HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 1.14.15.17 - pheophorbide a oxygenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The enzyme appears in viruses and cellular organisms
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
1.14.15.17
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
pheophorbide a oxygenase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
epoxypheophorbide a + H2O = red chlorophyll catabolite
spontaneous
-
-
-
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = epoxypheophorbide a + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
(1a)
-
-
-
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
overall reaction
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
pheophorbide-a,ferredoxin:oxygen oxidoreductase (biladiene-forming)
This enzyme catalyses a key reaction in chlorophyll degradation, which occurs during leaf senescence and fruit ripening in higher plants. The enzyme from Arabidopsis contains a Rieske-type iron-sulfur cluster [2] and requires reduced ferredoxin, which is generated either by NADPH through the pentose-phosphate pathway or by the action of photosystem I [4]. While still attached to this enzyme, the product is rapidly converted into primary fluorescent chlorophyll catabolite by the action of EC 1.3.7.12, red chlorophyll catabolite reductase [2,6]. Pheophorbide b acts as an inhibitor. In 18O2 labelling experiments, only the aldehyde oxygen is labelled, suggesting that the other oxygen atom may originate from H2O [1].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
211049-58-0
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cv. Ponkan, collected from a commercial orchard in Quzhou, Zhejiang (China)., gene CitPaO
-
-
cv. Ponkan, collected from a commercial orchard in Quzhou, Zhejiang (China)., gene CitPaO
-
-
cv. Carvendish, from ercial banana orchard at the Pearl River Delta Plain, south-eastern China
-
-
nuclear gene EAS1, i.e. early senescence 1
UniProt
PAO is identical to ACCELERATED CELL DEATH (ACD) 1 and the ortholog of LETHAL LEAF SPOT 1
-
-
significant reduction in pheophorbide a oxygenase activity is detected in nonyellowing mutant nye1-1
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
AtPaO is a Rieske-type iron–sulfur cluster-containing enzyme that is identical to Arabidopsis accelerated cell death 1 and homologous to lethal leaf spot 1 (LLS1) of maize
evolution
PaO is an evolutionarily conserved protein, and EAS1 is 68% identical to the Arabidopsis ACCERLERATED CELL DEATH (ACD1) protein
evolution
-
PaO is an evolutionarily conserved protein, and EAS1 is 68% identical to the Arabidopsis ACCERLERATED CELL DEATH (ACD1) protein
-
malfunction
-
enzyme inhibition or downregulation leads to accumulation of pheophorbide a, a key intermediate of chlorophyll catabolism, which causes cell death in complete darkness in a transgenic Arabidopsis plant, As-ACD1. When senescence is induced by a continuous dark period, leaves of As-ACD1 plants become dehydrated, phenotype, overview
malfunction
during the early growth stage (at the 3th leaf stage), eas1 mutants do not show detectable differences compared to wild-type plants. At the heading stage, old leaves of eas1 mutants turn yellowish or brownish, when wild-type plants are still healthy and green. Small chlorotic lesions are first observed near the tip, and then spread down to the entire leaves of eas1 mutants. At the grain filling stage, the leaf senescence phenotype of eas1 is more apparent compared to wild-type, as most eas1 mutant leaves, culms and sheaths turned to dark brown. In addition to the leaf senescence phenotype, the mature eas1 mutant plants also exhibit apparent developmental defects, such as semi-dwarfism, reduced tiller number and partial-filling
malfunction
-
the absence of PAO in mutants or antisense lines from different plant species results in premature cell death. Phototoxicity of Pheide a is considered to trigger the observed cell death phenotype in a light-dependent manner
malfunction
-
during the early growth stage (at the 3th leaf stage), eas1 mutants do not show detectable differences compared to wild-type plants. At the heading stage, old leaves of eas1 mutants turn yellowish or brownish, when wild-type plants are still healthy and green. Small chlorotic lesions are first observed near the tip, and then spread down to the entire leaves of eas1 mutants. At the grain filling stage, the leaf senescence phenotype of eas1 is more apparent compared to wild-type, as most eas1 mutant leaves, culms and sheaths turned to dark brown. In addition to the leaf senescence phenotype, the mature eas1 mutant plants also exhibit apparent developmental defects, such as semi-dwarfism, reduced tiller number and partial-filling
-
metabolism
enzyme PaO seems to be a key regulator of chlorophyll catabolism
metabolism
-
