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
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macrocycle
- porphyrin
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pheide
- 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
- 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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General Information
General Information on EC 1.3.7.12 - red chlorophyll catabolite reductase
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evolution
malfunction
metabolism
physiological function
additional information
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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCC-2. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
Selaginella sp.
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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCC-2. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCC-2. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCC-2. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
Equisetum sp.
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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCC-2. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
Cycas sp.
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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCC-2. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
Cleome graveolens
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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCC-2. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCC-2. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
-
evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCC-2. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
-
evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCC-2. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
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evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
-
evolutionary tree of vascular plants based on analysis of several molecular data sets for enzymes RCCR, overview. Two forms of primary fluorescent chlorophyll catabolite, pFCC, are found in plants, the slightly more polar pFCC-1 or the less polar pFCC-2. A third form, pFCC-3 is found only in basal pteridophytes and in some gymnosperms, it seems to be produced by an ancestral type of RCCR. RCCR-1 appears to have evolved independently in some unrelated lineages. It has a restricted phylogenetic distribution and most likely represents recent derivations from RCCR-2. The situation within monocots appears to be quite clear cut. All the grasses and Carex tested are characterized by type 1 of RCCR, all other monocots produce pFCC-2
evolution
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in chlorophyll breakdown, the basic mechanism of macrocycle cleavage appears to be the same in green algae and in angiosperms
evolution
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RCC reductase activity can be demonstrated in mono- as well as in dicotyledons, and is also found in pteridophytes and gymnosperms. Within a plant family RCC reductases from different genera and species have the same stereospecificity
evolution
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RCC reductase activity can be demonstrated in mono- as well as in dicotyledons, and is also found in pteridophytes and gymnosperms. Within a plant family RCC reductases from different genera and species have the same stereospecificity
evolution
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RCC reductase activity can be demonstrated in mono- as well as in dicotyledons, and is also found in pteridophytes and gymnosperms. Within a plant family RCC reductases from different genera and species have the same stereospecificity
evolution
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RCC reductase activity can be demonstrated in mono- as well as in dicotyledons, and is also found in pteridophytes and gymnosperms. Within a plant family RCC reductases from different genera and species have the same stereospecificity
evolution
RCC reductase activity can be demonstrated in mono- as well as in dicotyledons, and is also found in pteridophytes and gymnosperms. Within a plant family RCC reductases from different genera and species have the same stereospecificity
evolution
RCCR is distantly related to a family of bilin reductases
evolution
red chlorophyll catabolite reductases appear to represent a phylogenetically early addition to the chlorophyll catabolic pathway. Two types of red chlorophyll-catabolite reductases (RCCR), named RCCR-type 1 and RCCR-type 2, appear to have evolved in higher plants. Chlorophyll catabolism in higher plants differs remarkably from that in the green alga by the formation of FCCs and NCCs
