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

Cloned

Cloned 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.
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
development of a system to produce phytochromobilin in Escherichia coli by coexpression of heme oxygenase and phytochromobilin:ferredoxin oxidoreductase in a single operon in conjunction with apophytochrome using two compatible plasmids
-
expressed in Escherichia coli strain BL21
-
expression in Nicotiana plumbaginifolia and Escherichia coli
-
expression in Pichia pastoris
-
overexpression in Synechococcus sp. strain PCC 7002, from endogenous plasmid pAQ1 under the control of the Synechocystis sp. strain PCC 6803 cpcBA promoter, leads to overproduction of phytochromobilin, the cells show a phenotype only slightly less pigmented and blue-green than the wild-type, the strain producing phycobiliproteins carrying phytochromobilin grow much more slowly at low light intensity. Transformant colonies in which pcyA is inactivated in the HY2 overexpression background does not develop a chlorotic appearance, and segregation of the mutant and wild-type alleles is rapidly achieved
-
recombinant functional expression of HT-HY2 in Escherichia coli with production of phytochromobilin, functional co-expression with cyanobacterial heme oxygenase, and the phycocyanin alpha-subunit, CpcA, from Synechocystis sp. PCC 6803 or Synechococcus sp. PCC 7002, and with the phycocyanin alpha-subunit phycocyanobilin lyase, CpcE/CpcF, or the phycoerythrocyanin alpha-subunit phycocyanobilin isomerizing lyase, PecE/PecF, from Noctoc sp. PCC 7120. Production levels of fluorescent pigments and chromophore analysis, overview
-
wild type and mutant allels
-