BRENDA - Enzyme Database show
show all sequences of 1.3.7.12

Chlorophyll breakdown in oilseed rape

Hoertensteiner, S.; Kraeutler, B.; Photosyn. Res. 64, 137-146 (2000)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
O2
the enzyme is sensitive to O2
Arabidopsis thaliana
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
chloroplast
-
Arabidopsis thaliana
9507
-
chloroplast
-
Brassica napus
9507
-
gerontoplast
-
Arabidopsis thaliana
34400
-
gerontoplast
-
Brassica napus
34400
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
Arabidopsis thaliana
-
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
Brassica napus
-
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Brassica napus
Q1ELT7
gene RCCR
-
Arabidopsis thaliana
Q8LDU4
gene RCCR
-
Oxidation Stability
Oxidation Stability
Organism
RCCR activity is sensitive to oxygen
Brassica napus
the enzyme is sensitive to O2
Arabidopsis thaliana
Source Tissue
Source Tissue
Commentary
Organism
Textmining
cotyledon
senescent
Arabidopsis thaliana
-
cotyledon
senescent
Brassica napus
-
leaf
-
Arabidopsis thaliana
-
seed
-
Brassica napus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
736949
Arabidopsis thaliana
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
736949
Brassica napus
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
a red tetrapyrrole
736949
Arabidopsis thaliana
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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+
a red tetrapyrrole
736949
Brassica napus
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
Ferredoxin
-
Arabidopsis thaliana
Ferredoxin
-
Brassica napus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
Ferredoxin
-
Arabidopsis thaliana
Ferredoxin
-
Brassica napus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
O2
the enzyme is sensitive to O2
Arabidopsis thaliana
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
chloroplast
-
Arabidopsis thaliana
9507
-
chloroplast
-
Brassica napus
9507
-
gerontoplast
-
Arabidopsis thaliana
34400
-
gerontoplast
-
Brassica napus
34400
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
Arabidopsis thaliana
-
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
Brassica napus
-
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
?
Oxidation Stability (protein specific)
Oxidation Stability
Organism
RCCR activity is sensitive to oxygen
Brassica napus
the enzyme is sensitive to O2
Arabidopsis thaliana
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
cotyledon
senescent
Arabidopsis thaliana
-
cotyledon
senescent
Brassica napus
-
leaf
-
Arabidopsis thaliana
-
seed
-
Brassica napus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
736949
Arabidopsis thaliana
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
736949
Brassica napus
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
a red tetrapyrrole
736949
Arabidopsis thaliana
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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+
a red tetrapyrrole
736949
Brassica napus
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
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
-
-
?
General Information
General Information
Commentary
Organism
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
Arabidopsis thaliana
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
Brassica napus
physiological function
chlorophyll degradation is an integral part of leaf senescence or fruit ripening
Arabidopsis thaliana
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
Brassica napus
General Information (protein specific)
General Information
Commentary
Organism
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
Arabidopsis thaliana
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
Brassica napus
physiological function
chlorophyll degradation is an integral part of leaf senescence or fruit ripening
Arabidopsis thaliana
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
Brassica napus
Other publictions for EC 1.3.7.12
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
736190
Xiao
Cloning and expression analysi ...
Capsicum annuum
Genet. Mol. Res.
14
368-379
2015
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1
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726323
Liu
Nitric oxide deficiency accele ...
Arabidopsis thaliana
PLoS ONE
8
e56345
2013
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726877
Sakuraba
7-Hydroxymethyl chlorophyll a ...
Arabidopsis thaliana
Biochem. Biophys. Res. Commun.
430
32-37
2013
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726165
Sakuraba
STAY-GREEN and chlorophyll cat ...
Arabidopsis thaliana
Plant Cell
24
507-518
2012
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1
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736688
Zhang
Correlation of leaf senescence ...
Brassica rapa
J. Plant Physiol.
168
2081-2087
2011
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1
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2
1
1
2
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712769
Sugishima
Crystal structures of the subs ...
Arabidopsis thaliana
J. Mol. Biol.
402
879-891
2010
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2
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3
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699585
Sugishima
Crystal structure of red chlor ...
Arabidopsis thaliana
J. Mol. Biol.
389
376-387
2009
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700695
Ougham
The control of chlorophyll cat ...
Arabidopsis thaliana
Plant Biol.
10 Suppl 1
4-14
2008
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676436
Pruzinska
In vivo participation of red c ...
Arabidopsis thaliana
Plant Cell
19
369-387
2007
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671354
Hörtensteiner
Chlorophyll degradation during ...
Arabidopsis sp., Hordeum vulgare, Solanum lycopersicum, Spinacia oleracea
Annu. Rev. Plant Biol.
57
55-77
2006
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3
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3
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735438
Hoertensteiner
Chlorophyll degradation during ...
Arabidopsis thaliana
Annu. Plant Biol.
57
55-77
2006
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676587
Pruzinska
Chlorophyll breakdown in senes ...
Arabidopsis thaliana
Plant Physiol.
139
52-63
2005
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736960
Roca
Analysis of the chlorophyll ca ...
Lolium temulentum
Phytochemistry
65
1231-1238
2004
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676913
Mach
The Arabidopsis-accelerated ce ...
Arabidopsis sp.
Proc. Natl. Acad. Sci. USA
98
771-776
2001
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1
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676395
Hörtensteiner
-
Evolution of chlorophyll degra ...
Angiopteris, Auxenochlorella protothecoides, Carex, Cleome graveolens, Cycas sp., Equisetum sp., Euptelea, Ginkgo biloba, Hordeum vulgare, Metasequoia, Picea, Psilotum, Selaginella sp., Solanum lycopersicum, Spinacia oleracea, Taxus baccata, Taxus sp., Tropaeolum majus
Plant Biol.
2
63-67
2000
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2
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27
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15
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18
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18
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38
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1
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15
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15
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27
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18
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38
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1
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1
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15
15
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676490
Wüthrich
Molecular cloning, functional ...
Arabidopsis thaliana, Hordeum vulgare
Plant J.
21
189-198
2000
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2
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2
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1
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1
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2
1
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1
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1
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2
2
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1
2
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3
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2
1
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3
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1
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2
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2
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3
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2
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4
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7
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5
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6
14
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5
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1
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5
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16
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2
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1
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