EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.3.7.6 | D105E | site-directed mutagenesis, the mutant fully retains the ability to catalyse the first reduction at the 15,16-methine bridge, but cannot catalyse the second reduction at the A-ring 2,3,31,32-diene system, thereby yielding 15,16-DHBV as the final product | Prochlorococcus phage P-SSM2 |
1.3.7.6 | D206E | site-directed mutagenesis, the mutant fully retains the ability to catalyse the first reduction at the 15,16-methine bridge, but cannot catalyse the second reduction at the A-ring 2,3,31,32-diene system, however, in this mutant the reaction can be pushed further to produce (3Z)-phycoerythrobilin by a 10fold increase in ferredoxin concentration | Prochlorococcus phage P-SSM2 |
1.3.7.6 | D206N | site-directed mutagenesis, the mutant fully retains the ability to catalyse the first reduction at the 15,16-methine bridge, but cannot catalyse the second reduction at the A-ring 2,3,31,32-diene system, thereby yielding 15,16-DHBV as the final product | Prochlorococcus phage P-SSM2 |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
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 |
---|---|---|---|---|
1.3.7.6 | Prochlorococcus phage P-SSM2 | - |
Prochlorococcus-infecting | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
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 | - |
? | |
1.3.7.6 | biliverdin IXalpha + 2 reduced ferredoxin | ferredoxin from Synechococcus sp. PCC 7002 or from cyanophage P-SSM2 | Prochlorococcus phage P-SSM2 | (3Z)-phycoerythrobilin + 2 oxidized ferredoxin | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
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 |
---|---|---|---|---|
1.3.7.6 | 17 | - |
assay at | Prochlorococcus phage P-SSM2 |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.3.7.6 | 8 | - |
assay at | Prochlorococcus phage P-SSM2 |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.3.7.6 | Ferredoxin | - |
Prochlorococcus phage P-SSM2 |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.3.7.6 | evolution | the enzyme belongs to the ferredoxin-dependent bilin reductase family | Prochlorococcus phage P-SSM2 |
1.3.7.6 | additional information | PebS-catalysed PEB synthesis proceeds via a radical mechanism and both aspartate residues involved, Asp105 and Asp206, are important for stereospecific substrate protonation and conversion. Both Asp residues are highly conserved throughout the family of ferredoxin-dependent bilin reductases, bilin radical intermediates during PebS reaction, and superposition of the active site of the wild-type enzyme, the D105N and D206N mutant with bound substrate biliverdin | Prochlorococcus phage P-SSM2 |