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Enzyme Nomenclature
Information on EC 1.3.7.12 - red chlorophyll catabolite reductase
for references in articles please use BRENDA:EC1.3.7.12
Word Map on EC 1.3.7.12
- 1.3.7.12
- oxygenase
- pheophorbide
- leaf
- pao
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pheide
- porphyrin
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macrocycle
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colorless
- chlorophyllase
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phototoxic
-
ferredoxin
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ripening
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brassica
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nonfluorescent
-
light-dependent
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chl-binding
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bilin
-
dark-induced
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stay-green
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ferredoxin-dependent
- napus
-
thylakoids
-
mendel
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oxygenolytic
- canola
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ring-opening
- annuum
- tetrapyrrole
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pheophytinase
-
remobilization
- protothecoides
- agriculture
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.3.7.12
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RECOMMENDED NAME
GeneOntology No.
red chlorophyll catabolite reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster = red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster = red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
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primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster = red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
reaction pathway overview
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primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster = red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
reaction pathway overview
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primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster = red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
reaction pathway overview
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primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster = red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
reaction pathway overview
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primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster = red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
reaction pathway overview
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster = red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
reaction pathway overview
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primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster = red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
reaction pathway overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster = red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
The enzyme participates in chlorophyll degradation, which occurs during leaf senescence and fruit ripening in higher plants. The reaction requires reduced ferredoxin, which is generated from NADPH produced either through the pentose-phosphate pathway or by the action of photosystem I [1,2]. This reaction takes place while red chlorophyll catabolite is still bound to EC 1.14.15.17, pheophorbide a oxygenase [3]. Depending on the plant species used as the source of enzyme, one of two possible C-1 epimers of primary fluorescent chlorophyll catabolite (pFCC), pFCC-1 or pFCC-2, is normally formed, with all genera or species within a family producing the same isomer [3,4]. After modification and export, pFCCs are eventually imported into the vacuole, where the acidic environment causes their non-enzymic conversion into colourless breakdown products called non-fluorescent chlorophyll catabolites (NCCs) [2].
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CAS REGISTRY NUMBER
COMMENTARY
199618-44-5
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
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
metabolism
physiological function
additional information
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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in chlorophyll breakdown, the basic mechanism of macrocycle cleavage appears to be the same in green algae and in angiosperms
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
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
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
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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. 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. 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
-
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
-
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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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
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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
RCCR is distantly related to a family of bilin reductases
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
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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
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
evolution
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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
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
metabolism
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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 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 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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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
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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 (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
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 (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
-
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
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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
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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
physiological function
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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 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
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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 enzyme is involved in defense responses to various stresses
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
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
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
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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
-
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
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
-
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
-
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
-
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
-
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
-
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
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
primary fluorescent chlorophyll catabolite + NADP+
red chlorophyll catabolite + NADPH + H+
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
red chlorophyll catabolite + reduced acceptor
primary fluorescent chlorophyll catabolite + acceptor
-
three different primary fluorescent chlorophyll catabolites are produced, two of which could be identified as the stereoisomeric pFCCs from canola (Brassica napus) (pFCC-1) and sweet pepper (Capsicum annuum) (pFCC-2), respectively
-
-
?
