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1.3.7.2: 15,16-dihydrobiliverdin:ferredoxin oxidoreductase

This is an abbreviated version!
For detailed information about 15,16-dihydrobiliverdin:ferredoxin oxidoreductase, go to the full flat file.

Word Map on EC 1.3.7.2

Reaction

15,16-dihydrobiliverdin
+
oxidized ferredoxin
=
biliverdin IXalpha
 +
reduced ferredoxin
 + 2 H+

Synonyms

15,16-DHBV:ferredoxin oxidoreductase, 15,16-dihydrobiliverdin:ferredoxin oxidoreductase, BRADO1265, DHBV:ferredoxin oxidoreductase, FDBR, ferredoxin-dependent bilin reductase, ferredoxin:15,16-dihydrobiliverdin oxidoreductase, GtPEBA, oxidoreductase, ferredoxin:15,16-dihydrobiliverdin, PcyA, PebA

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.7 With an iron-sulfur protein as acceptor
                1.3.7.2 15,16-dihydrobiliverdin:ferredoxin oxidoreductase

Engineering

Engineering on EC 1.3.7.2 - 15,16-dihydrobiliverdin:ferredoxin oxidoreductase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D105N
-
site-directed mutagenesis, altered substrate biliverdin binding compared to wild-type, the mutant shows 89% reduced activity compared to wild-type
E76Q
-
site-directed mutagenesis, the mutant shows 80% reduced activity compared to wild-type
H88Q
-
site-directed mutagenesis, altered substrate biliverdin binding compared to wild-type, the mutant shows 95% reduced activity compared to wild-type
I86D
-
site-directed mutagenesis, inactive mutant
D205N
site-directed mutagenesis, the mutant retains activity
D84E
site-directed mutagenesis, the mutant retains activity
D84N
site-directed mutagenesis, inactive mutant
D205N
-
site-directed mutagenesis, the mutant retains activity
-
D84E
-
site-directed mutagenesis, the mutant retains activity
-
D84N
-
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 then 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