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Enzyme Nomenclature
Information on EC 1.3.7.3 - phycoerythrobilin:ferredoxin oxidoreductase
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.3.7.3
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RECOMMENDED NAME
GeneOntology No.
phycoerythrobilin:ferredoxin oxidoreductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(3Z)-phycoerythrobilin + oxidized ferredoxin = 15,16-dihydrobiliverdin + reduced ferredoxin
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
(3Z)-phycoerythrobilin:ferredoxin oxidoreductase
Catalyses the two-electron reduction of the C2 and C31 diene system of 15,16-dihydrobiliverdin. Specific for 15,16-dihydrobiliverdin. It has been proposed that this enzyme and EC 1.3.7.2, 15,16-dihydrobiliverdin:ferredoxin oxidoreductase, function as a dual enzyme complex in the conversion of biliverdin IXalpha to phycoerythrobilin.
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CAS REGISTRY NUMBER
COMMENTARY
347401-21-2
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
additional information
evolution
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the enzyme belongs to the the ferredoxin-dependent bilin reductase family. All members of the FDBR family are radical enzymes
evolution
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the enzyme belongs to the the ferredoxin-dependent bilin reductase family. All members of the FDBR family are radical enzymes
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metabolism
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PebB, i.e. phycoerythrobilinPEB:ferredoxin oxidoreductase, acts in tandem with PebA, i.e. 15,16-DHBV:ferredoxin oxidoreductase, EC 1.3.7.2, which reduces biliverdin IXalpha at the C15-C16 double bond to produce 15,16-dihydrobiliverdin. Both enzymes function in close contact for metabolic channeling of 15,16-dihydrobiliverdin
metabolism
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PebB, i.e. phycoerythrobilinPEB:ferredoxin oxidoreductase, acts in tandem with PebA, i.e. 15,16-DHBV:ferredoxin oxidoreductase, EC 1.3.7.2, which reduces biliverdin IXalpha at the C15-C16 double bond to produce 15,16-dihydrobiliverdin. Both enzymes function in close contact for metabolic channeling of 15,16-dihydrobiliverdin
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additional information
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the highly conserved aspartate residues Asp107 and Asp231 are critical for the reduction. In addition to the importance of certain catalytic residues, the shape of the active site and consequently the binding of the substrate highly determines the catalytic properties
additional information
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the highly conserved aspartate residues Asp107 and Asp231 are critical for the reduction. In addition to the importance of certain catalytic residues, the shape of the active site and consequently the binding of the substrate highly determines the catalytic properties
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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enzyme acts via a substrate radical mechanism. No substrate: biliverdin IXalpha
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(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
3E-isomer occurs by non-enzyme-mediated side reaction caused by heat and reduced gluthathione
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-
?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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3E-isomer occurs by non-enzyme-mediated side reaction caused by heat and reduced gluthathione
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?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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biosynthesis of bilin pigments, functions with EC1.3.7.2. as a dual enzyme complex in the conversion of biliverdin Ixa into phycoerythrobilin
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?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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-
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?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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3E-isomer occurs by non-enzyme-mediated side reaction caused by heat and reduced gluthathione
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-
?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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biosynthesis of bilin pigments, functions with EC1.3.7.2. as a dual enzyme complex in the conversion of biliverdin Ixa into phycoerythrobilin
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?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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r
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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r
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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-
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r
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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r
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
Q93TM8
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?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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biosynthesis of bilin pigments, functions with EC1.3.7.2. as a dual enzyme complex in the conversion of biliverdin Ixa into phycoerythrobilin
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-
?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
-
-
-
-
?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
-
biosynthesis of bilin pigments, functions with EC1.3.7.2. as a dual enzyme complex in the conversion of biliverdin Ixa into phycoerythrobilin
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by two affinity chromatography steps to 90% purity and a third gel filtration step
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
into pASK-IBA45+ and transformed in Escherichia coli DH10B cells
into vector pKT270, co-expression with cyanobacterial phytochrome 1 in Escherichia coli JM109
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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metabolic engineering of bacteria for the production of various bilins for assembly into phytochromes will facilitate the molecular analysis of photoreceptors
additional information
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metabolic engineering of bacteria for the production of various bilins for assembly into phytochromes will facilitate the molecular analysis of photoreceptors
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LINKS TO OTHER DATABASES (specific for EC-Number 1.3.7.3)
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