Cloned (Comment) | Organism |
---|---|
gene pebA, recombinant expression of wild-type and mutant enzymes, native and selenomethionine-labeled PebA | Synechococcus sp. |
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 | 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 | 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 C15C16 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 C15C16 double bond to produce 15,16-dihydrobiliverdin | biliverdin IXalpha + reduced ferrdoxin | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Synechococcus sp. | Q02189 | gene pebA | - |
Synechococcus sp. WH8020 | Q02189 | gene pebA | - |
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 C15C16 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 C15C16 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 C15C16 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 C15C16 double bond to produce 15,16-dihydrobiliverdin, assay under anaerobic conditions | Synechococcus sp. WH8020 | biliverdin IXalpha + reduced ferrdoxin | - |
r |
Synonyms | Comment | Organism |
---|---|---|
15,16-DHBV:ferredoxin oxidoreductase | - |
Synechococcus sp. |
ferredoxin-dependent bilin reductase | - |
Synechococcus sp. |
PebA | - |
Synechococcus sp. |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
Ferredoxin | - |
Synechococcus sp. |
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. |