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Information on EC 1.3.7.2 - 15,16-dihydrobiliverdin:ferredoxin oxidoreductase for references in articles please use BRENDA:EC1.3.7.2
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EC Tree
IUBMB Comments Catalyses the two-electron reduction of biliverdin IXalpha at the C15 methine bridge. It has been proposed that this enzyme and EC 1.3.7.3, phycoerythrobilin:ferredoxin oxidoreductase, function as a dual enzyme complex in the conversion of biliverdin IXalpha into phycoerythrobilin.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
15,16-DHBV:ferredoxin oxidoreductase, ferredoxin-dependent bilin reductase, ferredoxin:15,16-dihydrobiliverdin oxidoreductase, oxidoreductase, ferredoxin:15,16-dihydrobiliverdin, PebA,
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15,16-DHBV:ferredoxin oxidoreductase
ferredoxin-dependent bilin reductase
ferredoxin:15,16-dihydrobiliverdin oxidoreductase
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oxidoreductase, ferredoxin:15,16-dihydrobiliverdin
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15,16-DHBV:ferredoxin oxidoreductase
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15,16-DHBV:ferredoxin oxidoreductase
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ferredoxin-dependent bilin reductase
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ferredoxin-dependent bilin reductase
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PebA
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15,16-dihydrobiliverdin + oxidized ferredoxin = biliverdin IXalpha + reduced ferredoxin
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15,16-dihydrobiliverdin:ferredoxin oxidoreductase
Catalyses the two-electron reduction of biliverdin IXalpha at the C15 methine bridge. It has been proposed that this enzyme and EC 1.3.7.3, phycoerythrobilin:ferredoxin oxidoreductase, function as a dual enzyme complex in the conversion of biliverdin IXalpha into phycoerythrobilin.
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15,16-dihydrobiliverdin + oxidized ferrdoxin
biliverdin IXalpha + reduced ferrdoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
phycoerythrobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
biliverdin IXalpha + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
phytochromobilin + biliverdin IXa + reduced ferredoxin
phycoerythrobilin
additional information
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15,16-dihydrobiliverdin + oxidized ferrdoxin
biliverdin IXalpha + reduced ferrdoxin
the 15,16-DHBV:ferredoxin oxidoreductase PebA reduces biliverdin IXalpha at the C15–C16 double bond to produce 15,16-dihydrobiliverdin
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15,16-dihydrobiliverdin + oxidized ferrdoxin
biliverdin IXalpha + reduced ferrdoxin
the 15,16-DHBV:ferredoxin oxidoreductase PebA reduces biliverdin IXalpha at the C15–C16 double bond to produce 15,16-dihydrobiliverdin, assay under anaerobic conditions
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15,16-dihydrobiliverdin + oxidized ferrdoxin
biliverdin IXalpha + reduced ferrdoxin
the 15,16-DHBV:ferredoxin oxidoreductase PebA reduces biliverdin IXalpha at the C15–C16 double bond to produce 15,16-dihydrobiliverdin
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15,16-dihydrobiliverdin + oxidized ferrdoxin
biliverdin IXalpha + reduced ferrdoxin
the 15,16-DHBV:ferredoxin oxidoreductase PebA reduces biliverdin IXalpha at the C15–C16 double bond to produce 15,16-dihydrobiliverdin, assay under anaerobic conditions
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15,16-dihydrobiliverdin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
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15,16-dihydrobiliverdin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
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15,16-dihydrobiliverdin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
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biosynthesis of bilin pigments, functions with EC1.3.7.3. as a dual enzyme complex in the conversion of biliverdin IXa into phycoerythrobilin
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15,16-dihydrobiliverdin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
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15,16-dihydrobiliverdin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
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biosynthesis of bilin pigments, functions with EC1.3.7.3. as a dual enzyme complex in the conversion of biliverdin IXa into phycoerythrobilin
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15,16-dihydrobiliverdin + reduced ferredoxin
phycoerythrobilin + oxidized ferredoxin
Q6UR88
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15,16-dihydrobiliverdin + reduced ferredoxin
phycoerythrobilin + oxidized ferredoxin
Q6UR88
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biliverdin IXa + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
Q6UR88
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biliverdin IXa + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
Q6UR88
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biliverdin IXa + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
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biliverdin IXa + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
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biliverdin IXalpha + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
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biliverdin IXalpha + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
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biliverdin IXalpha + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
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biliverdin IXalpha + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
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phytochromobilin + biliverdin IXa + reduced ferredoxin
phycoerythrobilin
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phytochromobilin + biliverdin IXa + reduced ferredoxin
phycoerythrobilin
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r
additional information
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does not convert 3E-phycocyanobilin
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additional information
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Q6UR88
does not convert 3E-phycocyanobilin
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additional information
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Q6UR88
does not convert 3E-phycocyanobilin
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additional information
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does not convert phycocyanobilin
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additional information
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does not convert phycocyanobilin
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15,16-dihydrobiliverdin + oxidized ferrdoxin
biliverdin IXalpha + reduced ferrdoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
biliverdin IXalpha + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
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15,16-dihydrobiliverdin + oxidized ferrdoxin
