Information on EC 1.14.15.17 - pheophorbide a oxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.15.17
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RECOMMENDED NAME
GeneOntology No.
pheophorbide a oxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
epoxypheophorbide a + H2O = red chlorophyll catabolite
show the reaction diagram
spontaneous
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pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = epoxypheophorbide a + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
show the reaction diagram
(1a)
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pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2 = red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
overall reaction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
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Porphyrin and chlorophyll metabolism
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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].
CAS REGISTRY NUMBER
COMMENTARY hide
211049-58-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
cv. Ponkan, collected from a commercial orchard in Quzhou, Zhejiang (China)., gene CitPaO
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Manually annotated by BRENDA team
cv. Ponkan, collected from a commercial orchard in Quzhou, Zhejiang (China)., gene CitPaO
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Manually annotated by BRENDA team
L. Carina
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Manually annotated by BRENDA team
cv. Carvendish, from ercial banana orchard at the Pearl River Delta Plain, south-eastern China
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Manually annotated by BRENDA team
Musa cavendishii
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Manually annotated by BRENDA team
nuclear gene EAS1, i.e. early senescence 1
UniProt
Manually annotated by BRENDA team
nuclear gene EAS1, i.e. early senescence 1
UniProt
Manually annotated by BRENDA team
JI2775
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Manually annotated by BRENDA team
JI2775
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
PAO is identical to ACCELERATED CELL DEATH (ACD) 1 and the ortholog of LETHAL LEAF SPOT 1
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
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
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
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enzyme PAO is a Rieske-type monooxygenase
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?
pheophorbide a + NADPH + H+ + O2
red chlorophyll catabolite + NADP+
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
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
pheophorbide a + 2 reduced ferredoxin [iron-sulfur] cluster 2 H+ + O2
red chlorophyll catabolite + 2 oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
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enzyme PAO is a Rieske-type monooxygenase
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
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iron-sulfur centre
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encoded protein contains the typical Rieske 2Fe-2S and mononuclear iron-binding domains as well as the C-terminus CxxC motif
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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accumulation of sugars in the peel is a major factor regulating chlorophyll degradation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.006
pheophorbide a
pH 7.0, 24°C, recombinant enzyme
additional information
additional information
Michaelis-Menten kinetics
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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active in vivo at 20°C, inactivate at 30°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2
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calculated
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
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
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58300
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x * 58300, calculated
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 58300, calculated
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
phosphorylation is a posttranslational control mechanism; phosphorylation is a posttranslational control mechanism
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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expression in Escherichia coli; gene PaO, functional recombinant expression in Escherichia coli strain C43
gene CitPaO, expression analysis by quantitive real-time PCR
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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
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
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expression is not induced by salicylic acid and gibberellic acid or after infection with Puccinia striiformis f. sp. tritici
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expression is upregulated by abscisic acid and methyl jasmonate and can be induced by wounding, low temperature, and high salinity
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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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information