evolution
red chlorophyll catabolite reductases appear to represent a phylogenetically early addition to the chlorophyll catabolic pathway. Two types of red chlorophyll-catabolite reductases (RCCR), named RCCR-type 1 and RCCR-type 2, appear to have evolved in higher plants. Chlorophyll catabolism in higher plants differs remarkably from that in the green algae by the formation of FCCs and NCCs
evolution
the enzyme belongs to the ferredoxin-dependent bilin reductase (FDBR) family, which synthesizes a variety of phytobilin pigments, on the basis of sequence similarity, ferredoxin dependency, and the common tetrapyrrole skeleton of their substrates. The tertiary structure of RCCR is similar to those of FDBRs, strongly supporting that these enzymes evolved from a common ancestor
evolution
the enzyme belongs to the ferredoxin-dependent bilin reductase (FDBR) family. RCC is bound to the pocket between the beta-sheet and the C-terminal alpha-helices, as seen in substrate-bound FDBRs, but RCC binding to RCCR is much looser than substrate binding to FDBRs
evolution
the enzyme belongs to the ferredoxin-dependent bilin reductase family, FDBR, and contains two conserved acidic residue sites (Glu151 and Asp288), which are involved in catalysis and/or substrate binding
mutants defective in pheophorbide a oxygenase or red chlorophyll catabolite reductase, e.g. acd2 mutants that exhibit a light-dependent cell death phenotype with spontaneous spreading lesions, the mutants develop a lesion mimic phenotype, due to accumulation of breakdown intermediates
malfunction
chlorine dioxide (ClO2) , a class A1 safe disinfectant with strong bactericidal capacities used to preserve the quality of vegetables and fruits, delays reddening by suppressing the expression of certain genes associated with chlorophyll breakdown and carotenoid synthesis in harvested green peppers. The mechanism involves delayed degradation of chlorophyll and significantly reduced synthesis of capsanthin and beta-carotene. Additionally, the transcript levels of pheophytin pheophorbide hydrolase (PPH), pheophorbide a oxygenase (PAO), and red chlorophyll catabolite reductase (RCCR) genes, associated with chlorophyll breakdown, are inhibited by ClO2 treatment, and the relative expression of phytoene synthase (Psy), lycopene beta-cyclase enzyme (Lcyb), apsanthin/capsorubin synthase (Ccs), and beta-carotene hydroxygenase enzyme (Crtz) genes, associated with carotenoid synthesis, are suppressed
malfunction
expression levels of red chlorophyll catabolite reductase (RCCR) is strongly enhanced at an early stage (2 cm long) in wild-type but not in green pod mutants. The expression levels of genes involved in cellulose synthesis is inhibited by the pod degreening. Metabolomic profiling shows that the content of most flavonoid, flavones, and isoflavonoid is decreased during pod development, but the content of afzelechin, taxifolin, dihydrokaempferol, and cyanidin 3-O-rutinoside is remarkably increased in both wild-type and green pod mutant. Analysis of transcriptome and metabolome of the yellow pod cultivar of the common bean golden hook ecotype and its green pod mutants yielded via gamma radiation, phenotypes, overview
malfunction
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melatonin treatment significantly suppresses the RCCR expression, which reduces the enzyme activity in melatonin-treated florets compared to levels in control florets throughout the whole storage
malfunction
methylcyclopropene (1-MCP) and chlorine dioxide (ClO2) both inhibit the enzyme expression in green pepper. Synergistic inhibitory effect of 1-MCP and ClO2 treatment on chlorophyll degradation of green pepper fruit during storage, pheophytinase (PPH), pheophorbide a oxygenase (PAO), and red chlorophyll catabolite reductase (RCCR) are suppressed by all treatments , overview
in chlorophyll breakdown, the conversion of pheophorbide a to primary fluorescent chlorophyll catabolites is catalyzed by the joint action of the two enzymes PaO, a membrane-bound enzyme, and the soluble stroma enzyme RCCR. The former cleaves the porphyrin macrocycle oxidatively and produces a bound form of the intermediary catabolite (RCC), which seems to be reduced stereoselectively on the C20=C1 bond by the action of the reductase
metabolism
in chlorophyll breakdown, the conversion of pheophorbide a to primary fluorescent chlorophyll catabolites is catalyzed by the joint action of the two enzymes PaO, a membrane-bound enzyme, and the soluble stroma enzyme RCCR. The former cleaves the porphyrin macrocycle oxidatively and produces a bound form of the intermediary catabolite (RCC), which seems to be reduced stereoselectively on the C20=C1 bond by the action of the reductase
