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
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1.3.7.4
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litoria
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phytochrome
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lycoris
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calpurnia
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alstroemeria
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amaryllidaceae
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matricaria
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tabebuia
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phytochrome-deficient
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phyllostachys
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venerupis
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bilins
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galanthamine
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ethnobotanical
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biotechnology
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synthesis
- 1.3.7.4
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litoria
-
phytochrome
-
lycoris
-
calpurnia
-
alstroemeria
-
amaryllidaceae
-
matricaria
-
tabebuia
-
phytochrome-deficient
-
phyllostachys
-
venerupis
-
bilins
- galanthamine
-
ethnobotanical
- biotechnology
- synthesis
Reaction
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
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Engineering
Engineering on EC 1.3.7.4 - phytochromobilin:ferredoxin oxidoreductase
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D116N
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mutant still retains the ability of substrate binding, but with only 1.5% relative activity of wild type protein
D146N
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mutant completely loses catalytic activity and also the ability of biliverdin binding
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
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
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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
identification of elongated hypocotyl-1 (elh1) mutant C1238, comparison of mutant seedlings with wild-type CCMC seedlings, phenotype, overview. Analysis of the effect of CsHY2 mutation on the function of phys, the expression dynamics of cucumber PHYs genes (CsPHYA1, CsPHYA2, CsPHYB, CsPHYC, and CsPHYE). The 35S:CsHY2-EGFP plasmid construct is transformed into Agrobacterium tumefaciens strain GV3101. Arabidopsis hy2-1 recessive homozygous mutants are transformed and the phenotype is analyzed. The expression level of CsHY2 in mutant is the highest in male and female flowers, followed in order by stem, true leaves, root, cotyledon, and fruit. There is no significant difference in CsHY2 expression in all these organs except cotyledons, true leaves, and stem between wild-type and mutant elh1
additional information
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identification of elongated hypocotyl-1 (elh1) mutant C1238, comparison of mutant seedlings with wild-type CCMC seedlings, phenotype, overview. Analysis of the effect of CsHY2 mutation on the function of phys, the expression dynamics of cucumber PHYs genes (CsPHYA1, CsPHYA2, CsPHYB, CsPHYC, and CsPHYE). The 35S:CsHY2-EGFP plasmid construct is transformed into Agrobacterium tumefaciens strain GV3101. Arabidopsis hy2-1 recessive homozygous mutants are transformed and the phenotype is analyzed. The expression level of CsHY2 in mutant is the highest in male and female flowers, followed in order by stem, true leaves, root, cotyledon, and fruit. There is no significant difference in CsHY2 expression in all these organs except cotyledons, true leaves, and stem between wild-type and mutant elh1
additional information
the flooding (rf) mutation is analysed in the tomato gene AUREA (AU), it not only led to leaf chlorosis but also causes the spontaneous formation of adventitious roots (ARs) on stems. Under flooding stress, au mutants extensively form ARs along the stem, while wild-type plants produce ARs only at the root-shoot junction. After submergence for 7 days, the resistant to flooding (rf) mutants show higher sensitivity to flooding regarding AR initiation compared to wild-type. Mutation of the AU gene appears to have minimal impact on tomato growth and fruit yield. The flooding resistance of rf mutants mainly results from the accumulation of heme and enhanced HO-1 activity, both of which function in the phytochrome synthesis pathway. In addition, the exchange of substances, including heme, between leaves and stems accounts for AR formation on stems
additional information
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the flooding (rf) mutation is analysed in the tomato gene AUREA (AU), it not only led to leaf chlorosis but also causes the spontaneous formation of adventitious roots (ARs) on stems. Under flooding stress, au mutants extensively form ARs along the stem, while wild-type plants produce ARs only at the root-shoot junction. After submergence for 7 days, the resistant to flooding (rf) mutants show higher sensitivity to flooding regarding AR initiation compared to wild-type. Mutation of the AU gene appears to have minimal impact on tomato growth and fruit yield. The flooding resistance of rf mutants mainly results from the accumulation of heme and enhanced HO-1 activity, both of which function in the phytochrome synthesis pathway. In addition, the exchange of substances, including heme, between leaves and stems accounts for AR formation on stems