the enzyme is important in the chlorophyll degradation pathway during leaf senescence. The porphyrin macrocycle of pheophorbide is oxygenolytically cleaved by the joint action of pheophorbide, the pheophorbide a oxygenase, PaO, and the red chlorophyll catabolite reductase, RCCR, overview
metabolism
-
in land plants, chlorophyll is broken down to colorless linear tetrapyrroles in a highly conserved multistep pathway. The pathway is termed the PAO pathway, because the opening of the chlorine macrocycle present in chlorophyll catalyzed by pheophorbide a oxygenase (PAO), the key enzyme of the pathway. The PAO pathway is active during leaf senescence and in ripening fruits. Chlorophyll breakdown does not only occur during leaf senescence and fruit ripening, but also at steady state, during post-harvest and in response to biotic and abiotic stresses, chlorophyll is turned over or degraded, at least to some extent
metabolism
-
in land plants, chlorophyll is broken down to colorless linear tetrapyrroles in a highly conserved multistep pathway. The pathway is termed the PAO pathway, because the opening of the chlorophyllide macrocycle present in chlorophyll catalyzed by pheophorbide a oxygenase (PAO), the key enzyme of the pathway. The PAO pathway is active during leaf senescence and in ripening fruits. Chlorophyll breakdown does not only occur during leaf senescence and fruit ripening, but also at steady state, during post-harvest and in response to biotic and abiotic stresses, chlorophyll is turned over or degraded, at least to some extent
metabolism
Musa cavendishii
-
in land plants, chlorophyll is broken down to colorless linear tetrapyrroles in a highly conserved multistep pathway. The pathway is termed the PAO pathway, because the opening of the chlorophyllide macrocycle present in chlorophyll catalyzed by pheophorbide a oxygenase (PAO), the key enzyme of the pathway. The PAO pathway is active during leaf senescence and in ripening fruits. Chlorophyll breakdown does not only occur during leaf senescence and fruit ripening, but also at steady state, during post-harvest and in response to biotic and abiotic stresses, chlorophyll is turned over or degraded, at least to some extent
metabolism
-
in land plants, chlorophyll is broken down to colorless linear tetrapyrroles in a highly conserved multistep pathway. The pathway is termed the PAO pathway, because the opening of the chlorophyllide macrocycle present in chlorophyll catalyzed by pheophorbide a oxygenase (PAO), the key enzyme of the pathway. The PAO pathway is active during leaf senescence and in ripening fruits. Chlorophyll breakdown does not only occur during leaf senescence and fruit ripening, but also at steady state, during post-harvest and in response to biotic and abiotic stresses, chlorophyll is turned over or degraded, at least to some extent
metabolism
-
in land plants, chlorophyll is broken down to colorless linear tetrapyrroles in a highly conserved multistep pathway. The pathway is termed the PAO pathway, because the opening of the chlorophyllide macrocycle present in chlorophyll catalyzed by pheophorbide a oxygenase (PAO), the key enzyme of the pathway. The PAO pathway is active during leaf senescence and in ripening fruits. Chlorophyll breakdown does not only occur during leaf senescence and fruit ripening, but also at steady state, during post-harvest and in response to biotic and abiotic stresses, chlorophyll is turned over or degraded, at least to some extent
metabolism
-
chlorophyll metabolism and proteins (enzymes) involved, including pheophorbide a oxygenase, overview
metabolism
-
chlorophyll metabolism and proteins (enzymes) involved, including pheophorbide a oxygenase, overview
-
physiological function
chlorophyll breakdown during senescence is an integral part of plant development and leads to the accumulation of colorless catabolites. The loss of green pigment is due to an oxygenolytic opening of the porphyrin macrocycle of pheophorbide (pheide) a followed by a reduction to yield a fluorescent chlorophyll catabolite. This step is comprised of the interaction of two enzymes, pheide a oxygenase (PaO) and red chl catabolite reductase. Senescence-related activity of PaO
physiological function
-
a close correlation between chlorophyll degradation and enzyme expression exists during broccoli senescence
physiological function
gene EAS1 encodes a PaO enzyme containing a putative bipartite chloroplast-targeting peptide, both of which are genetically important for the function of EAS1 during plant growth and development. Pheophorbide a oxygenase (PaO) is a key enzyme for chlorophyll breakdown and involved in chlorophyll degradation during leaf senescence
physiological function
-
physical interaction between pheophorbide a oxygenase, PAO, and red chlorophyll catabolite reductase, RCCR, required for activity, and interaction with stay-green proteins, the latter is required for PaO-RCCR interaction. PaO enzyme expression is highly regulated
physiological function
-
