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Literature summary for 1.3.7.3 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 pebB, recombinant expression of wild-type and mutant enzymes Synechococcus sp.

Protein Variants

Protein Variants Comment Organism
D107E site-directed mutagenesis, the mutant retains activity Synechococcus sp.
D107N site-directed mutagenesis, inactive mutant Synechococcus sp.
D231E site-directed mutagenesis, the mutant retains activity Synechococcus sp.
D231N site-directed mutagenesis, inactive mutant Synechococcus sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(3Z)-phycoerythrobilin + oxidized ferredoxin Synechococcus sp.
-
15,16-dihydrobiliverdin + reduced ferredoxin
-
?
(3Z)-phycoerythrobilin + oxidized ferredoxin Synechococcus sp. WH8020
-
15,16-dihydrobiliverdin + reduced ferredoxin
-
?

Organism

Organism UniProt Comment Textmining
Synechococcus sp.
-
gene pebB
-
Synechococcus sp. WH8020
-
gene pebB
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(3Z)-phycoerythrobilin + oxidized ferredoxin
-
Synechococcus sp. 15,16-dihydrobiliverdin + reduced ferredoxin
-
?
(3Z)-phycoerythrobilin + oxidized ferredoxin
-
Synechococcus sp. WH8020 15,16-dihydrobiliverdin + reduced ferredoxin
-
?

Synonyms

Synonyms Comment Organism
PEB:ferredoxin oxidoreductase
-
Synechococcus sp.
PebB
-
Synechococcus sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
assay at Synechococcus sp.

Cofactor

Cofactor Comment Organism Structure
Ferredoxin
-
Synechococcus sp.

General Information

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