biliverdin IXalpha + reduced ferrdoxin
Q02189
the 15,16-DHBV:ferredoxin oxidoreductase PebA reduces biliverdin IXalpha at the C15–C16 double bond to produce 15,16-dihydrobiliverdin
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15,16-dihydrobiliverdin + oxidized ferrdoxin
biliverdin IXalpha + reduced ferrdoxin
Q02189
the 15,16-DHBV:ferredoxin oxidoreductase PebA reduces biliverdin IXalpha at the C15–C16 double bond to produce 15,16-dihydrobiliverdin
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15,16-dihydrobiliverdin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
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biosynthesis of bilin pigments, functions with EC1.3.7.3. as a dual enzyme complex in the conversion of biliverdin IXa into phycoerythrobilin
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15,16-dihydrobiliverdin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
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biosynthesis of bilin pigments, functions with EC1.3.7.3. as a dual enzyme complex in the conversion of biliverdin IXa into phycoerythrobilin
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NADPH
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reaction depends on NADPH regenerating system
Ferredoxin
Q6UR88
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NADP+
Q6UR88
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additional information
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insensitivity toward metal chelators like 0.01 mM EDTA, 0.005 mM o-phenanthroline, or 0.005 mM 2,2'-dipyridyl
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additional information
Q6UR88
insensitivity toward metal chelators like 0.01 mM EDTA, 0.005 mM o-phenanthroline, or 0.005 mM 2,2'-dipyridyl
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brenda
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Q6UR88
SwissProt
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Uniprot
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strain SS120, strain MED4
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Q6UR88
SwissProt
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UniProt
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gene pebA
UniProt
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strain WH8020, strain WH8102
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UniProt
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gene pebA
UniProt
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evolution
the enzyme belongs to 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 ferredoxin-dependent bilin reductase family. All members of the FDBR family are radical enzymes
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metabolism
PebB, phycoerythrobilinPEB:ferredoxin oxidoreductase, EC 1.3.7.3, acts in tandem with PebA, 15,16-DHBV:ferredoxin oxidoreductase, 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, phycoerythrobilinPEB:ferredoxin oxidoreductase, EC 1.3.7.3, acts in tandem with PebA, 15,16-DHBV:ferredoxin oxidoreductase, 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
the highly conserved aspartate residue Asp105 is 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 residue Asp105 is 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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PebA in complex with substrate biliverdin IXalpha, hanging drop vapour diffusion method, 12-20 mg/ml protein in 0.1 M HEPE, pH 7.0, and 28% PEG 4000, 18°C, X-ray diffraction structure determination and analysis at 1.55 A resolution
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D205N
site-directed mutagenesis, the mutant retains activity
D84E
site-directed mutagenesis, the mutant retains activity
D84N
site-directed mutagenesis, inactive mutant
D205N
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site-directed mutagenesis, the mutant retains activity
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D84E
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site-directed mutagenesis, the mutant retains activity
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D84N
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site-directed mutagenesis, inactive mutant
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by two affinity chromatography steps to 90% purity and a third gel filtration step
GST-tagged PebA forms inactive aggregates
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by two affinity chromatography steps to 90% purity and a third gel filtration step
Q6UR88
by two affinity chromatography steps to 90% purity and a third gel filtration step
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GST-tagged PebA forms inactive aggregates
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GST-tagged PebA forms inactive aggregates
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expressed in Escherichia coli
expressed using a tac promoter-driven N-terminal GST fusion protein
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expression in Escherichia coli
gene pebA, recombinant expression of wild-type and mutant enzymes, native and selenomethionine-labeled PebA
into pGEX-6P-3 vector for N-terminal fusion with glutathione S-transferase and transformed in Escherichia coli BL21(lambdaDE3) cells
Q6UR88
expressed in Escherichia coli
expressed in Escherichia coli
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expressed in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
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Frankenberg, N.; Mukougawa, K.; Kohchi, T.; Lagarias, J.C.
Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms
Plant Cell
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965-978
2001
Nostoc punctiforme (Q93TL6), Prochlorococcus sp., Synechococcus sp.
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Alvey, R.M.; Karty, J.A.; Roos, E.; Reilly, J.P.; Kehoe, D.M.
Lesions in phycoerythrin chromophore biosynthesis in Fremyella diplosiphon reveal coordinated light regulation of apoprotein and pigment biosynthetic enzyme gene expression
Plant Cell
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2448-2463
2003
Microchaete diplosiphon
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Dammeyer, T.; Frankenberg-Dinkel, N.
Insights into phycoerythrobilin biosynthesis point toward metabolic channeling
J. Biol. Chem.
281
27081-27089
2006
Microchaete diplosiphon, Microchaete diplosiphon (Q6UR88), Microchaete diplosiphon Fd33 (Q6UR88), Synechococcus sp., Synechococcus sp. WH8020
brenda
Busch, A.W.; Reijerse, E.J.; Lubitz, W.; Frankenberg-Dinkel, N.; Hofmann, E.
Structural and mechanistic insight into the ferredoxin-mediated two-electron reduction of bilins
Biochem. J.
439
257-264
2011
Synechococcus sp. (Q02189), Synechococcus sp., Synechococcus sp. WH8020 (Q02189)
brenda
Overkamp, K.; Gasper, R.; Kock, K.; Herrmann, C.; Hofmann, E.; Frankenberg-Dinkel, N.
Insights into the biosynthesis and assembly of cryptophycean phycobiliproteins
J. Biol. Chem.
289
26691-26707
2014
Guillardia theta, Synechococcus sp. (Q02189), Synechococcus sp. WH8020 (Q02189)
brenda
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1.3.7.2 15,16-dihydrobiliverdin:ferredoxin oxidoreductase
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