EC Number | Cloned (Comment) | Organism |
---|---|---|
1.3.7.2 | gene pebA, recombinant expression of wild-type and mutant enzymes, native and selenomethionine-labeled PebA | Synechococcus sp. |
1.3.7.3 | gene pebB, recombinant expression of wild-type and mutant enzymes | Synechococcus sp. |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.3.7.2 | 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. |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.3.7.2 | D205N | site-directed mutagenesis, the mutant retains activity | Synechococcus sp. |
1.3.7.2 | D84E | site-directed mutagenesis, the mutant retains activity | Synechococcus sp. |
1.3.7.2 | D84N | site-directed mutagenesis, inactive mutant | Synechococcus sp. |
1.3.7.3 | D107E | site-directed mutagenesis, the mutant retains activity | Synechococcus sp. |
1.3.7.3 | D107N | site-directed mutagenesis, inactive mutant | Synechococcus sp. |
1.3.7.3 | D231E | site-directed mutagenesis, the mutant retains activity | Synechococcus sp. |
1.3.7.3 | D231N | site-directed mutagenesis, inactive mutant | Synechococcus sp. |
1.3.7.6 | D105E | site-directed mutagenesis, the mutant catalyzes only the first reaction step, i.e. the formation of 15,16-dihydrobiliverdin, reaction of EC 1.3.7.2 | Prochlorococcus phage P-SSM2 |
1.3.7.6 | D105N | site-directed mutagenesis, inactive mutant | Prochlorococcus phage P-SSM2 |
1.3.7.6 | D206E | site-directed mutagenesis, the mutant catalyzes only the second reaction step, i.e. the formation of (3Z)-phycoerythrobilin from 15,16-dihydrobiliverdin, reaction of EC 1.3.7.3 | Prochlorococcus phage P-SSM2 |
1.3.7.6 | D206N | site-directed mutagenesis, the mutant catalyzes only the first reaction step, i.e. the formation of 15,16-dihydrobiliverdin, reaction of EC 1.3.7.2 | Prochlorococcus phage P-SSM2 |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.3.7.2 | 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 | |
1.3.7.2 | 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 | |
1.3.7.3 | (3Z)-phycoerythrobilin + oxidized ferredoxin | Synechococcus sp. | - |
15,16-dihydrobiliverdin + reduced ferredoxin | - |
? | |
1.3.7.3 | (3Z)-phycoerythrobilin + oxidized ferredoxin | Synechococcus sp. WH8020 | - |
15,16-dihydrobiliverdin + reduced ferredoxin | - |
? | |
1.3.7.6 | biliverdin IXalpha + 2 reduced ferredoxin | Prochlorococcus phage P-SSM2 | a two-step reaction via intermediate 15,16-dihydrobiliverdin, the single steps form the reactions of EC 1.3.7.2 and 1.3.7.3, overview | (3Z)-phycoerythrobilin + 2 oxidized ferredoxin | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.3.7.2 | Synechococcus sp. | Q02189 | gene pebA | - |
1.3.7.2 | Synechococcus sp. WH8020 | Q02189 | gene pebA | - |
1.3.7.3 | Synechococcus sp. | - |
gene pebB | - |
1.3.7.3 | Synechococcus sp. WH8020 | - |
gene pebB | - |
1.3.7.6 | Prochlorococcus phage P-SSM2 | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.3.7.2 | 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 | |
1.3.7.2 | 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 | |
1.3.7.2 | 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 | |
1.3.7.2 | 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 | |
1.3.7.3 | (3Z)-phycoerythrobilin + oxidized ferredoxin | - |
Synechococcus sp. | 15,16-dihydrobiliverdin + reduced ferredoxin | - |
? | |
1.3.7.3 | (3Z)-phycoerythrobilin + oxidized ferredoxin | - |
Synechococcus sp. WH8020 | 15,16-dihydrobiliverdin + reduced ferredoxin | - |
? | |
1.3.7.6 | biliverdin IXalpha + 2 reduced ferredoxin | - |
Prochlorococcus phage P-SSM2 | (3Z)-phycoerythrobilin + 2 oxidized ferredoxin | - |
? | |
1.3.7.6 | biliverdin IXalpha + 2 reduced ferredoxin | a two-step reaction via intermediate 15,16-dihydrobiliverdin, the single steps form the reactions of EC 1.3.7.2 and 1.3.7.3, overview | Prochlorococcus phage P-SSM2 | (3Z)-phycoerythrobilin + 2 oxidized ferredoxin | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.3.7.2 | 15,16-DHBV:ferredoxin oxidoreductase | - |
Synechococcus sp. |
1.3.7.2 | ferredoxin-dependent bilin reductase | - |
Synechococcus sp. |
1.3.7.2 | PebA | - |
Synechococcus sp. |
1.3.7.3 | PEB:ferredoxin oxidoreductase | - |
Synechococcus sp. |
1.3.7.3 | PebB | - |
Synechococcus sp. |
1.3.7.6 | PEB synthase | - |
Prochlorococcus phage P-SSM2 |
1.3.7.6 | PebS | - |
Prochlorococcus phage P-SSM2 |
1.3.7.6 | phycoerythrobilin synthase | - |
Prochlorococcus phage P-SSM2 |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.3.7.3 | 20 | - |
assay at | Synechococcus sp. |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.3.7.2 | Ferredoxin | - |
Synechococcus sp. | |
1.3.7.3 | Ferredoxin | - |
Synechococcus sp. | |
1.3.7.6 | Ferredoxin | - |
Prochlorococcus phage P-SSM2 |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.3.7.2 | evolution | the enzyme belongs to the ferredoxin-dependent bilin reductase family. All members of the FDBR family are radical enzymes | Synechococcus sp. |
1.3.7.2 | 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. |
1.3.7.2 | 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. |
1.3.7.3 | evolution | the enzyme belongs to the the ferredoxin-dependent bilin reductase family. All members of the FDBR family are radical enzymes | Synechococcus sp. |
1.3.7.3 | 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. |
1.3.7.3 | 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. |
1.3.7.6 | evolution | the enzyme belongs to the ferredoxin-dependent bilin reductase family | Prochlorococcus phage P-SSM2 |
1.3.7.6 | metabolism | a two-step reaction via intermediate 15,16-dihydrobiliverdin, the single steps form the reactions of EC 1.3.7.2 and 1.3.7.3, overview | Prochlorococcus phage P-SSM2 |
1.3.7.6 | additional information | aspartate residues Asp105 and Asp206 are both involved in interactions with the pyrrole nitrogens upon substrate binding. Both are essential for the complete reduction of biliverdin IXalpha to (3Z)-phycoerythrobilin by PebS and are highly conserved throughout the family of ferredoxin-dependent bilin reductases | Prochlorococcus phage P-SSM2 |