physical interaction between pheophorbide a oxygenase, PAO, and red chlorophyll catabolite reductase, RCCR, required for activity, and interaction with stay-green proteins
physiological function
Musa cavendishii
-
physical interaction between pheophorbide a oxygenase, PAO, and red chlorophyll catabolite reductase, RCCR, required for activity, and interaction with stay-green proteins
physiological function
-
physical interaction between pheophorbide a oxygenase, PAO, and red chlorophyll catabolite reductase, RCCR, required for activity, and interaction with stay-green proteins
physiological function
-
physical interaction between pheophorbide a oxygenase, PAO, and red chlorophyll catabolite reductase, RCCR, required for activity, and interaction with stay-green proteins
physiological function
-
gene EAS1 encodes a PaO enzyme containing a putative bipartite chloroplast-targeting peptide, both of which are genetically important for the function of EAS1 during plant growth and development. Pheophorbide a oxygenase (PaO) is a key enzyme for chlorophyll breakdown and involved in chlorophyll degradation during leaf senescence
-
additional information
-
catabolites such as hypermodified FCCs and urobilinogenoidic chlorophyll catabolites point to divergent paths of the PAO pathway that might exist in some plant species
additional information
-
catabolites such as hypermodified FCCs and urobilinogenoidic chlorophyll catabolites point to divergent paths of the PAO pathway that might exist in some plant species
additional information
Musa cavendishii
-
catabolites such as hypermodified FCCs and urobilinogenoidic chlorophyll catabolites point to divergent paths of the PAO pathway that might exist in some plant species
additional information
-
catabolites such as hypermodified FCCs and urobilinogenoidic chlorophyll catabolites point to divergent paths of the PAO pathway that might exist in some plant species
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
enzyme PAO is a Rieske-type monooxygenase
-
-
?
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
enzyme PAO is a Rieske-type monooxygenase
-
-
?
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Musa cavendishii
-
-
-
-
?
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Musa cavendishii
-
enzyme PAO is a Rieske-type monooxygenase
-
-
?
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
enzyme PAO is a Rieske-type monooxygenase
-
-
?
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
-
?
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
enzyme PAO is a Rieske-type monooxygenase
-
-
?
additional information
?
-
-
ACD1 is involved in PaO activity, and its inhibition led to photooxidative destruction of the cell
-
-
-
additional information
?
-
PaO expression is correlated positively with senescence. The in vivo function of PaO is the degradation of pheide a during senescence
-
-
-
additional information
?
-
-
rred chlorophyll catabolite reductase together with pheophorbide a oxygenase is required for the detoxification of chlorophyll catabolites
-
-
-
additional information
?
-
-
significant reduction in pheophorbide a oxygenase activity is detected in nonyellowing mutant nye1-1. NYE1 plays an important regulatory role in chlorophyll degradation during senescence by modulating pheophorbide a oxygenase activity
-
-
-
additional information
?
-
-
the enzyme is involved in breakdown of pheophorbide a in chlorophyll degradation, involvement of pheophorbide a in the signaling pathway for programmed cell death, overview
-
-
-
additional information
?
-
-
substrate specificity of PAO for pheophorbide (Pheide) a
-
-
-
additional information
?
-
-
substrate specificity of PAO for pheophorbide (Pheide) a
-
-
-
additional information
?
-
-
the enzyme is involved in the mechanism of banana fruit peel staying green after riping, detailed overview. The stay-green ripe bananas exhibit a similar phenotype to type C stay-green mutants
-
-
-
additional information
?
-
Musa cavendishii
-
substrate specificity of PAO for pheophorbide (Pheide) a
-
-
-
additional information
?
-
-
substrate specificity of PAO for pheophorbide (Pheide) a
-
-
-
additional information
?
-
PaO is a Fe-dependent monooxygenase that oxygenolytically opens the porphyrin macrocycle of pheophorbide a and converts pheophorbide a to red chlorophyll catabolite (RCC)
-
-
-
additional information
?
-
PaO is a Fe-dependent monooxygenase that oxygenolytically opens the porphyrin macrocycle of pheophorbide a and converts pheophorbide a to red chlorophyll catabolite (RCC)
-
-
-
additional information
?
-
-
SGR absence in JI2775 does not influence the PAO pathway
-
-
-
additional information
?
-
-
SGR absence in JI2775 does not influence the PAO pathway
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
enzyme PAO is a Rieske-type monooxygenase
-
-
?
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Q9FYC2
-
-
-
?
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
enzyme PAO is a Rieske-type monooxygenase
-
-
?
