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Literature summary for 1.3.7.2 extracted from

  • 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 (2011), Biochem. J., 439, 257-264.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene pebA, recombinant expression of wild-type and mutant enzymes, native and selenomethionine-labeled PebA Synechococcus sp.

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Synechococcus sp.

Protein Variants

Protein Variants Comment Organism
D205N site-directed mutagenesis, the mutant retains activity Synechococcus sp.
D84E site-directed mutagenesis, the mutant retains activity Synechococcus sp.
D84N site-directed mutagenesis, inactive mutant Synechococcus sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
15,16-dihydrobiliverdin + oxidized ferrdoxin Synechococcus sp. the 15,16-DHBV:ferredoxin oxidoreductase PebA reduces biliverdin IXalpha at the C15–C16 double bond to produce 15,16-dihydrobiliverdin biliverdin IXalpha + reduced ferrdoxin
-
r
15,16-dihydrobiliverdin + oxidized ferrdoxin Synechococcus sp. WH8020 the 15,16-DHBV:ferredoxin oxidoreductase PebA reduces biliverdin IXalpha at the C15–C16 double bond to produce 15,16-dihydrobiliverdin biliverdin IXalpha + reduced ferrdoxin
-
r

Organism

Organism UniProt Comment Textmining
Synechococcus sp. Q02189 gene pebA
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Synechococcus sp. WH8020 Q02189 gene pebA
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
15,16-dihydrobiliverdin + oxidized ferrdoxin the 15,16-DHBV:ferredoxin oxidoreductase PebA reduces biliverdin IXalpha at the C15–C16 double bond to produce 15,16-dihydrobiliverdin Synechococcus sp. biliverdin IXalpha + reduced ferrdoxin
-
r
15,16-dihydrobiliverdin + oxidized 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 Synechococcus sp. biliverdin IXalpha + reduced ferrdoxin
-
r
15,16-dihydrobiliverdin + oxidized ferrdoxin the 15,16-DHBV:ferredoxin oxidoreductase PebA reduces biliverdin IXalpha at the C15–C16 double bond to produce 15,16-dihydrobiliverdin Synechococcus sp. WH8020 biliverdin IXalpha + reduced ferrdoxin
-
r
15,16-dihydrobiliverdin + oxidized 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 Synechococcus sp. WH8020 biliverdin IXalpha + reduced ferrdoxin
-
r

Synonyms

Synonyms Comment Organism
15,16-DHBV:ferredoxin oxidoreductase
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Synechococcus sp.
ferredoxin-dependent bilin reductase
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Synechococcus sp.
PebA
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Synechococcus sp.

Cofactor

Cofactor Comment Organism Structure
Ferredoxin
-
Synechococcus sp.

General Information

General Information Comment Organism
evolution the enzyme belongs to the ferredoxin-dependent bilin reductase family. All members of the FDBR family are radical enzymes Synechococcus sp.
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 Synechococcus sp.
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 Synechococcus sp.