metabolism
in the chlorophyll breakdown pathway, the key reaction which causes loss of green color in leaf senescence is catalyzed in a two-step reaction by pheophorbide an oxygenase and red chlorophyll catabolite reductase. Red chlorophyll catabolite, RCC, the primary product of oxygenolytic Pheide a cleavage by pheophorbide a oxygenase, PaO, is subsequently reduced to primary fluorescent chlorophyll catabolite by red chlorophyll catabolite reductase, RCCR. RCC appears not to be released from PaO, but is directly reduced to pFCC by RCCR, suggesting a close physical contact between the two protein components during catalysis and metabolic channeling of the red intermediate. Both partial reactions require reduced ferredoxin as the source of electrons, whereby ferredoxin is kept in the reduced state either by photosystem I or the pentose phosphate cycle. Since the PaO reaction is accompanied by the incorporation of two oxygen atoms and RCCR activity is sensitive to oxygen, the interaction of PaO and RCCR is a prerequisite for RCCR action
metabolism
in the chlorophyll breakdown pathway, the key reaction which causes loss of green color in leaf senescence is catalyzed in a two-step reaction by pheophorbide an oxygenase and red chlorophyll catabolite reductase. Red chlorophyll catabolite, RCC, the primary product of oxygenolytic Pheide a cleavage by pheophorbide a oxygenase, PaO, is subsequently reduced to primary fluorescent chlorophyll catabolite by red chlorophyll catabolite reductase, RCCR. RCC appears not to be released from PaO, but is directly reduced to pFCC by RCCR, suggesting a close physical contact between the two protein components during catalysis and metabolic channeling of the red intermediate. Both partial reactions require reduced ferredoxin as the source of electrons, whereby ferredoxin is kept in the reduced state either by photosystem I or the pentose phosphate cycle. Since the PaO reaction is accompanied by the incorporation of two oxygen atoms and RCCR activity is sensitive to oxygen, the interaction of PaO and RCCR is a prerequisite for RCCR action
metabolism
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leaf senescence is accompanied by the metabolism of chlorophyll (Chl) to nonfluorescent catabolites (NCCs). The pathway of Chl degradation comprises several reactions and includes the occurrence of intermediary catabolites. After removal of phytol and the central Mg atom from Chl by chlorophyllase and Mg dechelatase, respectively, the porphyrin macrocycle of pheophorbide (Pheide) a is cleaved. This two-step reaction is catalyzed by Pheide a oxygenase and RCC reductase and yields a primary fluorescent catabolite (pFCC). After hydroxylation and additional species-specific modifications, FCCs are tautomerized nonenzymically to NCCs inside the vacuole
metabolism
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leaf senescence is accompanied by the metabolism of chlorophyll (Chl) to nonfluorescent catabolites (NCCs). The pathway of Chl degradation comprises several reactions and includes the occurrence of intermediary catabolites. After removal of phytol and the central Mg atom from Chl by chlorophyllase and Mg dechelatase, respectively, the porphyrin macrocycle of pheophorbide (Pheide) a is cleaved. This two-step reaction is catalyzed by Pheide a oxygenase and RCC reductase and yields a primary fluorescent catabolite (pFCC). After hydroxylation and additional species-specific modifications, in Chlorella, the final degradation products of chlorophyll are excreted into the surrounding medium, whereas in higher plants they are deposited in the vacuoles of mesophyll cells. Occurrence of catabolites of both Chl a and b in Chlorella. In Chlorella porphyrin cleavage does not require the joint action of a monooxygenase and a reductase as is the case in higher plants
metabolism
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leaf senescence is accompanied by the metabolism of chlorophyll (Chl) to nonfluorescent catabolites (NCCs). The pathway of Chl degradation comprises several reactions and includes the occurrence of intermediary catabolites. After removal of phytol and the central Mg atom from Chl by chlorophyllase and Mg dechelatase, respectively, the porphyrin macrocycle of pheophorbide (Pheide) a is cleaved. This two-step reaction is catalyzed by Pheide a oxygenase and RCC reductase and yields a primary fluorescent catabolite (pFCC). Two atoms of oxygen are introduced into RCC, pFCC-1 and the corresponding red catabolites of Chlorella protothecoides and production of pFCC-1 from Pheide a requires dioxygen. After hydroxylation and additional species-specific modifications, FCCs are tautomerized nonenzymically to NCCs inside the vacuole
