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Information on EC 1.3.1.33 - protochlorophyllide reductase and Organism(s) Arabidopsis thaliana and UniProt Accession P21218
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1.3.1.33 protochlorophyllide reductaseIUBMB Comments
The enzyme catalyses a light-dependent trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration.
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Word Map
- 1.3.1.33
- chloroplast
- seedlings
- plastid
-
etiolated
- etioplasts
- barley
-
prolamellar
-
dark-grown
-
angiosperm
- thylakoids
- tetrapyrrole
- bacteriochlorophyll
-
light-harvesting
- plb
-
photoreduction
-
lpors
-
nitrogenase-like
-
phytochrome
-
photoactive
- chelatase
-
phototransformation
-
1.6.99.1
-
photoconversion
-
mg-chelatase
- mg-protoporphyrin
-
pigment-protein
- chls
-
photoenzyme
- l-protein
-
de-etiolation
-
shibata
- analysis
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
protochlorophyllide oxidoreductase, protochlorophyllide reductase, nadph:protochlorophyllide oxidoreductase, nadph-protochlorophyllide oxidoreductase, por a, por b, osporb, dark-operative protochlorophyllide oxidoreductase, lipor, nadph protochlorophyllide oxidoreductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
light-dependent NADPH:protochlorophyllide oxidoreductase
LPOR
NADPH-protochlorophyllide oxidoreductase
-
-
-
-
NADPH-protochlorophyllide reductase
-
-
-
-
NADPH2-protochlorophyllide oxidoreductase
-
-
-
-
NADPH:protochlorophyllide oxidoreductase
POR
POR C
PORA
PORB
PORC
protochlorophyllide oxidoreductase
protochlorophyllide oxidoreductase A
protochlorophyllide oxidoreductase C
protochlorophyllide photooxidoreductase
-
-
-
-
light-dependent NADPH:protochlorophyllide oxidoreductase
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LPOR
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-
-
-
protochlorophyllide oxidoreductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
SYSTEMATIC NAME
IUBMB Comments
chlorophyllide-a:NADP+ 7,8-oxidoreductase
The enzyme catalyses a light-dependent trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration.
CAS REGISTRY NUMBER
COMMENTARY
68518-04-7
-
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
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
the enzyme (LPOR) catalyzes a photocatalytic reaction
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
key enzyme of chlorophyll biosynthesis
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
light-dependent reaction. Isoform PORB and PORC are interchangeable and functionally redundant in developed plants. PORB as well as PORA, functions in assembly of prolamellar bodies and in photoactive protochlorophylluide formation in etiolated seedlings. At the onset of greening, prolamellar bodies are important for efficient capture of light energy for photoconversion under various light conditions, and PORC, which is induced by light irradiation, contributes to photoprotection during greening of the etiolated seedlings
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
light-dependent reaction
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
light-dependent reaction
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
the enzyme (LPOR) catalyzes a photocatalytic reaction
-
-
?
NATURAL SUBSTRATE
NATURAL 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
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
the enzyme (LPOR) catalyzes a photocatalytic reaction
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
key enzyme of chlorophyll biosynthesis
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
light-dependent reaction. Isoform PORB and PORC are interchangeable and functionally redundant in developed plants. PORB as well as PORA, functions in assembly of prolamellar bodies and in photoactive protochlorophylluide formation in etiolated seedlings. At the onset of greening, prolamellar bodies are important for efficient capture of light energy for photoconversion under various light conditions, and PORC, which is induced by light irradiation, contributes to photoprotection during greening of the etiolated seedlings
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
the enzyme (LPOR) catalyzes a photocatalytic reaction
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
light-dependent enzyme. Enzyme (LPOR) activity is induced by light and is fully inhibited in the dark
-
additional information
light-dependent enzyme. Enzyme (LPOR) activity is induced by light and is fully inhibited in the dark
-
additional information
light-dependent enzyme. Enzyme (LPOR) activity is induced by light and is fully inhibited in the dark
-
additional information
light-dependent enzyme. Enzyme (LPOR) activity is induced by light and is fully inhibited in the dark
-
additional information
