Cloned (Comment) | Organism |
---|---|
gene pebB, recombinant expression of wild-type and mutant enzymes | Synechococcus sp. |
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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Synechococcus sp. | - |
gene pebB | - |
Synechococcus sp. WH8020 | - |
gene pebB | - |
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 | Comment | Organism |
---|---|---|
PEB:ferredoxin oxidoreductase | - |
Synechococcus sp. |
PebB | - |
Synechococcus sp. |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
20 | - |
assay at | Synechococcus sp. |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
Ferredoxin | - |
Synechococcus sp. |
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. |