Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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
+
oxidized ferredoxin
=
biliverdin IXalpha
+
reduced ferredoxin
+ 2 H+

Synonyms

3Z-phytochromobilin:ferredoxin oxidoreductase, At3g09150, AUREA, Csa_1G616870, CsHY2, HT-HY2, HY2, HY2 protein, PFB synthase, phytochromobilin synthase, PphiB synthase, Solyc01 g008930, 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

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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
D123N
site-directed mutagenesis, the mutated enzyme retains biliverdin IXalpha binding activity and radical formation activity, whereas the PPhiB formation activity is negligible
D263N
site-directed mutagenesis, the mutated enzyme retains biliverdin IXalpha binding activity and radical formation activity, whereas the PPhiB formation activity is negligible
V121A
site-directed mutagenesis, single-turnover analysis demonstrates that the V121A mutated protein is slightly slower, although it produces 3Z/E-PPhiB on wild-type level, whereas no activity is detected in the V121A mutated protein in the steady-state analysis
additional information