light-dependent enzyme. Enzyme (LPOR) activity is induced by light and is fully inhibited in the dark
-
additional information
light-dependent enzyme. Enzyme (LPOR) activity is induced by light and is fully inhibited in the dark
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosphatidylglycerol
active complexes of PORB preferentially bind to the lipid membranes due to the interaction with phosphatidylglycerol
additional information
-
phosphatidylglycerol and sulfoquinovosyl diacylglycerol increase the affinity towards NADPH a 100fold
-
phosphatidylglycerol
isoform PORC can bind chlorophyllide without the lipids under low NADPH concentrations. When the lipid concentration is high, PORC can oligomerize on the lipid membrane, which increases its activity
phosphatidylglycerol
the interaction with PG increases the affinity of the PORA towards NADPH, so active PORA complexes preferentially bind to the lipid membranes
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LPOR-B is present in etiolated tissue. LPOR-A is expressed during early phases of development when large amounts of pigments need to be synthesized quickly, while LPOR-B and LPOR-C are responsible for the bulk chlorophyll synthesis of adult or green plants
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translocon constituent toc33 is indispensable for the import of isoform PorB
undetectable in dark-grown cells, light response during greening. Expression in mature cells
LPOR-A is present in etiolated tissue. LPOR-A is expressed during early phases of development when large amounts of pigments need to be synthesized quickly, while LPOR-B and LPOR-C are responsible for the bulk chlorophyll synthesis of adult or green plants
additional information
high expression in dark-grown cells, no light response during greening. Constitutive enzym, expression in mature cells
high expression in dark-grown cells, no light response during greening. Very low expression in mature cells
-
translocon constituent toc33 is indispensable for the import of isoform PorB
-
-
-
strong expression of enzyme isoforms PorA, PorB in early seedling development
additional information
LPOR-C is expressed typically in green tissues
additional information
LPOR-C is expressed typically in green tissues
additional information
LPOR-C is expressed typically in green tissues
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes
LPOR is an integral monotopic membrane protein which is permanently attached to one side of the plastid inner membrane. Tubuloreticular prolamellar body membrane, envelope membrane
the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes
the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes
the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes
LPOR is an integral monotopic membrane protein which is permanently attached to one side of the plastid inner membrane. Tubuloreticular prolamellar body membrane, envelope membrane
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nucleus-encoded enzyme is synthesized as a larger precursor in the cytosol and imported into the plastid in a substrate-dependent manner. Plastid envelope membrane proteins, called protochlorophyllide-dependent translocon proteins, Ptcs, interact with pPORA during import. Partial suppression of pPORB import in white light
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import of isoform PorA into plastids of cotyledons is substrate-dependent and organ-specific
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
all modern sequences of light-dependent protochlorophyllide oxidoreductase POR diverged from a single sequence about 1.36 billlion years ago. The LPOR gene was then duplicated at least 10 times in angiosperms, leading to the formation of two or even more LPOR isoforms in multiple species. In the case of Arabidopsis thaliana, isoforms PORA and PORB originated in one duplication event, in contrary to the isoform PORC, which diverged first
evolution
all modern sequences of light-dependent protochlorophyllide oxidoreductase POR diverged from a single sequence about 1.36 billlion years ago. The LPOR gene was then duplicated at least 10 times in angiosperms, leading to the formation of two or even more LPOR isoforms in multiple species. In the case of Arabidopsis thaliana, isoforms PORA and PORB originated in one duplication event, in contrary to the isoform PORC, which diverged first
malfunction
metabolism
-
the enzyme allows for the rapid formation of chlorophyll after illumination while avoiding photodamage. The formation of protochlorophyllide-enzyme(LPOR) complexes is an initial step of etioplast development. the formation of pigment-LPOR complexes in prolamellar bodies is essential for the rapid and safe conversion of etioplasts to chloroplasts during the dark-to-light transition
malfunction
-
