Information on EC 1.3.7.12 - red chlorophyll catabolite reductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.3.7.12
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RECOMMENDED NAME
GeneOntology No.
red chlorophyll catabolite reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster = red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
chlorophyll a degradation I
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chlorophyll a degradation II
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Porphyrin and chlorophyll metabolism
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Biosynthesis of secondary metabolites
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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 hide
199618-44-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Angiopteris sp.
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Manually annotated by BRENDA team
var. parachinensis
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Cleome graveolens
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Manually annotated by BRENDA team
Cycas sp.
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Manually annotated by BRENDA team
Equisetum sp.
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Manually annotated by BRENDA team
Euptelea sp.
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Manually annotated by BRENDA team
gene RCCR
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Metasequoia sp.
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Manually annotated by BRENDA team
gene RCCR
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Manually annotated by BRENDA team
gene RCCR
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Manually annotated by BRENDA team
Picea sp.
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Manually annotated by BRENDA team
Psilotum sp.
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Manually annotated by BRENDA team
Selaginella sp.
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Taxus sp.
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
primary fluorescent chlorophyll catabolite + NADP+
red chlorophyll catabolite + NADPH + H+
show the reaction diagram
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
red chlorophyll catabolite + reduced acceptor
primary fluorescent chlorophyll catabolite + acceptor
show the reaction diagram
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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
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-
?
red chlorophyll catabolite + reduced acceptor
primary fluorescent chlorophyll catabolite + oxidized acceptor
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
primary fluorescent chlorophyll catabolite + NADP+
red chlorophyll catabolite + NADPH + H+
show the reaction diagram
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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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r
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
red chlorophyll catabolite + reduced acceptor
primary fluorescent chlorophyll catabolite + oxidized acceptor
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
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NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
iron sulfur cluster
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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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 hide
LITERATURE
IMAGE
0.6
red chlorophyll catabolite
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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assay at room temperature
25
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58000
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gel filtration
60000
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about, gel filtration; dimer, determined by gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 35000, precursor enzyme, SDS-PAGE, x * 31000, mature enzyme, SDS-PAGE
dimer
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2 * 31000, SDS-PAGE
homodimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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AtRCCR encodes a 35000 Da protein that is processed to a mature form of 31000 Da
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
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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
RCCR activity is sensitive to oxygen
736949
the enzyme is sensitive to O2
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736949
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
anion exchange chromatography
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from senescent barley leaves to homogeneity
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
a partial gene sequence
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chimeric RCCRs composed of portions of the Arabidopsis and the tomato proteins are expressed in Escherichia coli
cloning and expression in Escherichia coli
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expression in Escherichia coli
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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
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gene CaRCCR, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree
gene RCCR, cloned from leaves, quantitative enzyme expression analysis
gene RCCR, the enzyme interacts with the 7-hydroxymethyl chlorophyll a reductase, HCAR, in in yeast two-hybrid assay
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overexpression of ACD2 protein makes the plants tolerant but not resistant to bacterial infection
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recombinant expression of chimeric enzyme mutants in Escherichia coli
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
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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
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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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
V218V
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mutation changes the specificity of the protein from pFCC-1 (C1 isomers of pFCC) to pFCC-2 (C1 isomers of pFCC) production
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
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economically important plants overexpressing ACD2 might also show increased tolerance to pathogens and might be useful for increasing crop yields