-75 gel filtration
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ammonium sulfate precipitation, DE-52 column chromatography, and Sephadex G-75 gel filtration
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ammonium sulfate precipitation, Sephadex G-75 gel filtration , DE-52 column chromatography, and hydroxyapatite column chromatography
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partial purification by nickel chelating column chromatography
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Q sepharose column chromatography
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Talon-cobalt-affinity column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli and in an Arabidopsis thaliana hy1 mutant
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expressed in Escherichia coli BL21 cells
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expressed in Escherichia coli BL21(DE3) cells
expressed in Nicotiana benthamiana and Escherichia coli BL21 (DE3) cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression increases about 7fold during incubation of cells for 72 h in iron-deficient medium
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.15.20)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)