BRENDA - Enzyme Database show
show all sequences of 1.3.7.12

The key step in chlorophyll breakdown in higher plants. Cleavage of pheophorbide a macrocycle by a monooxygenase

Hörtensteiner, S.; Wüthrich, K.L.; Matile, P.; Ongania, K.H.; Kräutler, B.; J. Biol. Chem. 273, 15335-15339 (1998)

Data extracted from this reference:

Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
chloroplast stroma
-
Brassica napus
9570
-
gerontoplast stroma
-
Brassica napus
-
-
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+
Brassica napus
-
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Brassica napus
Q1ELT7
-
-
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+
-
674404
Brassica napus
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
674404
Brassica napus
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
product epimer Bn-FCC-2
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
Ferredoxin
-
Brassica napus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
Ferredoxin
-
Brassica napus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
chloroplast stroma
-
Brassica napus
9570
-
gerontoplast stroma
-
Brassica napus
-
-
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+
Brassica napus
-
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
?
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+
-
674404
Brassica napus
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
red chlorophyll catabolite + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
674404
Brassica napus
primary fluorescent chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
product epimer Bn-FCC-2
-
-
?
General Information
General Information
Commentary
Organism
metabolism
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
Brassica napus
physiological function
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
Brassica napus
General Information (protein specific)
General Information
Commentary
Organism
metabolism
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
Brassica napus
physiological function
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
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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3
3
1
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726323
Liu
Nitric oxide deficiency accele ...
Arabidopsis thaliana
PLoS ONE
8
e56345
2013
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1
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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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736688
Zhang
Correlation of leaf senescence ...
Brassica rapa
J. Plant Physiol.
168
2081-2087
2011
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1
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712769
Sugishima
Crystal structures of the subs ...
Arabidopsis thaliana
J. Mol. Biol.
402
879-891
2010
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1
1
2
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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
1
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1
1
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3
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2
2
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2
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3
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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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-
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2
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1
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4
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676436
Pruzinska
In vivo participation of red c ...
Arabidopsis thaliana
Plant Cell
19
369-387
2007
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2
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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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3
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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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1
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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
1
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2
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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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15
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27
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38
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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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736215
Muehlecker
-
Breakdown of chlorophyll: A fl ...
Brassica napus, Capsicum annuum
Helv. Chim. Acta
83
278-286
2000
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8
8
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736949
Hoertensteiner
Chlorophyll breakdown in oilse ...
Arabidopsis thaliana, Brassica napus
Photosyn. Res.
64
137-146
2000
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4
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2
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4
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4
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735913
Hoertensteiner
Chlorophyll breakdown in highe ...
Auxenochlorella protothecoides, Brassica napus, Capsicum annuum, Festuca pratensis, Hordeum vulgare, Parachlorella kessleri, Phaseolus vulgaris
Cell. Mol. Life Sci.
56
330-347
1999
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5
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14
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5
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7
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16
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7
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7
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14
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9
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5
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16
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17
17
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674404
Hörtensteiner
The key step in chlorophyll br ...
Brassica napus
J. Biol. Chem.
273
15335-15339
1998
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2
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676564
Rodoni
Chlorophyll breakdown in senes ...
Brassica napus
Plant Physiol.
115
669-676
1997
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676565
Rodoni
Partial purification and chara ...
Hordeum vulgare
Plant Physiol.
115
677-682
1997
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1
1
1
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5
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-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
1
-
1
1
-
-
1
-
-
-
1
-
2
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-