1.3.7.12: red chlorophyll catabolite reductase
This is an abbreviated version!
For detailed information about red chlorophyll catabolite reductase, go to the full flat file.
Word Map on EC 1.3.7.12
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1.3.7.12
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oxygenase
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pheophorbide
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pao
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macrocycle
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porphyrin
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pheide
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chlorophyllase
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colorless
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pheophytinase
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phototoxic
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nonfluorescent
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light-dependent
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ferredoxin-dependent
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dark-induced
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stay-green
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bilin
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degreening
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chl-binding
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postharvest
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agriculture
- 1.3.7.12
- oxygenase
- pheophorbide
- pao
-
macrocycle
- porphyrin
-
pheide
- chlorophyllase
-
colorless
-
pheophytinase
-
phototoxic
-
nonfluorescent
-
light-dependent
-
ferredoxin-dependent
-
dark-induced
-
stay-green
-
bilin
-
degreening
-
chl-binding
-
postharvest
- agriculture
Reaction
+ 2 oxidized ferredoxin [iron-sulfur] cluster = + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
Synonyms
ACD2 protein, At-RCCR, AtRCCR, BoRCCR, BrRCCR, CaRCCR, EC 1.3.1.80, HvRCCR, PHAVU_008G280300g, RCC reductase, RCCR, RCCR-1, RCCR-2, red Chl catabolite reductase, red chlorophyll catabolite reductase, red-chlorophyll-catabolite reductase
ECTree
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Crystallization
Crystallization on EC 1.3.7.12 - red chlorophyll catabolite reductase
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at 2.4 A resolution, determination of the crystal structure of, where chloroplast transit peptide is truncated and a Gly-Pro-Leu-Gly-Ser peptide is added to the N terminus, 2 peptide chains A and B are located in an asymmetric unit of the selenomethionine-RCCR crystal, these 2 chains form a homodimer, AtRCCR folds into an alpha/beta/alpha sandwich: 5 N-terminal alpha-helices, an anti-parallel beta-sheet consisting of 8 strands, and 4 C-terminal alpha-helices
purified recombinant RCC-bound wild-type enzyme AtRCCRDELTA49, RCC-bound and substrate-free enzyme mutant F218V AtRCCRDELTA49, sitting-drop vapor diffusion method, mixing of 10 mg/ml substrate-free and substrate-bound proteins in 20 mM Tris-HCl, pH 7.4, and 200 mM NaCl, with an equal volume of reservoir solution containing 30% or 35%, respectively, w/v PEG 2000 monomethyl ether, 0.1 M ammonium acetate, 3% v/v dioxane, and 0.1 M 4-morpholineethanesulfonic acid-NaOH, pH 6.5, equilibration gainst reservoir solution, 20°C, 1 day, X-ray diffraction structure determination and analysis at 2.0-2.6 A resolution
purified recombinant red chlorophyll catabolite-bound RCCRDELTA49, and red chlorophyll catabolite-bound or substrate-free F218V RCCRDELTA49, sitting drop vapor diffusion method, 20°C, protein solution is mixed with an equal volume of reservoir solution and equilibrated against reservoir solution containing 30% w/v PEG 2000 monomethyl ether, 0.1 M ammonium acetate, 3% v/v dioxane, and 0.1 M 4-morpholineethanesulfonic acid-NaOH, pH 6.5, 1 day, X-ray diffraction structure determination and analysis at 2.0-2.6 A resolution
purified substrate-free enzyme, with the chloroplast transit peptide truncated and a Gly-Pro-Leu-Gly-Ser peptide added to the N-terminus, X-ray diffraction structure determination and analysis at 2.5-2.7 A resolution, structure modelling