a PORA null mutant (porA-1) and PORA RNAi lines display severe photoautotrophic growth defects, which can be partially rescued on sucrose-supplemented growth media. Elimination of PORA during skotomorphogenesis results in reductions in the volume and frequency of prolamellar bodies, and in photoactive Pchlide conversion
malfunction
-
it is shown that a porA-1 null mutant (porA mutant) carries a second dissociation insertion in another gene closely linked to the PORA gene that is expected to affect the phenotype of the porA mutant
malfunction
-
it is shown that an Arabidopsis thaliana porB-1 porC-1 double mutant can be functionally rescued by the addition of ectopically expressed PORA, which suffices in the absence of either PORB or PORC to direct bulk chlorophyll synthesis and normal plant development
malfunction
-
overexpression of PORC in Arabidopsis thaliana reduces the accumulation of protochlorophyllide in high light-grown plants that results in minimal generation of 1O2 and plants are protected from 1O2-mediated oxidative damage caused by high light. PORC overexpression protects the plants from oxidative herbicidal action of 5-aminolevulinicacid. Overexpression of PORC results in coordinated upregulation of gene/protein expression of several Chl biosynthetic pathway enzymes resulting in enhanced Chl synthesis in light-grown plants
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PORB_ARATH
401
0
43359
Swiss-Prot
Chloroplast (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C276A
-
the mutant is hypersensitive to high-light conditions during greening
Cys303A
-
the mutant is hypersensitive to high-light conditions during greening
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the chaperone-like protein of por1 (CPP1) plays a role in the regulation of enzyme stability and function
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using a chitin bead column, the chitin-intein tag is removed
using a chitin bead column, the chitin-intein tag is removed
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
yes into the vector pTYB for expression in Escherichia coli BL21DE3 cells
cDNAs and/or gens encoding POR, also referred to as LPCR or PCR in some studies isolated
-
yes into the vector pTYB for expression in Escherichia coli BL21DE3 cells, for the construction of transgenic plants pDONR/ZeO and pGWB2 vectors are used
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
LPOR-A is expressed during early phases of development when large amounts of pigments need to be synthesized quickly, while LPOR-B and LPOR-C are responsible for the bulk chlorophyll synthesis of adult or green plants
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schulz, R.; Steinmueller, K.; Klaas, M.; Forreiter, C.; Rasmussen, S.; Hiller, C.; Apel, K.
Nucleotide sequence of a cDNA coding for the NADPH-protochlorophyllide oxidoreductase (PCR) of barley (Hordeum vulgare L.) and its expression in Escherichia coli
Mol. Gen. Genet.
217
355-361
1989
Arabidopsis thaliana, Hordeum vulgare, Triticum aestivum
Armstrong, G.A.; Runge, S.; Frick, G.; Sperling, U.; Apel, K.
Identification of NADPH:protochlorophyllide oxidoreductases A and B: a branched pathway for light-dependent chlorophyll biosynthesis in Arabidopsis thaliana
Plant Physiol.
108
1505-1517
1995
Arabidopsis thaliana, Avena sativa, Hordeum vulgare, Lepidium sativum, Pinus mugo, Pinus strobus, Pinus taeda, Pisum sativum, Triticum aestivum, Zea mays
Chahdi, M.A.O.; Schoefs, B.; Franck, F.
Isolation and characterization of photoactive complexes of NADPH:protochlorophyllide oxidoreductase from wheat
Planta
206
673-680
1998
Arabidopsis thaliana, Cucumis sativus, Hordeum vulgare, Phaseolus vulgaris, Pisum sativum, Triticum aestivum
-
Klement, H.; Helfrich, M.; Oster, U.; Schoch, S.; Rudiger, W.
Pigment-free NADPH:protochlorophyllide oxidoreductase from Avena sativa L: purification and substrate specificity
Eur. J. Biochem.
265
862-874
1999
Arabidopsis thaliana, Avena sativa, Hordeum vulgare, Pisum sativum
Lebedev, N.; Timko, M.P.
Protochlorophyllide oxidoreductase B-catalyzed protochlorophyllide photoreduction in vitro: insight into the mechanism of chlorophyll formation in light-adapted plants
Proc. Natl. Acad. Sci. USA
96
9954-9959
1999
Arabidopsis thaliana, Hordeum vulgare
Franck, F.; Sperling, U.; Frick, G.; Pochert, B.; Van Cleve, B.; Apel, K.; Armstrong, G.A.
Regulation of etioplast pigment-protein complexes, inner membrane architecture, and protochlorophyllide a chemical heterogeneity by light-dependent NADPH:protochlorophyllide oxidoreductases A and B
Plant Physiol.
124
1678-1696
2000
Arabidopsis thaliana, Avena sativa
Su, Q.; Frick, G.; Armstrong, G.; Apel, K.
POR C of Arabidopsis thaliana: a third light- and NADPH-dependent protochlorophyllide oxidoreductase that is differentially regulated by light
Plant Mol. Biol.