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Musa cavendishii
-
enzyme PAO is a Rieske-type monooxygenase
-
-
?
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
enzyme PAO is a Rieske-type monooxygenase
-
-
?
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Q10RT5
-
-
-
?
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
Q10RT5
-
-
-
?
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
-
enzyme PAO is a Rieske-type monooxygenase
-
-
?
additional information
?
-
-
ACD1 is involved in PaO activity, and its inhibition led to photooxidative destruction of the cell
-
-
-
additional information
?
-
Q9FYC2
PaO expression is correlated positively with senescence. The in vivo function of PaO is the degradation of pheide a during senescence
-
-
-
additional information
?
-
-
rred chlorophyll catabolite reductase together with pheophorbide a oxygenase is required for the detoxification of chlorophyll catabolites
-
-
-
additional information
?
-
-
significant reduction in pheophorbide a oxygenase activity is detected in nonyellowing mutant nye1-1. NYE1 plays an important regulatory role in chlorophyll degradation during senescence by modulating pheophorbide a oxygenase activity
-
-
-
additional information
?
-
-
the enzyme is involved in breakdown of pheophorbide a in chlorophyll degradation, involvement of pheophorbide a in the signaling pathway for programmed cell death, overview
-
-
-
additional information
?
-
-
the enzyme is involved in the mechanism of banana fruit peel staying green after riping, detailed overview. The stay-green ripe bananas exhibit a similar phenotype to type C stay-green mutants
-
-
-
additional information
?
-
Q10RT5
PaO is a Fe-dependent monooxygenase that oxygenolytically opens the porphyrin macrocycle of pheophorbide a and converts pheophorbide a to red chlorophyll catabolite (RCC)
-
-
-
additional information
?
-
Q10RT5
PaO is a Fe-dependent monooxygenase that oxygenolytically opens the porphyrin macrocycle of pheophorbide a and converts pheophorbide a to red chlorophyll catabolite (RCC)
-
-
-
additional information
?
-
-
SGR absence in JI2775 does not influence the PAO pathway
-
-
-
additional information
?
-
-
SGR absence in JI2775 does not influence the PAO pathway
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
iron-sulfur centre
-
encoded protein contains the typical Rieske 2Fe-2S and mononuclear iron-binding domains as well as the C-terminus CxxC motif
additional information
-
the enzyme contains an additional mononuclear iron center that is responsible for the activation of molecular oxygen. Electrons required to supply the iron-redox cycle of PAO are provided by reduced ferredoxin
-
additional information
-
the enzyme contains an additional mononuclear iron center that is responsible for the activation of molecular oxygen. Electrons required to supply the iron-redox cycle of PAO are provided by reduced ferredoxin
-
additional information
Musa cavendishii
-
the enzyme contains an additional mononuclear iron center that is responsible for the activation of molecular oxygen. Electrons required to supply the iron-redox cycle of PAO are provided by reduced ferredoxin
-
additional information
-
the enzyme contains an additional mononuclear iron center that is responsible for the activation of molecular oxygen. Electrons required to supply the iron-redox cycle of PAO are provided by reduced ferredoxin
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
Fe2+
Iron-sulfur cluster
[2Fe-2S] cluster
Rieske domain with a [2Fe-2S] cluster at its N-terminal region that accepts electrons from a reductase, and a functional PaO domain at the carboxyl-terminal region
Fe2+
-
in iron-sulfur clusters, the enzyme contains an additional mononuclear iron center that is responsible for the activation of molecular oxygen. Electrons required to supply the iron-redox cycle of PAO are provided by reduced ferredoxin
Fe2+
-
in iron-sulfur clusters, the enzyme contains an additional mononuclear iron center that is responsible for the activation of molecular oxygen. Electrons required to supply the iron-redox cycle of PAO are provided by reduced ferredoxin
Fe2+
Musa cavendishii
-
in iron-sulfur clusters, the enzyme contains an additional mononuclear iron center that is responsible for the activation of molecular oxygen. Electrons required to supply the iron-redox cycle of PAO are provided by reduced ferredoxin
Fe2+
-
in iron-sulfur clusters, the enzyme contains an additional mononuclear iron center that is responsible for the activation of molecular oxygen. Electrons required to supply the iron-redox cycle of PAO are provided by reduced ferredoxin
Fe2+
-
in iron-sulfur clusters, the enzyme contains an additional mononuclear iron center that is responsible for the activation of molecular oxygen. Electrons required to supply the iron-redox cycle of PAO are provided by reduced ferredoxin
Iron-sulfur cluster
AtPaO is a Rieske-type iron–sulfur cluster-containing enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
accumulation of sugars in the peel is a major factor regulating chlorophyll degradation
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
