1.3.7.3: phycoerythrobilin:ferredoxin oxidoreductase
This is an abbreviated version!
For detailed information about phycoerythrobilin:ferredoxin oxidoreductase, go to the full flat file.
Word Map on EC 1.3.7.3
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1.3.7.3
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bilins
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light-harvesting
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biliverdin
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cyanobacteria
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tetrapyrrole
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phycocyanobilin
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ferredoxin-dependent
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algae
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phycobiliproteins
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chromophore
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reductases
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phycocyanobilin:ferredoxin
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phytochromes
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heme
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open-chain
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two-electron
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phycobilins
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ixalpha
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four-electron
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cryptophytes
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apophytochrome
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d-ring
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phycobilisomes
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guillardia
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neutron
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pink
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fdbrs
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theta
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oxygenases
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peba
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biliproteins
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vinyl
- 1.3.7.3
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bilins
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light-harvesting
- biliverdin
- cyanobacteria
- tetrapyrrole
- phycocyanobilin
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ferredoxin-dependent
- algae
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phycobiliproteins
- chromophore
- reductases
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phycocyanobilin:ferredoxin
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phytochromes
- heme
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open-chain
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two-electron
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phycobilins
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ixalpha
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four-electron
- cryptophytes
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apophytochrome
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d-ring
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phycobilisomes
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guillardia
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neutron
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pink
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fdbrs
- theta
- oxygenases
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peba
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biliproteins
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vinyl
Reaction
Synonyms
bilin reductase, ferredoxin:3Z-phycoerythrobilin oxidoreductase, GtPEBB, oxidoreductase, ferredoxin:3Z-phycoerythrobilin, PEB:ferredoxin oxidoreductase, PebB
ECTree
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Substrates Products
Substrates Products on EC 1.3.7.3 - phycoerythrobilin:ferredoxin oxidoreductase
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REACTION DIAGRAM
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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-
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?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
3E-isomer occurs by non-enzyme-mediated side reaction caused by heat and reduced gluthathione
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-
?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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-
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?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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3E-isomer occurs by non-enzyme-mediated side reaction caused by heat and reduced gluthathione
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-
?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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biosynthesis of bilin pigments, functions with EC1.3.7.2. as a dual enzyme complex in the conversion of biliverdin Ixa into phycoerythrobilin
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-
?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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-
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?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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3E-isomer occurs by non-enzyme-mediated side reaction caused by heat and reduced gluthathione
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-
?
(3Z)-phycoerythrobilin + oxidized ferredoxin
15,16-dihydrobiliverdin + reduced ferredoxin
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biosynthesis of bilin pigments, functions with EC1.3.7.2. as a dual enzyme complex in the conversion of biliverdin Ixa into phycoerythrobilin
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-
?
(3Z)-phycoerythrobilin + oxidized ferredoxin
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-
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-
?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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-
-
?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
DHBV
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-
?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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-
-
?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
DHBV
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-
?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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-
-
-
?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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-
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r
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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-
-
r
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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-
-
-
?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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-
-
-
r
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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-
-
-
?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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-
-
?
15,16-dihydrobiliverdin + reduced ferredoxin
(3Z)-phycoerythrobilin + oxidized ferredoxin
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-
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r
?
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enzyme acts via a substrate radical mechanism. No substrate: biliverdin IXalpha
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additional information
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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
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additional information
?
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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
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-
-
additional information
?
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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
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additional information
?
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the enzyme performs substrate channeling with the 15,16-dihydrobiliverdin:ferredoxin oxidoreductase catalyzing the former catalytic step. Both enzymes transiently interact and that transfer of the intermediate is facilitated by a significantly higher binding affinity of DHBV toward phycoerythrobilin:ferredoxin oxidoreductase
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additional information
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development of an on-column assay with substrate channeling for FDBRs, transient interaction of both PebA and PebB during the conversion of biliverdin IXa (BV) to phycoerythrobilin (PEB) via 15,16-dihydrobiliverdin (DHBV)
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