red chlorophyll catabolite + reduced acceptor
primary fluorescent chlorophyll catabolite + oxidized acceptor
primary fluorescent chlorophyll catabolite + NADP+
red chlorophyll catabolite + NADPH + H+
-
stereospecific reaction
red chlorophyll catabolite, RCC, binding does not drastically change the RCCR structure, binding structure and mechanism analysis, overview. Comparison of the RCC-binding pockets of wild-type RCCRDELTA49 and F218V RCCRDELTA49, overview
-
r
primary fluorescent chlorophyll catabolite + NADP+
red chlorophyll catabolite + NADPH + H+
-
stereospecific reaction. RCCR catalyzes the ferredoxin-dependent and site-specific reduction of the C20/C1 double bond of red chlorophyll catabolite, RCC, the catabolic intermediate produced in chlorophyll degradation
-
-
r
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
catabolite pFCC-3
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
formation of a stereospecific product, overview
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
a red tetrapyrrole
two different fluorescent chlorophyll catabolites are formed from red chlorophyll catabolite and identified as primary fluorescent chlorophyll catabolite and its C1 epimer, 1-epi-pFCC
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
loose substrate binding allows for conformation change during the reaction, stereospcific reaction, mechanism, overview
formation of a stereospecific product, overview
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
reduction of the C20/C1 double bond of red chlorophyll catabolite is catalyzed by RCCR in a stereospecific manner forming the C1 isomer pFCC-1
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
in Chlorella, the release of red pigments is correlated with the loss of chlorophyll only if the cells are kept in the dark. These pigments are neither produced in light-grown cells nor in the dark if a source of nitrogen is provided
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
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
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
product epimer Bn-FCC-2
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
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
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
a red tetrapyrrole
two different fluorescent chlorophyll catabolites are formed from red chlorophyll catabolite and identified as primary fluorescent chlorophyll catabolite and its C1 epimer, 1-epi-pFCC
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
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, stereospecificity towards reduction of C1
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
i.e. Ca-pFCC-2, or 1-epi-FCC, or (1zeta,132R,17S,18S)-31,32-didehydro-1,4,5,10,17,18,20,22-octahydro-132-(methoxycarbonyl)-4,5-dioxo-4,5-secophytoporphyrin
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
stereospecificity towards reduction of C1
two products identified as pFCC-1 and pFCC-2, that have identical constitutions but differ in the absolute configuration at C1
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Cleome graveolens
-
-
catabolite pFCC-0, possible representing a modified version of either pFCC-1 or -2
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Cycas sp.
-
-
catabolite pFCC-3
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Equisetum sp.
-
-
catabolite pFCC-3
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
stereospecificity towards reduction of C1
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
stereospecificity towards reduction of C1
three products identified as pFCC-1 and pFCC-2, that have identical constitutions but differ in the absolute configuration at C1, and pFCC-3 with undetermined structure
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
in Chlorella, the release of red pigments is correlated with the loss of chlorophyll only if the cells are kept in the dark. These pigments are neither produced in light-grown cells nor in the dark if a source of nitrogen is provided
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
stereospecificity towards reduction of C1
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
catabolite pFCC-3
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Selaginella sp.
-
-
catabolite pFCC-3
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
catabolite pFCC-3
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
catabolite pFCC-0, possible representing a modified version of either pFCC-1 or -2
-
?
red chlorophyll catabolite + reduced acceptor
primary fluorescent chlorophyll catabolite + oxidized acceptor
-
chlorophyll catabolism, leaf senescence, ring-opening activity, a reduction destroys the residual conjugated bond system to yield the colourless product
pFCC, the fate of primary fluorescent chlorophyll catabolite is to be conjugated, imported into the vacuole and tautomerized to accumulate there as non-fluorescent chlorophyll catabolites and possibly other terminal catabolites
-
?
red chlorophyll catabolite + reduced acceptor
primary fluorescent chlorophyll catabolite + oxidized acceptor
-
the key steps in the degradation pathway of chlorophylls are the ring-opening reaction catalyzed by pheophorbide a oxygenase and sequential reduction by RCCR, RCCR catalyzes the ferredoxin-dependent reduction of the C20/C1 double bond of red chlorophyll catabolite
in the acidic environment of vacuoles, primary fluorescent chlorophyll catabolite is spontaneously converted into nonfluorescent chlorophyll catabolites
-
?
additional information
?
-
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
-
cell death gene ACD2 encodes red chlorophyll catabolite reductase and suppresses the spread of disease symptoms
-
-
-
additional information
?
