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Information on EC 1.3.7.12 - red chlorophyll catabolite reductase and Organism(s) Hordeum vulgare and UniProt Accession Q9MTQ6
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1.3.7.12 red chlorophyll catabolite reductaseIUBMB Comments
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 . 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) .
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Word Map
- 1.3.7.12
- oxygenase
- pheophorbide
- pao
-
macrocycle
- porphyrin
-
pheide
- chlorophyllase
-
colorless
-
pheophytinase
-
phototoxic
-
nonfluorescent
-
light-dependent
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ferredoxin-dependent
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dark-induced
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stay-green
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bilin
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degreening
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chl-binding
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postharvest
- agriculture
The taxonomic range for the selected organisms is: Hordeum vulgare
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
2
=
+
2
+
2
+
2
oxidized ferredoxin [iron-sulfur] cluster
=
+
2
reduced ferredoxin [iron-sulfur] cluster
+
2
Synonyms
red chlorophyll catabolite reductase, rcc reductase, red chl catabolite reductase, carccr, atrccr, brrccr, acd2 protein, borccr, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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+
reaction pathway overview
PATHWAY SOURCE
PATHWAYS
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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].
CAS REGISTRY NUMBER
COMMENTARY
199618-44-5
-
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
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 + 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
-
?
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
?
-
-
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
?
-
-
the enzyme is involved in chlorophyll breakdown
-
-
?
NATURAL SUBSTRATE
NATURAL 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
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
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
?
-
-
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
?
-
-
the enzyme is involved in chlorophyll breakdown
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
present in all stages of leaf development. The highest specific activity is found in senescent leaves
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
RCC reductase is a soluble protein of the stroma
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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
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
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). RCCR_HORVU
205
0
22868
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
735913
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hörtensteiner, S.
Chlorophyll degradation during senescence
Annu. Rev. Plant Biol.
57
55-77
2006
Arabidopsis sp., Hordeum vulgare, Solanum lycopersicum, Spinacia oleracea
Hörtensteiner, S.; Rodoni, S.; Schellenberg, M.; Vicentini, F.; Nandi, O.I.; Qui, Y.L.; Matile, P.
Evolution of chlorophyll degradation: the significance of RCC reductase
Plant Biol.
2
63-67
2000
Angiopteris, Auxenochlorella protothecoides, Carex, Cleome graveolens, Cycas sp., Equisetum sp., Euptelea, Ginkgo biloba, Hordeum vulgare (Q9MTQ6), Metasequoia, Picea, Psilotum, Selaginella sp., Solanum lycopersicum, Spinacia oleracea, Taxus baccata, Taxus sp., Tropaeolum majus
-
Wüthrich, K.L.; Bovet, L.; Hunziker, P.E.; Donnison, I.S.; Hörtensteiner, S.
Molecular cloning, functional expression and characterisation of RCC reductase involved in chlorophyll catabolism
Plant J.
21
189-198
2000
Arabidopsis thaliana, Hordeum vulgare (Q9MTQ6), Hordeum vulgare
Rodoni, S.; Vicentini, F.; Schellenberg, M.; Matile, P.; Hörtensteiner, S.
Partial purification and characterization of red chlorophyll catabolite reductase, a stroma protein involved in chlorophyll breakdown
Plant Physiol.
115
677-682
1997
Hordeum vulgare
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