47
805-813
2001
Arabidopsis thaliana, Chlamydomonas reinhardtii, Cucumis sativus, Cucurbita pepo, Hordeum vulgare, Leptolyngbya boryana, Marchantia paleacea, Pinus mugo, Pinus strobus, Pinus taeda, Pisum sativum, Rhodobacter capsulatus
Pattanayak, G.K.; Tripathy, B.C.
Catalytic function of a novel protein protochlorophyllide oxidoreductase C of Arabidopsis thaliana
Biochem. Biophys. Res. Commun.
291
921-924
2002
Arabidopsis thaliana (O48741), Arabidopsis thaliana
Masuda, T.; Takamiya, K.i.
Novel insights into the enzymology, regulation and physiological functions of light-dependent protochlorophyllide oxidoreductase in angiosperms
Photosynth. Res.
81
1-29
2004
Amaranthus tricolor, Anabaena sp., Arabidopsis thaliana (O48741), Arabidopsis thaliana (P21218), Arabidopsis thaliana (Q42536), Avena sativa (P15904), Bigelowiella natans, Chlamydomonas reinhardtii (Q39617), Cucumis sativus (Q41249), Daucus carota (Q9SDT1), Gloeobacter violaceus, Hordeum vulgare (P13653), Hordeum vulgare (Q42850), Lactuca sativa, Leptolyngbya boryana, Marchantia paleacea (O80333), Nicotiana tabacum (Q8LSZ2), Nicotiana tabacum (Q8LSZ3), Oryza sativa, Pinus mugo, Pinus mugo (Q41203), Pinus strobus, Pinus taeda, Pisum sativum, Prochlorococcus marinus, Solanum lycopersicum, Synechocystis sp. (Q59987), Thermosynechococcus vestitus BP-1, Triticum aestivum (Q41578), Vigna radiata (Q9LKH8)
Masuda, T.; Fusada, N.; Oosawa, N.; Takamatsu, K.; Yamamoto, Y.Y.; Ohto, M.; Nakamura, K.; Goto, K.; Shibata, D.; Shirano, Y.; Hayashi, H.; Kato, T.; Tabata, S.; Shimada, H.; Ohta, H.; Takamiya, K.
Functional analysis of isoforms of NADPH: protochlorophyllide oxidoreductase (POR), PORB and PORC, in Arabidopsis thaliana
Plant Cell Physiol.
44
963-974
2003
Arabidopsis thaliana
Reinbothe, S.; Pollmann, S.; Springer, A.; James, R.J.; Tichtinsky, G.; Reinbothe, C.
A role of Toc33 in the protochlorophyllide-dependent plastid import pathway of NADPH:protochlorophyllide oxidoreductase (POR) A
Plant J.
42
1-12
2005
Arabidopsis thaliana
Kim, C.; Ham, H.; Apel, K.
Multiplicity of different cell- and organ-specific import routes for the NADPH-protochlorophyllide oxidoreductases A and B in plastids of Arabidopsis seedlings
Plant J.
42
329-340
2005
Arabidopsis thaliana
Pollmann, S.; Springer, A.; Buhr, F.; Lahroussi, A.; Samol, I.; Bonneville, J.M.; Tichtinsky, G.; von Wettstein, D.; Reinbothe, C.; Reinbothe, S.
A plant porphyria related to defects in plastid import of protochlorophyllide oxidoreductase A
Proc. Natl. Acad. Sci. USA
104
2019-2023
2007
Arabidopsis thaliana
Schemenewitz, A.; Pollmann, S.; Reinbothe, C.; Reinbothe, S.
A substrate-independent, 14:3:3 protein-mediated plastid import pathway of NADPH:protochlorophyllide oxidoreductase A
Proc. Natl. Acad. Sci. USA
104
8538-8543
2007
Arabidopsis thaliana
Masuda, S.; Ikeda, R.; Masuda, T.; Hashimoto, H.; Tsuchiya, T.; Kojima, H.; Nomata, J.; Fujita, Y.; Mimuro, M.; Ohta, H.; Takamiya, K.
Prolamellar bodies formed by cyanobacterial protochlorophyllide oxidoreductase in Arabidopsis
Plant J.