-
-
with Arabidopsis RCCR, the C1 isomer pFCC-1 is formed. RCCR could be required to mediate an efficient interaction between red chlorophyll catabolite (still bound to pheophorbide a oxygenase) and ferredoxin, thereby enabling a fast, regio-, and stereoselective reduction to blue-fluorescing intermediate
-
-
-
additional information
?
-
-
RCCR absence causes leaf cell death as a result of the accumulation of photodynamic RCC. RCCR (together with pheophorbide a oxygenase) is required for the detoxification of chlorophyll catabolites
-
-
-
additional information
?
-
RCCR absence causes leaf cell death as a result of the accumulation of photodynamic RCC. RCCR (together with pheophorbide a oxygenase) is required for the detoxification of chlorophyll catabolites
-
-
-
additional information
?
-
-
the enzyme is involved in chlorophyll breakdown in senescent Arabidopsis leaves
-
-
-
additional information
?
-
-
the major product of reduction of red chlorophyll catabolite is pFCC1, but small quantities of its C1 epimer, pFCC-2, also accumulate. Red chlorophyll catabolite reductase and pheophorbide a oxygenase catalyse the key reaction of chlorophyll catabolism, porphin macrocycle cleavage of pheide a to a primary fluorescent catabolite
-
-
-
additional information
?
-
-
strongly interacts with catabolic enzymes (CCEs), NONYELLOW COLORING1 (NYC1), pheophorbide a oxygenase (PAO), NYC1-LIKE (NOL) and pheophytinase
-
-
-
additional information
?
-
the enzyme interacts with the 7-hydroxymethyl chlorophyll a reductase, HCAR, in in yeast two-hybrid assay and in Arabidopsis thaliana chlorophyll catabolism
-
-
-
additional information
?
-
-
in pFCC-1 of Brassica napus as well as in Chlorella protothecoides 18O is only found in the formyl group of pyrrole B, and the respective enzymes are monooxygenases. The lactam oxygen in pyrrole A is most probably derived from H2O
-
-
-
additional information
?
-
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
-
the enzyme is involved in breakdown of chlorophyll
-
-
-
additional information
?
-
-
in pFCC-1 of Brassica napus as well as in Chlorella protothecoides 18O is only found in the formyl group of pyrrole B, and hence the respective enzymes are monooxygenases. The lactam oxygen in pyrrole A is most probably derived from H2O
-
-
-
additional information
?
-
Cleome graveolens
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
Cycas sp.
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
Equisetum sp.
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
-
the enzyme is involved in chlorophyll breakdown
-
-
-
additional information
?
-
-
the major product of reduction of red chlorophyll catabolite is pFCC1, but small quantities of its C1 epimer, pFCC-2, also accumulate. Red chlorophyll catabolite reductase and pheophorbide a oxygenase catalyse the key eaction of chlorophyll catabolism, porphin macrocycle cleavage of pheide a to a primary fluorescent catabolite
-
-
-
additional information
?
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
Selaginella sp.
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
-
with tomato RCCR, the C1 isomer pFCC-2 is formed
-
-
-
additional information
?
-
-
spinach RCCR produces the C1 isomer pFCC-2
-
-
-
additional information
?
-
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
additional information
?
-
-
when heterologous combinations of PaO and RCCR are tested, the type of primary fluorescent chlorophyll catabolite turns out to be invariably determined by the source of RCCR, i.e. the slightly more polar pFCC-1 or the less polar pFCC-2
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
primary fluorescent chlorophyll catabolite + NADP+
red chlorophyll catabolite + NADPH + H+
-
stereospecific reaction. RCCR catalyzes the ferredoxin-dependent and site-specific reduction of the C20/C1 double bond of red chlorophyll catabolite, RCC, the catabolic intermediate produced in chlorophyll degradation
-
-
r
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
red chlorophyll catabolite + reduced acceptor
primary fluorescent chlorophyll catabolite + oxidized acceptor
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Q8LDU4
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
in Chlorella, the release of red pigments is correlated with the loss of chlorophyll only if the cells are kept in the dark. These pigments are neither produced in light-grown cells nor in the dark if a source of nitrogen is provided
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Q1ELT7
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Q1ELT7
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
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
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
V5K6J8
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Cleome graveolens
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Cycas sp.