BnPaO1 is identified during early seed development. Increase in PaO activity during seed maturation corresponds to a decrease in the phosphorylation of the PaO enzyme; BnPaO2 is identified during early seed development and in maturing, degreening seeds. Increase in PaO activity during seed maturation corresponds to a decrease in the phosphorylation of the PaO enzyme
additional information
-
PAO mRNA and PAO proteins are present at low levels in presenescent leaves, but are highly enriched during senescence. PAO is upregulated rapidly upon wounding
BnPaO1 is identified in senescing canola leaves; BnPaO2 is identified in senescing canola leaves
-
constitutively expressed, upregulated by dark-induced senescence in rice leaves. Senescence-induced expression is enhanced by abscisic acid, but inhibited by cytokinin
additional information
PaO activity is found only during senescence
additional information
enzyme expression analysis in different tissues of rice
additional information
-
enzyme expression analysis in different tissues of rice
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PaO is localized in the chloroplast inner envelope
integral enzyme, the enzyme contains two putative transit peptides at its N-terminus, which are essential for its functionality, suggesting that targeting of the enzyme to the chloroplast is likely mediated by a putative bipartite transit peptide. Once the precursors of luminal proteins reach the stroma, the first transit peptide for the chloroplast envelop is cleaved off by the stroma processing proteases, and then the intermediate precursor lacking the first transit peptide is translocated into the thylakoid lumen through the second transit peptide
-
integral enzyme, the enzyme contains two putative transit peptides at its N-terminus, which are essential for its functionality, suggesting that targeting of the enzyme to the chloroplast is likely mediated by a putative bipartite transit peptide. Once the precursors of luminal proteins reach the stroma, the first transit peptide for the chloroplast envelop is cleaved off by the stroma processing proteases, and then the intermediate precursor lacking the first transit peptide is translocated into the thylakoid lumen through the second transit peptide
-
the enzyme contains a chloroplast transit peptide
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphorylation is a posttranslational control mechanism; phosphorylation is a posttranslational control mechanism
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli; gene PaO, functional recombinant expression in Escherichia coli strain C43
gene EAS1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, quantitative RT-PCR analysis of EAS1 gene expression in different tissues of rice. Only a short version of EAS1 lacking the first putative transit peptide, but not the full-length EAS1, is capable of rescuing the Arabidopsis acd1 mutant phenotype
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is reduced during the fruit ripening at 30°C, when compared with 20°C, chlorophyll degradation is repressed at 30°C at various steps along the Chl catabolic pathway
-
expression is not induced by salicylic acid and gibberellic acid or after infection with Puccinia striiformis f. sp. tritici
-
expression is upregulated by abscisic acid and methyl jasmonate and can be induced by wounding, low temperature, and high salinity
-
expression of gene CitPaO is not affected by ethylene treatment, while ethylene increases the xpression of several other enzymes of the chlorophyll degradation pathway, overview
Expression of mRNA for pheophorbide a oxygenase is suppressed by expression of Acd1 antisense RNA
-
expression of gene CitPaO is not affected by ethylene treatment, while ethylene increases the xpression of several other enzymes of the chlorophyll degradation pathway, overview
-
expression of gene CitPaO is not affected by ethylene treatment, while ethylene increases the xpression of several other enzymes of the chlorophyll degradation pathway, overview
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
pheophorbide a, a key intermediate of chlorophyll catabolism, causes cell death in complete darkness in a transgenic Arabidopsis plant, As-ACD1. Expression of mRNA for pheophorbide a oxygenase is suppressed by expression of Acd1 antisense RNA. As-ACD1 accumulates an excessive amount of pheophorbide a when chlorophyll breakdown occurs. When senescence is induced by a continuous dark period, leaves of As-ACD1 plants become dehydrated, phenotype, overview
additional information
screening and genotyping for gene eas1 mutants showing an early senescence phenotype, overview. The eas1 mutant is defective in Chl breakdown, which may cause the accumulation of Chl intermediates, leading to the cell death phenotype in light conditions
additional information
-
screening and genotyping for gene eas1 mutants showing an early senescence phenotype, overview. The eas1 mutant is defective in Chl breakdown, which may cause the accumulation of Chl intermediates, leading to the cell death phenotype in light conditions
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 1.14.15.17)
html completed
Information
