1.3.7.5: phycocyanobilin:ferredoxin oxidoreductase
This is an abbreviated version!
For detailed information about phycocyanobilin:ferredoxin oxidoreductase, go to the full flat file.
Word Map on EC 1.3.7.5
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1.3.7.5
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bilins
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cyanobacteria
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ixalpha
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tetrapyrrole
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chromophore
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phytochrome
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light-harvesting
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synechocystis
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phycobiliproteins
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ferredoxins
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vinyl
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four-electron
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d-ring
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phycobilisomes
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phytochromobilin
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substrate-free
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phycoerythrobilin
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light-sensing
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biliproteins
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antenna
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holophytochrome
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two-electron
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nostoc
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apophytochrome
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cyanobacteriochromes
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photoreversible
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phycobilin
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cyanophage
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fdbrs
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reddish
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photoactive
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phycocyanin
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prochlorococcus
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proton-donating
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myovirus
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protein-substrate
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hydronium
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analysis
- 1.3.7.5
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bilins
- cyanobacteria
- ixalpha
- tetrapyrrole
- chromophore
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phytochrome
-
light-harvesting
- synechocystis
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phycobiliproteins
- ferredoxins
-
vinyl
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four-electron
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d-ring
-
phycobilisomes
- phytochromobilin
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substrate-free
- phycoerythrobilin
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light-sensing
-
biliproteins
-
antenna
-
holophytochrome
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two-electron
- nostoc
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apophytochrome
-
cyanobacteriochromes
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photoreversible
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phycobilin
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cyanophage
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fdbrs
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reddish
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photoactive
- phycocyanin
- prochlorococcus
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proton-donating
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myovirus
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protein-substrate
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hydronium
- analysis
Reaction
Synonyms
3Z-phycocyanobilin:ferredoxin oxidoreductase, AmPcyAc, AmPcyAp, bilin reductase, FDBR, ferredoxin-dependent biliverdin reductase, ferredoxin:3Z-phycocyanobilin oxidoreductase, HY2 protein, oxidoreductase, ferredoxin:3Z-phycocyanobilin, Pcb:Fd oxidoreductase, PCB:ferredoxin oxidoreductase, PcyA, PCYA1, phycocyanobilin synthase, phycocyanobilin-ferredoxin oxidoreductase, phycocyanobilin:ferredoxin oxidoreductase, SyPcyA
ECTree
1.3.7.5 phycocyanobilin:ferredoxin oxidoreductaseAdvanced search results
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results (Engineering
Engineering on EC 1.3.7.5 - phycocyanobilin:ferredoxin oxidoreductase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D102N
D105N
E76Q
site-directed mutagenesis, substrate-binding structure compared to the wild-type enzyme. Overall folds and the binding sites of the U-shaped substrates of all three complexes are similar with wild-type PcyABV, the orientation of the Glu76 side chain, which is in close contact with the exo-vinyl group in PcyA-biliverdin IXalpha, is rotated away from the bilin D-ring. The local structures around the A-rings in the three complexes, which all retain the ability to reduce the A-ring of their bound pigments, are nearly identical with that of wild-type PcyA-biliverdin IXalpha
H88Q
V225D
site-directed mutagenesis,substrate binding structure, overview
I86D
biliverdin bound to the I86D mutant is fully protonated (BVH+) and can accept an electron, but I86D is unable to donate protons for the reduction. Compared to the wild-type PcyA, the I86D mutant stabilizes BVH+
additional information
D102N
high-field electron paramagnetic resonance spectroscopy of frozen solutions and single crystals of the one-electron reduced protein-substrate complex of mutant D102N. Spectra reveal a biliverdin radical with a very narrow g tensor. This g tensor is consistent with a biliverdin radical where the carbonyl oxygen atoms on both the A and the D pyrrole rings are protonated
D105N
high-field electron paramagnetic resonance spectroscopy of frozen solutions and single crystals of the one-electron reduced protein-substrate complex of mutant D105N. Spectra reveal a biliverdin radical with a very narrow g tensor with principal values 2.00359(5), 2.00341(5), and 2.00218(5). This g tensor is consistent with a biliverdin radical where the carbonyl oxygen atoms on both the A and the D pyrrole rings are protonated
H88Q
the g anisotropy of the biliverdin radical in H88Q is measurably smaller than those of mutant D105N
additional information
identification of mutant pcya1-1, cloning and photosynthetic phenotype analysis, overview. Efficient PCYA1 knockdown by artificial microRNA does not impact algal phototrophic growth. Yeast two-hybrid analyses of protein-protein interaction with bilin biosynthesis metabolism proteins using the coding regions of CrPCYA11TP (amino acids 56-556), CrPCYA1-NTE (amino acids 56-174), CrPCYA1-FDBR (amino acids 175-451), CrPCYA1-CTE (amino acids 449-556), and pull-down assay
additional information
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identification of mutant pcya1-1, cloning and photosynthetic phenotype analysis, overview. Efficient PCYA1 knockdown by artificial microRNA does not impact algal phototrophic growth. Yeast two-hybrid analyses of protein-protein interaction with bilin biosynthesis metabolism proteins using the coding regions of CrPCYA11TP (amino acids 56-556), CrPCYA1-NTE (amino acids 56-174), CrPCYA1-FDBR (amino acids 175-451), CrPCYA1-CTE (amino acids 449-556), and pull-down assay
additional information
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identification of mutant pcya1-1, cloning and photosynthetic phenotype analysis, overview. Efficient PCYA1 knockdown by artificial microRNA does not impact algal phototrophic growth. Yeast two-hybrid analyses of protein-protein interaction with bilin biosynthesis metabolism proteins using the coding regions of CrPCYA11TP (amino acids 56-556), CrPCYA1-NTE (amino acids 56-174), CrPCYA1-FDBR (amino acids 175-451), CrPCYA1-CTE (amino acids 449-556), and pull-down assay
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additional information
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insertional inactivation of pcyA is not possible in wild-type Synechococcus sp. strain PCC 7002 due to lethality of the mutant, but in a variant heterologously expressing HY2 from Arabidopsis thaliana encoding a phytochromobilin:ferredoxin oxidoreductase
additional information
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insertional inactivation of pcyA is not possible in wild-type Synechococcus sp. strain PCC 7002 due to lethality of the mutant, but in a variant heterologously expressing HY2 from Arabidopsis thaliana encoding a phytochromobilin:ferredoxin oxidoreductase
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additional information
construction of a plasmid containing genes of apo-allophycocyanin alpha-subunit without chromophore and chromophore synthetases HO1, i.e. ferredoxin-dependent heme oxygenase, and PcyA, i.e. phycocyanobilin:ferredoxin oxidoreductase, and expression in Escherichia coli. Holo-allophycocyanin, i.e. allophycocyanin alpha-subunit with chromophore, can be synthesized by autocatalysis in Escherichia coli. Recombinant holo-allophycocyanin alpha-subunit shows the same spectral and fluorescent properties as phycocyanin and serves as a good substitute for native phycocyanin for fluorescent tagging. Recombinant allophycocyanin alpha-subunit can inhibit hydroxyl and peroxyl radicals more strongly than holo-allophycocyanin alpha-subunit and native allophycocyanin