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Equisetum sp.
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Q9MTQ6
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
in Chlorella, the release of red pigments is correlated with the loss of chlorophyll only if the cells are kept in the dark. These pigments are neither produced in light-grown cells nor in the dark if a source of nitrogen is provided
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Selaginella sp.
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
red chlorophyll catabolite + reduced acceptor
primary fluorescent chlorophyll catabolite + oxidized acceptor
-
chlorophyll catabolism, leaf senescence, ring-opening activity, a reduction destroys the residual conjugated bond system to yield the colourless product
pFCC, the fate of primary fluorescent chlorophyll catabolite is to be conjugated, imported into the vacuole and tautomerized to accumulate there as non-fluorescent chlorophyll catabolites and possibly other terminal catabolites
-
?
red chlorophyll catabolite + reduced acceptor
primary fluorescent chlorophyll catabolite + oxidized acceptor
-
the key steps in the degradation pathway of chlorophylls are the ring-opening reaction catalyzed by pheophorbide a oxygenase and sequential reduction by RCCR, RCCR catalyzes the ferredoxin-dependent reduction of the C20/C1 double bond of red chlorophyll catabolite
in the acidic environment of vacuoles, primary fluorescent chlorophyll catabolite is spontaneously converted into nonfluorescent chlorophyll catabolites
-
?
additional information
?
-
-
cell death gene ACD2 encodes red chlorophyll catabolite reductase and suppresses the spread of disease symptoms
-
-
-
additional information
?
-
-
with Arabidopsis RCCR, the C1 isomer pFCC-1 is formed. RCCR could be required to mediate an efficient interaction between red chlorophyll catabolite (still bound to pheophorbide a oxygenase) and ferredoxin, thereby enabling a fast, regio-, and stereoselective reduction to blue-fluorescing intermediate
-
-
-
additional information
?
-
-
RCCR absence causes leaf cell death as a result of the accumulation of photodynamic RCC. RCCR (together with pheophorbide a oxygenase) is required for the detoxification of chlorophyll catabolites
-
-
-
additional information
?
-
Q8LDU4
RCCR absence causes leaf cell death as a result of the accumulation of photodynamic RCC. RCCR (together with pheophorbide a oxygenase) is required for the detoxification of chlorophyll catabolites
-
-
-
additional information
?
-
-
the enzyme is involved in chlorophyll breakdown in senescent Arabidopsis leaves
-
-
-
additional information
?
-
-
the major product of reduction of red chlorophyll catabolite is pFCC1, but small quantities of its C1 epimer, pFCC-2, also accumulate. Red chlorophyll catabolite reductase and pheophorbide a oxygenase catalyse the key reaction of chlorophyll catabolism, porphin macrocycle cleavage of pheide a to a primary fluorescent catabolite
-
-
-
additional information
?
-
Q8LDU4
the enzyme interacts with the 7-hydroxymethyl chlorophyll a reductase, HCAR, in in yeast two-hybrid assay and in Arabidopsis thaliana chlorophyll catabolism
-
-
-
additional information
?
-
-
in pFCC-1 of Brassica napus as well as in Chlorella protothecoides 18O is only found in the formyl group of pyrrole B, and the respective enzymes are monooxygenases. The lactam oxygen in pyrrole A is most probably derived from H2O
-
-
-
additional information
?
-
-
the enzyme is involved in breakdown of chlorophyll
-
-
-
additional information
?
-
-
in pFCC-1 of Brassica napus as well as in Chlorella protothecoides 18O is only found in the formyl group of pyrrole B, and hence the respective enzymes are monooxygenases. The lactam oxygen in pyrrole A is most probably derived from H2O
-
-
-
additional information
?
