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
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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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Natural Substrates Products
Natural Substrates Products on EC 1.3.7.12 - red chlorophyll catabolite reductase
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REACTION DIAGRAM
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
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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
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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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
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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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
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Cleome graveolens
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Cycas sp.
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Equisetum sp.
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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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
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Selaginella sp.
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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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
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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
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cell death gene ACD2 encodes red chlorophyll catabolite reductase and suppresses the spread of disease symptoms
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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the enzyme is involved in chlorophyll breakdown in senescent Arabidopsis leaves
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additional information
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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
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additional information
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the enzyme interacts with the 7-hydroxymethyl chlorophyll a reductase, HCAR, in in yeast two-hybrid assay and in Arabidopsis thaliana chlorophyll catabolism
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additional information
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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
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additional information
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the enzyme is involved in breakdown of chlorophyll
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additional information
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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
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additional information
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the enzyme is involved in chlorophyll breakdown
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additional information
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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
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additional information
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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
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additional information
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with tomato RCCR, the C1 isomer pFCC-2 is formed
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