58
952-960
2009
Synechocystis sp. PCC 6803, Gloeobacter violaceus, Arabidopsis thaliana (O48741), Arabidopsis thaliana (P21218), Arabidopsis thaliana (Q42536)
Yuan, M.; Zhang, D.W.; Zhang, Z.W.; Chen, Y.E.; Yuan, S.; Guo, Y.R.; Lin, H.H.
Assembly of NADPH: protochlorophyllide oxidoreductase complex is needed for effective greening of barley seedlings
J. Plant Physiol.
169
1311-1316
2012
Arabidopsis thaliana, Hordeum vulgare
Paddock, T.; Lima, D.; Mason, M.E.; Apel, K.; Armstrong, G.A.
Arabidopsis light-dependent protochlorophyllide oxidoreductase A (PORA) is essential for normal plant growth and development
Plant Mol. Biol.
78
447-460
2012
Arabidopsis thaliana
Kim, C.; Apel, K.
Arabidopsis light-dependent NADPH: protochlorophyllide oxidoreductase A (PORA) is essential for normal plant growth and development: an addendum
Plant Mol. Biol.
80
237-240
2012
Arabidopsis thaliana
Pattanayak, G.; Tripathy, B.
Overexpression of protochlorophyllide oxidoreductase c regulates oxidative stress in arabidopsis
PLoS ONE
6
e26532
2011
Arabidopsis thaliana
Gabruk, M.; Mysliwa-Kurdziel, B.; Kruk, J.
MGDG, PG and SQDG regulate the activity of light-dependent protochlorophyllide oxidoreductase
Biochem. J.
474
1307-1320
2017
Arabidopsis thaliana
Gabruk, M.; Mysliwa-Kurdziel, B.
Light-dependent protochlorophyllide oxidoreductase: phylogeny, regulation, and catalytic properties
Biochemistry
54
5255-5262
2015
Arabidopsis thaliana
Lee, J.Y.; Lee, H.S.; Song, J.Y.; Jung, Y.J.; Reinbothe, S.; Park, Y.I.; Lee, S.Y.; Pai, H.S.
Cell growth defect factor1/chaperone-like protein of POR1 plays a role in stabilization of light-dependent protochlorophyllide oxidoreductase in Nicotiana benthamiana and Arabidopsis
Plant Cell
25
3944-3960
2013
Arabidopsis thaliana, Nicotiana benthamiana
Buhr, F.; Lahroussi, A.; Springer, A.; Rustgi, S.; von Wettstein, D.; Reinbothe, C.; Reinbothe, S.
NADPH:protochlorophyllide oxidoreductase B (PORB) action in Arabidopsis thaliana revisited through transgenic expression of engineered barley PORB mutant proteins
Plant Mol. Biol.
94
45-59
2017
Arabidopsis thaliana
Reinbothe, S.; Gray, J.; Rustgi, S.; von Wettstein, D.; Reinbothe, C.
Cell growth defect factor 1 is crucial for the plastid import of NADPH:protochlorophyllide oxidoreductase A in Arabidopsis thaliana
Proc. Natl. Acad. Sci. USA
112
5838-5843
2015
Arabidopsis thaliana
Fujii, S.; Kobayashi, K.; Nagata, N.; Masuda, T.; Wada, H.
Monogalactosyldiacylglycerol facilitates synthesis of photoactive protochlorophyllide in etioplasts
Plant Physiol.
174
2183-2198
2017
Arabidopsis thaliana
Gabruk, M.; Mysliwa-Kurdziel, B.
The origin, evolution and diversification of multiple isoforms of light-dependent protochlorophyllide oxidoreductase (LPOR) focus on angiosperms
Biochem. J.
477
2221-2236
2020
Arabidopsis thaliana (O48741), Arabidopsis thaliana (P21218), Arabidopsis thaliana (Q42536), Arabidopsis thaliana
Solymosi, K.; Mysliwa-Kurdziel, B.
The role of membranes and lipid-protein interactions in the Mg-branch of tetrapyrrole biosynthesis
Front. Plant Sci.
12
663309
2021
Magnoliopsida, Dinoroseobacter shibae (A8LUF3), Arabidopsis thaliana (O48741), Arabidopsis thaliana (P21218), Arabidopsis thaliana (Q42536), Hordeum vulgare (P13653), Hordeum vulgare (Q42850), Pisum sativum (Q01289), Triticum aestivum (Q41578), Nicotiana tabacum (Q8LSZ2), Nicotiana tabacum (Q8LSZ3)
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