-
-
the enzyme is involved in chlorophyll breakdown
-
-
-
additional information
?
-
-
the major product of reduction of red chlorophyll catabolite is pFCC1, but small quantities of its C1 epimer, pFCC-2, also accumulate. Red chlorophyll catabolite reductase and pheophorbide a oxygenase catalyse the key eaction of chlorophyll catabolism, porphin macrocycle cleavage of pheide a to a primary fluorescent catabolite
-
-
-
additional information
?
-
-
with tomato RCCR, the C1 isomer pFCC-2 is formed
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ferredoxin
-
the enzyme is ferredoxin dependent, but appears to lack a metal or flavin cofactor, indicating that electrons are directly transferred from ferredoxin to RCC
-
Ferredoxin
ferredoxin dependent, but appears to lack a metal or flavin cofactor, indicating that electrons are directly transferred from ferredoxin to red chlorophyll catabolite, RCC
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
iron sulfur cluster
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
O2
-
RCC reductase is sensitive towards oxygen, in vitro primary fluorescent chlorophyll catabolite formation from red chlorophyll catabolite occurs only under anoxic conditions
O2
-
RCC reductase is sensitive towards oxygen, in vitro primary fluorescent chlorophyll catabolite formation from red chlorophyll catabolite occurs only under anoxic conditions
O2
-
RCC reductase is sensitive towards oxygen, in vitro primary fluorescent chlorophyll catabolite formation from red chlorophyll catabolite occurs only under anoxic conditions
O2
RCC reductase is sensitive towards oxygen, in vitro primary fluorescent chlorophyll catabolite formation from red chlorophyll catabolite occurs only under anoxic conditions
O2
-
RCC reductase is sensitive towards oxygen, in vitro primary fluorescent chlorophyll catabolite formation from red chlorophyll catabolite occurs only under anoxic conditions
additional information
-
inactivation of RCCR by secondary compounds during tissue homogenization
-
additional information
-
inactivation of RCCR by secondary compounds during tissue homogenization
-
additional information
-
inactivation of RCCR by secondary compounds during tissue homogenization
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the catalytic activity of RCCR in vitro dramatically increases by coupling with PaO, possibly due to cooperative action, although PaO has been localized to the plastid envelope and RCCR is a soluble stroma enzyme; the catalytic activity of RCCR in vitro dramatically increases by coupling with pheophorbide alpha oxygenase, which also results in a stereospecific product
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the loss of RCCR in acd1/pao1 and acd2 mutants results n the formation of a lesion mimic phenotype, because of the accumulation of respective photodynamic chlorophyll breakdown intermediates
additional information
-
RCCR is constitutively active and its activity is rather constant during all phases of leaf development
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
in Chlorella, the release of red pigments is correlated with the loss of chlorophyll only if the cells are kept in the dark. These pigments are neither produced in light-grown cells nor in the dark if a source of nitrogen is provided
-
enzyme RCCR is a constitutive enzyme which is not only present in senescent leaves but also at other stages of leaf development
-
expression patterns of enzyme RCCR and other chlorophyll catabolic enzymes during leaf development, overview
highest enzyme expression level, the transcript level of CaRCCR is almost constant in the young leaves, fully expanded leaves, and senescent leaves
-
the enzyme is not only present in senescent leaves but also at other stages of leaf development
Cleome graveolens
-
enzyme RCCR is a constitutive enzyme which is not only present in senescent leaves but also at other stages of leaf development; the enzyme is not only present in senescent leaves but also at other stages of leaf development
Cycas sp.
-
enzyme RCCR is a constitutive enzyme which is not only present in senescent leaves but also at other stages of leaf development; the enzyme is not only present in senescent leaves but also at other stages of leaf development
Equisetum sp.
