1.3.7.4: phytochromobilin:ferredoxin oxidoreductase

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

Word Map on EC 1.3.7.4

Reaction

(3Z)-phytochromobilin
+ 2 oxidized ferredoxin =
biliverdin IXalpha
+ 2 reduced ferredoxin

Synonyms

3Z-phytochromobilin:ferredoxin oxidoreductase, At3g09150, HT-HY2, HY2, PFB synthase, phytochromobilin synthase, PphiB synthase, ZMHy2

ECTree

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

Engineering

Engineering on EC 1.3.7.4 - phytochromobilin:ferredoxin oxidoreductase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D116N
-
mutant still retains the ability of substrate binding, but with only 1.5% relative activity of wild type protein
D146N
-
mutant completely loses catalytic activity and also the ability of biliverdin binding
D256E
-
mutant retains only partial activity
E110Q
-
site-directed mutagenesis, the mutant shows 321.7% of wild-type activity
E187Q
-
site-directed mutagenesis, the mutant shows 20.3% of wild-type activity
H259Q
-
site-directed mutagenesis, the mutant shows 123.4% of wild-type activity
K183Q
-
site-directed mutagenesis, the mutant shows 24.6% of wild-type activity
K255Q
-
site-directed mutagenesis, the mutant shows 11.7% of wild-type activity
K263Q
-
site-directed mutagenesis, the mutant shows 25.8% of wild-type activity
N133
-
mutant produces only partial activity
R200Q
-
site-directed mutagenesis, the mutant shows 12.5% of wild-type activity
R200Q/R264Q
-
site-directed mutagenesis, the mutant shows 11.9% of wild-type activity
R252Q
-
mutant loses catalytic activity and the ability of substrate binding
R264Q
-
site-directed mutagenesis, the mutant shows 18.9% of wild-type activity