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
-
bilins
-
light-harvesting
- biliverdin
- cyanobacteria
- tetrapyrrole
- phycocyanobilin
-
ferredoxin-dependent
- algae
-
phycobiliproteins
- chromophore
- reductases
-
phycocyanobilin:ferredoxin
-
phytochromes
- heme
-
open-chain
-
two-electron
-
phycobilins
-
ixalpha
-
four-electron
- cryptophytes
-
apophytochrome
-
d-ring
-
phycobilisomes
-
guillardia
-
neutron
-
pink
-
fdbrs
- theta
- oxygenases
-
peba
-
biliproteins
-
vinyl
Reaction
Synonyms
bilin reductase, ferredoxin:3Z-phycoerythrobilin oxidoreductase, GtPEBB, oxidoreductase, ferredoxin:3Z-phycoerythrobilin, PEB:ferredoxin oxidoreductase, PebB
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Engineering
Engineering on EC 1.3.7.3 - phycoerythrobilin:ferredoxin oxidoreductase
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additional information
analysis wether addition of PebB to the immobilized PebA-DHBV complex will result in the interaction of PebA and PebB and, therefore, cause retention of PebB on the column. Retention of PebB on the immobilized PebA column is not observed, but a transfer of almost all PebA-bound DHBV to PebB is seen, DHBV is washed off the column with regular washing buffer. in Synechococcus sp. WH8020, the genes encoding for pebA and pebB share an overlapping region. The pebA stop codon TGA is part of the pebB start codon ATG. In order to generate a translational fusion between pebA and pebB, a guanine base is inserted into the start-stop region of the pebAB-operon generating an artificial fusion of both enzymes, termed PebAgB. The newly generated codon GTG encodes for a valine residue, which now serves as a diminutive linker between PebA and PebB. This fusion protein is significantly different to the phage encoded PebS (EC 1.3.7.6), which is a homologue to PebA. But the fusion protein PebAgB shows PebS-like activity. Comparison of the PebAgB-catalyzed conversion of BV with an assay containing both PebA and PebB reveals no significant changes in velocity