-
enzyme RCCR is a constitutive enzyme which is not only present in senescent leaves but also at other stages of leaf development; the enzyme is not only present in senescent leaves but also at other stages of leaf development
-
enzyme RCCR is a constitutive enzyme which is not only present in senescent leaves but also at other stages of leaf development
-
enzyme RCCR is a constitutive enzyme which is not only present in senescent leaves but also at other stages of leaf development
-
primary leaves of barley which had been induced to senesce in permanent darkness for 3 days. RCCR is a constitutive enzyme which is not only present in senescent leaves but also at other stages of leaf development
-
present in all stages of leaf development. The highest specific activity is found in senescent leaves
-
enzyme RCCR is a constitutive enzyme which is not only present in senescent leaves but also at other stages of leaf development
-
enzyme RCCR is a constitutive enzyme which is not only present in senescent leaves but also at other stages of leaf development
-
enzyme RCCR is a constitutive enzyme which is not only present in senescent leaves but also at other stages of leaf development
Selaginella sp.
-
enzyme RCCR is a constitutive enzyme which is not only present in senescent leaves but also at other stages of leaf development; the enzyme is not only present in senescent leaves but also at other stages of leaf development
-
the enzyme is not only present in senescent leaves but also at other stages of leaf development
-
primary leaves of barley which had been induced to senesce in permanent darkness for 3 days. RCCR is a constitutive enzyme which is not only present in senescent leaves but also at other stages of leaf development
-
enzyme RCCR is a constitutive enzyme which is not only present in senescent leaves but also at other stages of leaf development
Taxus sp.
-
the enzyme is not only present in senescent leaves but also at other stages of leaf development
-
enzyme RCCR is a constitutive enzyme which is not only present in senescent leaves but also at other stages of leaf development; the enzyme is not only present in senescent leaves but also at other stages of leaf development
additional information
-
in Chlorella, the release of red pigments is correlated with the loss of chlorophyll only if the cells are kept in the dark. These pigments are neither produced in light-grown cells nor in the dark if a source of nitrogen is provided
additional information
constitutive expression during all phases of development, analyses of tissue-specific expression and various stress-induced expression patterns of gene CaRCCR via quantitative real-time PCR
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
soluble protein of chloroplasts, in young Arabidopsis seedlings also associated with mitochondria
-
RCCR participates in chlorophyll breakdown inside the chloroplast
-
AtRCCR import is inhibited when the protein is missing 40 amino acids at the N-terminus
-
mainly; stroma, constitutive enzyme, the N-terminal 39-amino-acid stretch of RCCR is predicted to be the chloroplast transit peptide
RCC reductase is a soluble protein of the stroma
-
soluble protein of chloroplasts, in young Arabidopsis seedlings also associated with mitochondria
-
in young seedlings and in response to stress, RCCR is somewhat localized to mitochondria
additional information
-
RCCR is constitutively expressed in chloroplasts, whereas in young seedlings and in response to stress, it is also localized to mitochondria
-
additional information
in young Arabidopsis seedlings, the enzyme is also associated with mitochondria
-
additional information
the deduced CaRCCR protein contains a chloroplast transit peptide with 37-amino acid residues, its cleavage site was located between P37 and M38. The deduced CaRCCR does not have a signal peptide region or transmembrane helix
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
31000
32000
-
2 * 32000, about, sequence calculation; 2 * 32000, predicted by amino acid sequence, each subunit folds in an alpha/beta/alpha sandwich
35000
x * 35000, precursor enzyme, SDS-PAGE, x * 31000, mature enzyme, SDS-PAGE
31000
x * 35000, precursor enzyme, SDS-PAGE, x * 31000, mature enzyme, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 35000, precursor enzyme, SDS-PAGE, x * 31000, mature enzyme, SDS-PAGE
homodimer
additional information
homodimer
-