metabolism
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leaf senescence is accompanied by the metabolism of chlorophyll to nonfluorescent catabolites (NCCs). The pathway of chlorophyll degradation comprises several reactions and includes the occurrence of intermediary catabolites. After removal of phytol and the central Mg atom from chlorophyll by chlorophyllase and Mg dechelatase, respectively, the porphyrin macrocycle of pheophorbide (Pheide) a is cleaved. This two-step reaction is catalyzed by Pheide a oxygenase and RCC reductase and yields a primary fluorescent catabolite (pFCC). After hydroxylation and additional species-specific modifications, FCCs are tautomerized nonenzymically to NCCs inside the vacuole
metabolism
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leaf senescence is accompanied by the metabolism of chlorophyll to nonfluorescent catabolites (NCCs). The pathway of chlorophyll degradation comprises several reactions and includes the occurrence of intermediary catabolites. After removal of phytol and the central Mg atom from chlorophyll by chlorophyllase and Mg dechelatase, respectively, the porphyrin macrocycle of pheophorbide (Pheide) a is cleaved. This two-step reaction is catalyzed by Pheide a oxygenase and RCC reductase and yields a primary fluorescent catabolite (pFCC). After hydroxylation and additional species-specific modifications, FCCs are tautomerized nonenzymically to NCCs inside the vacuole
metabolism
leaf senescence is accompanied by the metabolism of chlorophyll to nonfluorescent catabolites (NCCs). The pathway of chlorophyll degradation comprises several reactions and includes the occurrence of intermediary catabolites. After removal of phytol and the central Mg atom from chlorophyll by chlorophyllase and Mg dechelatase, respectively, the porphyrin macrocycle of pheophorbide (Pheide) a is cleaved. This two-step reaction is catalyzed by Pheide a oxygenase and RCC reductase and yields a primary fluorescent catabolite (pFCC). After hydroxylation and additional species-specific modifications, FCCs are tautomerized nonenzymically to NCCs inside the vacuole
metabolism
opening the porphyrin macrocycle of pheophorbide a and forming the primary fluorescent chlorophyll catabolites are key steps in the chlorophyll catabolism pathway. These steps are catalyzed by pheophorbide a oxygenase and red chlorophyll catabolite reductase
metabolism
the chlorophyll catabolic enzymes (CCEs) NYC1, NOL, PPH, PAO and RCCR interact with the light harvesting complex II, LHCII. The enzyme RCCR interacts with the 7-hydroxymethyl chlorophyll a reductase, HCAR, a component of the proposed SGR-CCE-LHCII complex, in Arabidopsis thaliana chlorophyll catabolism
metabolism
The key step in Chl breakdown in green plants, the cleavage reaction of the porphinoid macrocycle, is catalyzed by an oxygenase that specifically recognizes pheophorbide a (Pheide a). The conversion of Pheide a to a primary blue fluorescent catabolite (pFCC) requires the joint action of PaO and the soluble stroma-located enzyme RCC reductase that reduces the intermediary red catabolite (RCC) to pFCC, structures of breakdown products of chlorophyll, overview
metabolism
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the oxygenase catalyzing porphyrin cleavage is a monooxygenase. In Chlorella, a mechanism with intermediary formation of a C4:C5 epoxide and subsequent hydrolytic cleavage and prototropic rearrangements has been proposed. Thereby, the second rearrangement at C10 has been demonstrated to be highly stereoselective. Two atoms of oxygen are introduced into RCC, pFCC-1 and the corresponding red catabolites of Chlorella protothecoides and production of pFCC-1 from Pheide a requires dioxygen. After hydroxylation and additional species-specific modifications, in Chlorella, the final degradation products of chlorophyll are excreted into the surrounding medium, whereas in higher plants they are deposited in the vacuoles of mesophyll cells. Occurrence of catabolites of both Chl a and b in Chlorella. In Chlorella porphyrin cleavage does not require the joint action of a monooxygenase and a reductase as is the case in higher plants
metabolism
