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EC Tree
IUBMB Comments Catalyses the two-electron reduction of the C2 and C31
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
ferredoxin:3Z-phycoerythrobilin oxidoreductase, oxidoreductase, ferredoxin:3Z-phycoerythrobilin, PEB:ferredoxin oxidoreductase, PebB,
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ferredoxin:3Z-phycoerythrobilin oxidoreductase
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oxidoreductase, ferredoxin:3Z-phycoerythrobilin
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PEB:ferredoxin oxidoreductase
PEB:ferredoxin oxidoreductase
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PEB:ferredoxin oxidoreductase
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PebB
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(3Z)-phycoerythrobilin + oxidized ferredoxin = 15,16-dihydrobiliverdin + reduced ferredoxin
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(3Z)-phycoerythrobilin:ferredoxin oxidoreductase
Catalyses the two-electron reduction of the C2 and C31
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(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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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(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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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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(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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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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(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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(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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NADPH
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reaction depends on NADPH regenerating system
Ferredoxin
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NADP+
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brenda
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SwissProt
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Uniprot
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strain SS120, strain MED4
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brenda
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brenda
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SwissProt
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gene pebB
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strain WH8020, strain WH8102
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brenda
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gene pebB
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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
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
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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D107E
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site-directed mutagenesis, the mutant retains activity
D107N
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site-directed mutagenesis, inactive mutant
D231E
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site-directed mutagenesis, the mutant retains activity
D231N
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site-directed mutagenesis, inactive mutant
D107E
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site-directed mutagenesis, the mutant retains activity
D107N
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site-directed mutagenesis, inactive mutant
D231E
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site-directed mutagenesis, the mutant retains activity
D231N
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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
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GST-tagged PebA forms inactive aggregates
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expressed using a tac promoter-driven N-terminal GST fusion protein
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expression in Escherichia coli
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gene pebB, recombinant expression of wild-type and mutant enzymes
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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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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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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
Prochlorococcus sp., Synechococcus sp., Nostoc punctiforme (Q93TM8)
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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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Mukougawa, K.; Kanamoto, H.; Kobayashi, T.; Yokota, A.; Kohchi, T.
Metabolic engineering to produce phytochromes with phytochromobilin, phycocyanobilin, or phycoerythrobilin chromophore in Escherichia coli
FEBS Lett.
580
1333-1338
2006
Synechococcus sp., Synechococcus sp. W8020
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Dammeyer, T.; Frankenberg-Dinkel, N.
Insights into phycoerythrobilin biosynthesis point toward metabolic channeling
J. Biol. Chem.
281
27081-27089
2006
Synechococcus sp., Microchaete diplosiphon (Q6UR87), Microchaete diplosiphon, Synechococcus sp. WH8020, Microchaete diplosiphon Fd33 (Q6UR87)
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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., Synechococcus sp. WH8020
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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
brenda
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1.3.7.3 phycoerythrobilin:ferredoxin oxidoreductase
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