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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-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 C15C16 double bond to produce 15,16-dihydrobiliverdin
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r
15,16-dihydrobiliverdin + oxidized ferrdoxin
biliverdin IXalpha + reduced ferrdoxin
the 15,16-DHBV:ferredoxin oxidoreductase PebA reduces biliverdin IXalpha at the C15C16 double bond to produce 15,16-dihydrobiliverdin, assay under anaerobic conditions
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r
15,16-dihydrobiliverdin + oxidized ferrdoxin
biliverdin IXalpha + reduced ferrdoxin
the 15,16-DHBV:ferredoxin oxidoreductase PebA reduces biliverdin IXalpha at the C15C16 double bond to produce 15,16-dihydrobiliverdin
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r
15,16-dihydrobiliverdin + oxidized ferrdoxin
biliverdin IXalpha + reduced ferrdoxin
the 15,16-DHBV:ferredoxin oxidoreductase PebA reduces biliverdin IXalpha at the C15C16 double bond to produce 15,16-dihydrobiliverdin, assay under anaerobic conditions
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r
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
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r
15,16-dihydrobiliverdin + reduced ferredoxin
phycoerythrobilin + oxidized ferredoxin
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r
biliverdin IXa + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
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r
biliverdin IXa + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
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r
biliverdin IXa + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
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r
biliverdin IXa + reduced ferredoxin
15,16-dihydrobiliverdin + oxidized ferredoxin
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r
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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r
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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does not convert 3E-phycocyanobilin
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additional information
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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
the 15,16-DHBV:ferredoxin oxidoreductase PebA reduces biliverdin IXalpha at the C15C16 double bond to produce 15,16-dihydrobiliverdin
-
-
r
15,16-dihydrobiliverdin + oxidized ferrdoxin
biliverdin IXalpha + reduced ferrdoxin
the 15,16-DHBV:ferredoxin oxidoreductase PebA reduces biliverdin IXalpha at the C15C16 double bond to produce 15,16-dihydrobiliverdin
-
-
r
15,16-dihydrobiliverdin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
biosynthesis of bilin pigments, functions with EC1.3.7.3. as a dual enzyme complex in the conversion of biliverdin IXa into phycoerythrobilin
-
-
?
15,16-dihydrobiliverdin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
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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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
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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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
13
965-978
2001
Prochlorococcus sp., Synechococcus sp., Nostoc punctiforme (Q93TL6)
brenda
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
15
2448-2463
2003
Microchaete diplosiphon
brenda
Dammeyer, T.; Frankenberg-Dinkel, N.
Insights into phycoerythrobilin biosynthesis point toward metabolic channeling
J. Biol. Chem.
281
27081-27089
2006
Synechococcus sp., Microchaete diplosiphon (Q6UR88), Microchaete diplosiphon, Synechococcus sp. WH8020, Microchaete diplosiphon Fd33 (Q6UR88)
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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History
1.3.7.2 15,16-dihydrobiliverdin:ferredoxin oxidoreductase
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