EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.3.7.3 | 15,16-dihydrobiliverdin + reduced ferredoxin |
- |
Guillardia theta |
(3Z)-phycoerythrobilin + oxidized ferredoxin |
- |
? |
1.3.7.3 | 15,16-dihydrobiliverdin + reduced ferredoxin |
DHBV |
Guillardia theta |
(3Z)-phycoerythrobilin + oxidized ferredoxin |
- |
? |
1.3.7.3 | more |
enzyme acts via a substrate radical mechanism. No substrate: biliverdin IXalpha |
Guillardia theta |
? |
- |
? |
1.3.7.3 | more |
the open-chain tetrapyrrole substrate DHBV is bound in an unexpected flipped orientation within the canonical FDBR active site. Two central aspartate residues Asp99 and Asp219 as essential for catalytic activity. In addition, the conserved Arg215 plays a critical role in substrate specificity, binding orientation, and active site integrity |
Guillardia theta |
? |
- |
- |
1.3.7.3 | 15,16-dihydrobiliverdin + reduced ferredoxin |
- |
Guillardia theta CCMP2712 |
(3Z)-phycoerythrobilin + oxidized ferredoxin |
- |
? |
1.3.7.3 | 15,16-dihydrobiliverdin + reduced ferredoxin |
DHBV |
Guillardia theta CCMP2712 |
(3Z)-phycoerythrobilin + oxidized ferredoxin |
- |
? |
1.3.7.3 | more |
the open-chain tetrapyrrole substrate DHBV is bound in an unexpected flipped orientation within the canonical FDBR active site. Two central aspartate residues Asp99 and Asp219 as essential for catalytic activity. In addition, the conserved Arg215 plays a critical role in substrate specificity, binding orientation, and active site integrity |
Guillardia theta CCMP2712 |
? |
- |
- |
1.3.7.3 | 15,16-dihydrobiliverdin + reduced ferredoxin |
- |
Microchaete diplosiphon |
(3Z)-phycoerythrobilin + oxidized ferredoxin |
- |
? |
1.3.7.3 | 15,16-dihydrobiliverdin + reduced ferredoxin |
- |
Microchaete diplosiphon |
(3Z)-phycoerythrobilin + oxidized ferredoxin |
- |
r |
1.3.7.3 | 15,16-dihydrobiliverdin + reduced ferredoxin |
- |
Microchaete diplosiphon Fd33 |
(3Z)-phycoerythrobilin + oxidized ferredoxin |
- |
r |