Information on EC 3.1.1.82 - pheophorbidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.1.82
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RECOMMENDED NAME
GeneOntology No.
pheophorbidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
C-132-carboxypyropheophorbide a = pyropheophorbide a + CO2
show the reaction diagram
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pheophorbide a + H2O = C-132-carboxypyropheophorbide a + methanol
show the reaction diagram
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pheophorbide a + H2O = pyropheophorbide a + methanol + CO2
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
chlorophyll a degradation I
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Porphyrin and chlorophyll metabolism
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
pheophorbide-a hydrolase
This enzyme forms part of the chlorophyll degradation pathway, and is found in higher plants and in algae. In higher plants it participates in de-greening processes such as fruit ripening, leaf senescence, and flowering. The enzyme exists in two forms: type 1 is induced by senescence whereas type 2 is constitutively expressed [1,2]. The enzyme is highly specific for pheophorbide as substrate (with a preference for pheophorbide a over pheophorbide b) as other chlorophyll derivatives such as protochlorophyllide a, pheophytin a and c, chlorophyll a and b, and chlorophyllide a cannot act as substrates [2]. Another enzyme, called pheophorbide demethoxycarbonylase (PDC), produces pyropheophorbide a from pheophorbide a without forming an intermediate although the precise reaction is not yet known [1].
CAS REGISTRY NUMBER
COMMENTARY hide
186207-01-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
low activity
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Manually annotated by BRENDA team
Chl b-less mutant NL-105
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
no activity in Camellia sinensis
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Manually annotated by BRENDA team
no activity in Chlamydomonas reinhardtii
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Manually annotated by BRENDA team
no activity in Chrysanthemum coronarium
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Manually annotated by BRENDA team
no activity in Corchorus olitorius
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Manually annotated by BRENDA team
no activity in Equisetum arvense
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Manually annotated by BRENDA team
no activity in Ginkgo biloba
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Manually annotated by BRENDA team
no activity in Hordeum vulgare
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Manually annotated by BRENDA team
no activity in Lepisorus thunbergianus
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Manually annotated by BRENDA team
no activity in Perilla frutescens
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Manually annotated by BRENDA team
no activity in Petroselinum sativum
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Manually annotated by BRENDA team
no activity in Pisum sativum
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Manually annotated by BRENDA team
no activity in Rumex acetosa
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Manually annotated by BRENDA team
no activity in Spinacia oleracea
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Manually annotated by BRENDA team
Zucc.
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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MES16-deficient mutants (mes16) are still able to degrade chlorophyll, but they accumulate FCCs (fluorescent chlorophyll) and NCCs (nonfluorescent chlorophyll) catabolites with an intact C132-carboxymethyl group. As a consequence, FCC-to-NCC isomerization is compromised and the mutants accumulate large quantities of FCCs, which causes senescent leaves to fluoresce under UV light
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
bacteriopheophorbide a + H2O
?
show the reaction diagram
pheophorbide a + H2O
pyropheophorbide a + methanol + CO2
show the reaction diagram
pheophorbide b + H2O
?
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 + H2O
pyropheophorbide a + methanol + CO2
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cycloheximide
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methanol
N-ethylmaleimide
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1 mM, 11% inhibition, Phedase type 1
phenylmethylsulfonic fluoride
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1 mM, 26.4% inhibition, Phedase type 2; 1 mM, 61% inhibition, Phedase type 1
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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1 mM, 22% activation, Phedase type 1; 1 mM, 9% activation, Phedase type 2
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.037 - 0.039
bacteriopheophorbide a
0.0125 - 0.955
pheophorbide a
0.232 - 0.243
pheophorbide b
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
71.6
methanol
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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in slow drying the phedase shows an increase of 0.94fold of its initial activity in fresh before 24 h but decreases sharply as time goes on with 25% activity remaining ultimately. Phedase of the 50°C samples in fast drying show a constant decrease
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
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Phedase type 2
7 - 7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 80
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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enzyme activity increases dependent on the age of the cell
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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extraplastidic part of the cell
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
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x * 28000 + x + 29000, SDS-PAGE
55000
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PPD-GST fusion protein, SDS-PAGE
57000
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2 * 57000, Phedase type 1, SDS-PAGE
83000
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1 * 87000 + 1 * 83000, SDS-PAGE
87000
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1 * 87000 + 1 * 83000, SDS-PAGE
105000
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gel filtration
113000
170000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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x * 28000 + x + 29000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
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50% loss of activity
68
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50% loss of activity at 67.5°C, Phedase type 1; 50% loss of activity at 67.5°C, Phedase type 2
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for over a year
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4°C, stable for a few months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Phedase type 1; Phedase type 2
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PPD type 1; PPD type 2
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single-step affinity chromatography through a GSTrap FF column
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using Ni-NTA chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
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PPD type 1; PPD type 2
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recombinant PPD is produced using a glutathione S-transferase (GST) fusion system. The PPD and GST genes are fused to a pGEX-2T vector and expressed in Escherichia coli BL21(DE3)pLysS strain under the control of a T7 promoter as a fusion protein
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