the three chl catabolic enzymes, chlorophyllase, pheophorbide a oxygenase (PAO), and red chlorophyll catabolite reductase (RCCR) catalyze chlorophyll breakdown, which is very important for plant development and survival. Chlorophyll breakdown is a prerequisite to detoxify the potentially phototoxic pigment within the vacuoles in order to permit the remobilization of nitrogen from chlorophyll-binding proteins to proceed during senescence. Enzyme RCCR might be required to mediate an efficient interaction between red chlorophyll catabolite (still bound to PAO) and ferredoxin, thereby enabling a fast, regio-, and stereoselective reduction to primary fluorescent chlorophyll catabolite
metabolism
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effects of ethylene on the expression of Chl catabolic genes (CCGs) of apple peel during ripening after treating harvested commercial mature apples with 1-methylcyclopropene (1-MCP): 1-MCP treatment leads to a delayed climacteric peak of respiration and ethylene production, exhibiting higher Chl content and hue angle compared to untreated fruit during ripening. Lower quantities of pheophorbide a oxygenase (PAO), pheophytinase (PPH) and red Chl catabolite reductase (RCCR) are also observed in peel tissues under 1-MCP treatment during ripening. Quantitative real-time polymerase chain reaction reveals that the expression of CCGs, except for MdNYE1a, increases at different degrees upon ripening. Meanwhile, the apples treated with 1-MCP present a downregulated expression of MdRCCR2, MdNYC1, MdNYC3 and MdNOL2 and a fluctuating expression of MdNYE1a, MdPPH1, MdPAO6, MdPAO8 and MdHCAR compared with the controls during ripening. Regulatory role of ethylene in the Chl degradation pathway of apple peel during ripening
metabolism
enzyme RCCR is involved in the chlorophyll breakdown pathway
a major goal of chlorophyll breakdown merely concerns the detoxification of the green plant pigment which may be destructive otherwise as a photosensitizer to the regulated processes that occur during senescence
physiological function
a major goal of chlorophyll breakdown merely concerns the detoxification of the green plant pigment which may be destructive otherwise as a photosensitizer to the regulated processes that occur during senescence
physiological function
chlorophyll degradation is an integral part of leaf senescence or fruit ripening
physiological function
Chlorophyll degradation is not only an integral part of leaf senescence or fruit ripening, but in several species, such as oilseed rape, also occurs in maturing seeds, significance of the chlorophyll breakdown pathway in respect to chlorophyll degradation during Brassica napus seed development
physiological function
red chlorophyll catabolite reductase (RCCR) catalyzes the ferredoxin-dependent reduction of the C20/C1 double bond of red chlorophyll catabolite (RCC), the catabolic intermediate produced in chlorophyll degradation
physiological function
the conversion of Pheide a to a primary blue fluorescent catabolite (pFCC) requires the joint action of PaO and a soluble stroma-located enzyme that reduces an intermediary red catabolite (RCC) to pFCC. Both PaO and RCC reductase require reduced ferredoxin as reductant. Although RCC reductase is present at all stages of development and in all tissues examined, PaO seems to occur in gerontoplasts exclusively
physiological function
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the enzyme is involved in chlorophyll catabolism in leaf senescence. Chlorophyll catabolism occurs throughout the plant life-cycle and is highly sensitive to both biotic and abiotic stresses
physiological function
the enzyme is involved in defense responses to various stresses
physiological function
the expression of BrPPH, BrPAO and BrRCCR, and the activity of Mg-dechelatase is closely associated with the chlorophyll degradation during the leaf senescence process in harvested Chinese flowering cabbages under dark conditions
physiological function
the key steps in the degradation pathway of chlorophylls are the ring opening reaction catalyzed by pheophorbide a oxygenase and sequential reduction by red chlorophyll catabolite reductase (RCCR). During these steps, chlorophyll catabolites lose their color and phototoxicity. Enzyme RCCR catalyzes the ferredoxin-dependent reduction of the C20/C1 double bond of red chlorophyll catabolite
physiological function
red chlorophyll catabolite reductase (RCCR) is involved in chlorophyll degradation
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in contrast to the enzyme's O2 sensitivity, the coupled in vitro assay (formation of pFCC from Pheide a) requires oxygen for incorporation into the substrate. In the metabolic channelling of the two partial reactions, PaO creates an oxygen-depleted microenvironment which allows the action of RCC reductase
additional information