2 * 32000, about, sequence calculation; 2 * 32000, predicted by amino acid sequence, each subunit folds in an alpha/beta/alpha sandwich
additional information
-
enzyme RCCR forms a homodimer, in which each subunit folds in an alphabetaalpha sandwich, five N-terminal alpha-helices (H1/H2/H3/H5/H7), an anti-parallel beta-sheet consisting of eight strands (S1-S8), and four C-terminal alpha-helices (H4/H6/H8/H9). The two subunits are related by noncrystallographic 2fold symmetry in which the alpha-helices near the edge of the beta-sheet unique in RCCR participate in intersubunit interaction. The putative RCC-binding site forms an open pocket surrounded by conserved residues among RCCRs. Residues Glu154 and Asp291 stand opposite each other in the substrate binding pocket and are likely involved in substrate binding and/or catalysis. Primary structure comparisons, overview
additional information
-
RCCR folds into a characteristic alpha/beta/alpha sandwich, similar to that observed in the ferredoxin-dependent bilin reductase family, structure comparisosns, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
AtRCCR encodes a 35000 Da protein that is processed to a mature form of 31000 Da
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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 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
-
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
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
RCC reductase is sensitive towards oxygen, in vitro primary fluorescent chlorophyll catabolite formation from red chlorophyll catabolite occurs only under anoxic conditions
RCC reductase is sensitive towards oxygen, in vitro primary fluorescent chlorophyll catabolite formation from red chlorophyll catabolite occurs only under anoxic conditions
-
735913
RCC reductase is sensitive towards oxygen, in vitro primary fluorescent chlorophyll catabolite formation from red chlorophyll catabolite occurs only under anoxic conditions
-
735913
RCC reductase is sensitive towards oxygen, in vitro primary fluorescent chlorophyll catabolite formation from red chlorophyll catabolite occurs only under anoxic conditions
-
735913
RCC reductase is sensitive towards oxygen, in vitro primary fluorescent chlorophyll catabolite formation from red chlorophyll catabolite occurs only under anoxic conditions
-
735913
RCC reductase is sensitive towards oxygen, in vitro primary fluorescent chlorophyll catabolite formation from red chlorophyll catabolite occurs only under anoxic conditions
735913
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged wild-type and F218V mutant RCCR lacking the chloroplast transit peptide, Met1 to Gln39, i.e. RCCRDELTA49; recombinant truncated wild-type and mutant enzymes AtRCCRDELTA49 and F218V AtRCCRDELTA49
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chimeric RCCRs composed of portions of the Arabidopsis and the tomato proteins are expressed in Escherichia coli
expression of GST-tagged wild-type and F218V mutant RCCR lacking the chloroplast transit peptide, Met1 to Gln39; expression of wild-type and mutant enzymes lacking the chloroplast transit peptide (Met1 to Gln39) and N-termial residues 40-48 as GST-tagged enzymes
-
gene CaRCCR, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree
gene RCCR, the enzyme interacts with the 7-hydroxymethyl chlorophyll a reductase, HCAR, in in yeast two-hybrid assay
-
overexpression of ACD2 protein makes the plants tolerant but not resistant to bacterial infection
-
recombinant expression of chimeric enzyme mutants in Escherichia coli
chimeric RCCRs composed of portions of the Arabidopsis and the tomato proteins are expressed in Escherichia coli
-
chimeric RCCRs composed of portions of the Arabidopsis and the tomato proteins are expressed in Escherichia coli
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after senescence induction RCCR and other chlorophyll catabolic enzymes are significantly higher expressed in the pheophytinase-GFP overexpressing plants than in the wild-type plants
-
Chl degradation in ethylene-treated cabbage is faster than it is in control leaves, strong activation in the expression of the enzyme, as well as of the other two chlorophyll degradation related genes, pheophytinase (BrPPH) and pheophorbide a oxygenase (BrPAO), in control and ethylene-treated leaves. After 7 days, leavese the entire cabbages, except for the young leaves at the top, in control and ethylene treatment turn yellow
