Information on EC 1.3.7.4 - phytochromobilin:ferredoxin oxidoreductase

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

EC NUMBER
COMMENTARY hide
1.3.7.4
-
RECOMMENDED NAME
GeneOntology No.
phytochromobilin:ferredoxin oxidoreductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(3Z)-phytochromobilin + 2 oxidized ferredoxin = biliverdin IXalpha + 2 reduced ferredoxin
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
phytochromobilin biosynthesis
-
-
Porphyrin and chlorophyll metabolism
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-
SYSTEMATIC NAME
IUBMB Comments
(3Z)-phytochromobilin:ferredoxin oxidoreductase
Catalyses the two-electron reduction of biliverdin IXalpha. Can use [2Fe-2S] ferredoxins from a number of sources as acceptor but not the [4Fe-4S] ferredoxin from Clostridium pasteurianum. The isomerization of (3Z)-phytochromobilin to (3E)-phytochromobilin is thought to occur prior to covalent attachment to apophytochrome in the plant cell cytoplasm. Flavodoxins can be used instead of ferredoxin.
CAS REGISTRY NUMBER
COMMENTARY hide
138263-99-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
oat
-
-
Manually annotated by BRENDA team
cucumber
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
aurea is a mutant of phytochromobilin synthase
Uniprot
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
synthesis of linear tetrapyrrole chromophores in cyanobacteria, algae, and plants, overview
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
show the reaction diagram
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXalpha + reduced ferredoxin
show the reaction diagram
-
-
-
-
?
biliverdin IXalpha + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
show the reaction diagram
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
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
show the reaction diagram
(3Z)-phytochromobilin + oxidized ferredoxin
biliverdin IXalpha + reduced ferredoxin
show the reaction diagram
-
-
-
-
?
biliverdin IXalpha + reduced ferredoxin
(3Z)-phytochromobilin + oxidized ferredoxin
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
-
cofactor ferredoxin
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
stimulates at 1 mM
NADH
-
stimulates slightly at 1 mM
NADPH
-
stimulates slightly at 1 mM
additional information
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NADPH regenerating system with glucose-6-phosphate and glucose-6-phosphate dehydrogenase stimulates
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012 - 0.0035
Ferredoxin
-
additional information
additional information
-
sub-micromolar Km for biliverdin IXa
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.67
biliverdin IXa
Avena sativa
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above
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000004
-
in etiolated plastids
0.0000011
-
specific activity of plastid protein
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3
-
assay at
8.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
-
SDS-PAGE
33000
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calculated from amino acid sequence, mature protein
33400
-
SDS-PAGE
38100
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calculated from amino acid sequence, precursor protein with putative N-terminal plastid transit peptide
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 29000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
50000fold
-
90% homogeneity
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HPLC Phenomenex Ultracarb reverse phase column chromatography
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recombinant ZmHy2
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Superdex 200 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
development of a system to produce phytochromobilin in Escherichia coli by coexpression of heme oxygenase and phytochromobilin:ferredoxin oxidoreductase in a single operon in conjunction with apophytochrome using two compatible plasmids
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expressed in Escherichia coli strain BL21
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expression in Nicotiana plumbaginifolia and Escherichia coli
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overexpression in Synechococcus sp. strain PCC 7002, from endogenous plasmid pAQ1 under the control of the Synechocystis sp. strain PCC 6803 cpcBA promoter, leads to overproduction of phytochromobilin, the cells show a phenotype only slightly less pigmented and blue-green than the wild-type, the strain producing phycobiliproteins carrying phytochromobilin grow much more slowly at low light intensity. Transformant colonies in which pcyA is inactivated in the HY2 overexpression background does not develop a chlorotic appearance, and segregation of the mutant and wild-type alleles is rapidly achieved
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recombinant functional expression of HT-HY2 in Escherichia coli with production of phytochromobilin, 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
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wild type and mutant allels
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D116N
-
mutant still retains the ability of substrate binding, but with only 1.5% relative activity of wild type protein
D146N
-
mutant completely loses catalytic activity and also the ability of biliverdin binding
D256E
-
mutant retains only partial activity
E110Q
-
site-directed mutagenesis, the mutant shows 321.7% of wild-type activity
E187Q
-
site-directed mutagenesis, the mutant shows 20.3% of wild-type activity
H259Q
-
site-directed mutagenesis, the mutant shows 123.4% of wild-type activity
K183Q
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site-directed mutagenesis, the mutant shows 24.6% of wild-type activity
K255Q
-
site-directed mutagenesis, the mutant shows 11.7% of wild-type activity
K263Q
-
site-directed mutagenesis, the mutant shows 25.8% of wild-type activity
N133
-
mutant produces only partial activity
R200Q
-
site-directed mutagenesis, the mutant shows 12.5% of wild-type activity
R200Q/R264Q
-
site-directed mutagenesis, the mutant shows 11.9% of wild-type activity
R252Q
-
mutant loses catalytic activity and the ability of substrate binding
R264Q
-
site-directed mutagenesis, the mutant shows 18.9% of wild-type activity