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Literature summary for 1.3.7.2 extracted from

  • Sommerkamp, J.; Frankenberg-Dinkel, N.; Hofmann, E.
    Crystal structure of the first eukaryotic bilin reductase GtPEBB reveals a flipped binding mode of dihydrobiliverdin (2019), J. Biol. Chem., 294, 13889-13901 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.3.7.2

Cloned(Commentary)

Cloned (Comment) Organism
gene pebA, recombinant expression of GST-tagged enzyme in Escherichia coli Synechococcus sp. WH 8020

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ in cofactor ferredoxin Synechococcus sp. WH 8020

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
biliverdin IXalpha + reduced ferredoxin Synechococcus sp. WH 8020
-
 15,16-dihydrobiliverdin + oxidized ferredoxin
-
 ?

Organism

Organism UniProt Comment Textmining
Synechococcus sp. WH 8020 Q02189
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant GST-tagged enzyme from Escherichia coli by ultrafiltration, glutathione affinity chromatography, and gel filtration Synechococcus sp. WH 8020

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
biliverdin IXalpha + reduced ferredoxin
-
 Synechococcus sp. WH 8020 15,16-dihydrobiliverdin + oxidized ferredoxin
-
 ?

Synonyms

Synonyms Comment Organism
15,16-dihydrobiliverdin:ferredoxin oxidoreductase
-
 Synechococcus sp. WH 8020
DHBV:ferredoxin oxidoreductase
-
 Synechococcus sp. WH 8020
GtPEBA
-
 Synechococcus sp. WH 8020
PebA
-
 Synechococcus sp. WH 8020

Cofactor

Cofactor Comment Organism Structure
Ferredoxin ferredoxin from Synechococcus sp. PCC7002 is used in the enzyme assay Synechococcus sp. WH 8020

General Information

General Information Comment Organism
metabolism phycobilins are light-harvesting pigments of cyanobacteria, red algae, and cryptophytes. The biosynthesis of phycoerythrobilin (PEB) is catalyzed by the subsequent action of two ferredoxin-dependent bilin reductases (FDBRs). 15,16-Dihydrobiliverdin (DHBV):ferredoxin oxidoreductase (PebA) catalyzes the two-electron reduction of biliverdin IXalpha to 15,16-DHBV, and PEB:ferredoxin oxidoreductase (PebB) reduces this intermediate further to PEB. The biosynthetic intermediate DHBV is transferred via proximity channeling to PEB:ferredoxin oxidoreductase (PebB) Synechococcus sp. WH 8020
additional information structure comparisons of Synechococcus WH8020 PebA and Guillardia theta PebB, overview. The Asp-99/Asp-219 pair is structurally conserved in most FDBRs, while the corresponding residues are relevant for PebB, for PebA only the homologue of Asp99 (Asp84) is essential for catalytic activity. The homologue of Asp219 (Asp205) is not essential and is rotated out of the active site. PebB binds DHBV analogous to the binding of BV in PebA/PebS Synechococcus sp. WH 8020
physiological function phycobilins are light-harvesting pigments of cyanobacteria, red algae, and cryptophytes. The biosynthesis of phycoerythrobilin (PEB) is catalyzed by the subsequent action of two ferredoxin-dependent bilin reductases (FDBRs). 15,16-Dihydrobiliverdin (DHBV):ferredoxin oxidoreductase (PebA) catalyzes the two-electron reduction of biliverdin IXalpha to 15,16-DHBV, and PEB:ferredoxin oxidoreductase (PebB) reduces this intermediate further to PEB Synechococcus sp. WH 8020