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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

Reaction

(3Z)-phycoerythrobilin
+
oxidized ferredoxin
=
15,16-dihydrobiliverdin
+
reduced ferredoxin
+ 2 H+

Synonyms

bilin reductase, ferredoxin:3Z-phycoerythrobilin oxidoreductase, GtPEBB, oxidoreductase, ferredoxin:3Z-phycoerythrobilin, PEB:ferredoxin oxidoreductase, PebB

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.7 With an iron-sulfur protein as acceptor
                1.3.7.3 phycoerythrobilin:ferredoxin oxidoreductase

Engineering

Engineering on EC 1.3.7.3 - phycoerythrobilin:ferredoxin oxidoreductase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D219N
site-directed mutagenesis, inactive mutant
D99N
site-directed mutagenesis, inactive mutant
R215A
site-directed mutagenesis, inactive mutant
R215K
site-directed mutagenesis, inactive mutant
R215L
site-directed mutagenesis, inactive mutant
R215M
site-directed mutagenesis, inactive mutant
R215S
site-directed mutagenesis, inactive mutant
D219N
-
site-directed mutagenesis, inactive mutant
-
D99N
-
site-directed mutagenesis, inactive mutant
-
R215A
-
site-directed mutagenesis, inactive mutant
-
R215K
-
site-directed mutagenesis, inactive mutant
-
R215L
-
site-directed mutagenesis, inactive mutant
-
D107E
-
site-directed mutagenesis, the mutant retains activity
D107N
-
site-directed mutagenesis, inactive mutant
D231E
-
site-directed mutagenesis, the mutant retains activity
D231N
-
site-directed mutagenesis, inactive mutant
D107E
-
site-directed mutagenesis, the mutant retains activity
-
D107N
-
site-directed mutagenesis, inactive mutant
-
D231E
-
site-directed mutagenesis, the mutant retains activity
-
D231N
-
site-directed mutagenesis, inactive mutant
-
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