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in contrast to the enzyme's O2 sensitivity, the coupled in vitro assay (formation of pFCC from Pheide a) requires oxygen for incorporation into the substrate. In the metabolic channelling of the two partial reactions, PaO creates an oxygen-depleted microenvironment which allows the action of RCC reductase
additional information
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in contrast to the enzyme's O2 sensitivity, the coupled in vitro assay (formation of pFCC from Pheide a) requires oxygen for incorporation into the substrate. In the metabolic channelling of the two partial reactions, PaO creates an oxygen-depleted microenvironment which allows the action of RCC reductase
additional information
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in contrast to the enzyme's O2 sensitivity, the coupled in vitro assay (formation of pFCC from Pheide a) requires oxygen for incorporation into the substrate. In the metabolic channelling of the two partial reactions, PaO creates an oxygen-depleted microenvironment which allows the action of RCC reductase
additional information
in contrast to the enzyme's O2 sensitivity, the coupled in vitro assay (formation of pFCC from Pheide a) requires oxygen for incorporation into the substrate. In the metabolic channelling of the two partial reactions, PaO creates an oxygen-depleted microenvironment which allows the action of RCC reductase
additional information
Residues Glu154 and Asp291 stand opposite each other in the substrate binding pocket and are likely involved in substrate binding and/or catalysis
additional information
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Residues Glu154 and Asp291 stand opposite each other in the substrate binding pocket and are likely involved in substrate binding and/or catalysis
additional information
the primary fluorescent chlorophyll catabolite Ca-FCC-2 from sweet pepper, Capsicum annuum, chromoplasts has similar optical properties, but is slightly less polar than the primary FCC from senescent cotyledons of oilseed rape, Brassica napus, determination of structure and constitution by fast-atom-bombardment mass spectra and homo- and heteronuclear magnetic resonance experiments. Two-dimensional homonuclear spectra of Ca-FCC-2 reveals it to differ from pFCC by the configuration at the methine atom C1, whose configuration results from the action of red chlorophyll catabolite reductase, RCCR. Structure analysis, overview
additional information
the primary fluorescent chlorophyll catabolite Ca-FCC-2 from sweet pepper, Capsicum annuum, chromoplasts has similar optical properties, but is slightly less polar than the primary FCC from senescent cotyledons of oilseed rape, Brassica napus, determination of structure and constitution by fast-atom-bombardment mass spectra and homo- and heteronuclear magnetic resonance experiments. Two-dimensional homonuclear spectra of Ca-FCC-2 reveals it to differ from pFCC by the configuration at the methine atom C1, whose configuration results from the action of red chlorophyll catabolite reductase, RCCR. Structure analysis, overview
additional information
the substrate red chlorophyll catabolite is bound to the pocket between the beta-sheet and the C-terminal alpha-helices. Substrate RCC binds quiet lossely to the enzyme. The loose binding seems beneficial to the large conformational change in red chlorophyll catabolite upon reduction. Two conserved acidic residues, Glu154 and Asp291, sandwich the C20/C1 double bond of RCC, suggesting that these two residues are involved in site-specific reduction. The geometrical arrangement of RCC and the carboxy groups of Glu154 and Asp291 in RCCR is essential for the stereospecificity of the RCCR reaction, substrate binding mechanism, overview. Analysis of substrate-free and substrate-bound enzyme crystal structures, and comparison to F218V enzyme mutant structures, overview
additional information
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the substrate red chlorophyll catabolite is bound to the pocket between the beta-sheet and the C-terminal alpha-helices. Substrate RCC binds quiet lossely to the enzyme. The loose binding seems beneficial to the large conformational change in red chlorophyll catabolite upon reduction. Two conserved acidic residues, Glu154 and Asp291, sandwich the C20/C1 double bond of RCC, suggesting that these two residues are involved in site-specific reduction. The geometrical arrangement of RCC and the carboxy groups of Glu154 and Asp291 in RCCR is essential for the stereospecificity of the RCCR reaction, substrate binding mechanism, overview. Analysis of substrate-free and substrate-bound enzyme crystal structures, and comparison to F218V enzyme mutant structures, overview