downregulation of expression of chlorophyll degradation related genes, pheophytinase (BrPPH), pheophorbide a oxygenase (BrPAO), and RCC reductase (RCCR) by 6-benzyl aminopurine. After 7 days, leaves in 6-BA treatment display lightly yellowing, while the entire cabbages, except for the young leaves at the top, in control leaves turn yellow
RCCR is not an inducible gene upon dark treatment, whereas its transcript level is slightly reduced during senescence. RCCR is constitutively active and its activity is rather constant during all phases of leaf development
-
the enzyme is upregulated by abscisic acid, methyl jasmonate, and salicylic acid, and it is induced by high salinity and drought stress treatments. The enzyme expression is also slightly increased when the pepper plants are infected with Phytophthora capsici strain HX-9
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
V218V
-
mutation changes the specificity of the protein from pFCC-1 (C1 isomers of pFCC) to pFCC-2 (C1 isomers of pFCC) production
F218V
additional information
F218V
-
mutation switches At-RCCR stereospecificity from pFCC-1 to pFCC-2 production
F218V
-
a mutant protein that produces the stereoisomer of primary fluorescent chlorophyll catabolites at the C1 position, the F218V mutation changes the stereospecificity in RCCR. Construction of wild-type and F218V mutant RCCR lacking the chloroplast transit peptide, Met1 to Gln39, i.e. RCCRDELTA49; the AtRCCR mutant protein produces the stereoisomer of primary fluorescent chlorophyll catabolites at the C1 position. The RCC in F218V AtRCCR rotates slightly compared with that in wild-type to fill in the space generated by the substitution of Phe218 with valine. Concomitantly, the two carboxy groups of Glu154 and Asp291 move slightly away from the C20/C1 double bond. Analysis of substrate-free and substrate-bound enzyme crystal structures, and comparison to wild-type structures, overview
additional information
-
chimeric RCCRs composed of portions of the Arabidopsis and the tomato proteins are expressed in Escherichia coli
additional information
-
chimeric RCCRs are produced in Escherichia coli by replacing parts of mature enzyme from Arabidopsis thaliana with the respective sequences from Lycopersicon esculentum. A reversal of specificity is found in protein M, in which a domain of 37 amino acids of At-RCCR have been replaced with the respective Le-RCCR domain
additional information
-
construction of N-terminally truncated variants of wild-type enzyme and enzyme mutant F218V, i.e. AtRCCRDELTA49 and F218V AtRCCRDELTA49
additional information
construction of chimeric enzymes composed of portions of the Arabidopsis and the tomato proteins and expression in Escherichia coli, functional complementation of Arabidopsis acd2-2 mutant
additional information
-
in the homologous system with both components from barley leaves, the slightly more polar pFCC-1 is produced, whereas the combination of barley membranes with soluble protein from spinach yields the less polar pFCC-2
additional information
-
introduction of the stay-green gene from Festuca pratensis enzyme activity related to chlorophyll catabolism are analyzed in senescing leaves of wild-type Lolium temulentum and compared with mutant stay line leaves. During senescence of wild-type leaves chlorophylls a and b are continuously catabolised to colourless products and no other derivatives are observed, whereas in mutant stay-green leaves there is an accumulation of dephytylated and oxidised catabolites including chlorophyllide a, phaeophorbide a and 132 OH-chlorophyllide a. Pigment analysis, overview. The stay-green phenotype is not due to a mutation in RCCR in Lolium temulentum
additional information
-
chimeric RCCRs composed of portions of the Arabidopsis and the tomato proteins are expressed in Escherichia coli
additional information
-
in the homologous system with both components from barley leaves, the slightly more polar pFCC-1 is produced, whereas the combination of barley membranes with soluble protein from spinach yields the less polar pFCC-2
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
economically important plants overexpressing ACD2 might also show increased tolerance to pathogens and might be useful for increasing crop yields
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LINKS TO OTHER DATABASES (specific for EC-Number 1.3.7.12)
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