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Information on EC 1.3.1.33 - protochlorophyllide reductase and Organism(s) Hordeum vulgare and UniProt Accession Q42850
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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: Hordeum vulgare
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
LHPP
-
the light-harvesting NADPH:protochlorophyllide (Pchlide) oxidoreductase:Pchlide complex of etiolated plants, is developmentally expressed across the barley leaf gradient
LPOR
NADPH-protochlorophyllide oxidoreductase
NADPH-protochlorophyllide reductase
-
-
-
-
NADPH2-protochlorophyllide oxidoreductase
-
-
-
-
NADPH:Pchlide oxidoreductase
NADPH:protochlorophyllide oxidoreductase
PORA
protochlorophyllide oxidoreductase
-
-
-
-
protochlorophyllide photooxidoreductase
-
-
-
-
LPOR
-
-
-
-
NADPH-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 a + NADP+
the enzyme (LPOR) catalyzes a photocatalytic reaction
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
the enzyme (LPOR) catalyzes a photocatalytic reaction
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
393832, 393833, 393834, 393836, 393838, 393839, 393841, 393842, 393843, 393844, 393848, 393851, 393852, 393853, 393855, 393856, 393857, 393858, 393859, 393860, 393865, 657112
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
biosynthetic pathway leading to chlorophyll a
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
chlorophyll-biosynthetic pathway
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
key enzyme for the light-induced greening of etiolated angiosperm plants
-
-
?
additional information
?
-
-
naturally occurring esterified protochlorophyllide and chemically prepared protochlorophyllide methyl ester are not substrates for the enzyme, removal of Mg2+ from the protochlorophyllide leads to inactivity of the compound as a substrate
-
-
?
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 a + NADP+
the enzyme (LPOR) catalyzes a photocatalytic reaction
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
393833, 393836, 393838, 393839, 393841, 393842, 393843, 393844, 393851, 393852, 393853, 393855, 393857, 393858, 393859, 393860, 393865
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
biosynthetic pathway leading to chlorophyll a
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
chlorophyll-biosynthetic pathway
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
key enzyme for the light-induced greening of etiolated angiosperm plants
-
-
?
additional information
?
-
-
naturally occurring esterified protochlorophyllide and chemically prepared protochlorophyllide methyl ester are not substrates for the enzyme, removal of Mg2+ from the protochlorophyllide leads to inactivity of the compound as a substrate
-
-
?
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
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
-
removal of Mg2+ from the protochlorophyllide leads to inactivity of the compound as a substrate, activity can be restored by replacing the magnesium with zinc, whereas nickel, copper or cobalt fail to restore substrate activity
Zn2+
-
removal of Mg2+ from the protochlorophyllide leads to inactivity of the compound as a substrate, activity can be restored by replacing the magnesium with zinc, whereas nickel, copper or cobalt fail to restore substrate activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 60
-
linear drop of the relative concentration of the enzyme protein up to 30°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
-
-
additional information
high expression in, constitutive enzyme
very high expression in, no light-response during greening, undetectable in mature cells
additional information
LPOR-B is responsible for the bulk chlorophyll synthesis of adult or green plants
additional information
LPOR-B is responsible for the bulk chlorophyll synthesis of adult or green plants
additional information
isoenzyme LPOR-A is present in etiolated tissue
additional information
isoenzyme LPOR-A is present in etiolated tissue
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
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
oxygen-sensitive dark-operative NADPH:Pchlide oxidoreductase enzyme (DPOR) and light-dependent NADPH:protochlorophyllide oxidoreductase (LPOR) show very low sequence homology. In most organisms they occur simultaneously. However, angiosperms lack LPOR and became unable to synthesize chlorophyllides and chlorophylls (Chls) in the absence of light
evolution
oxygen-sensitive dark-operative NADPH:Pchlide oxidoreductase enzyme (DPOR) and light-dependent NADPH:protochlorophyllide oxidoreductase (LPOR) show very low sequence homology. In most organisms they occur simultaneously. However, angiosperms lack LPOR and became unable to synthesize chlorophyllides and chlorophylls (Chls) in the absence of light
physiological function
-
LHPP (light-harvesting POR:Pchlide complexes) assembly is indispensable for barley POR functions and seedling greening
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_HORVU
395
0
42148
Swiss-Prot
Chloroplast (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
36000
38000
44000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
oligomer
-
barley PORA can form a five-unit oligomer that interacts with a single PORB
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
x * 46000 Da, precursor protein, x * 38000 Da, mature protein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C104A
-
no detectable effect on the import of protein to plastid and processing in darkness
C166A
-
no detectable effect on the import of protein to plastid and processing in darkness
C195A
-
mutant, constructed for the identification of the protochlorophyllide binding site
C222A
-
mutant, constructed for the identification of the protochlorophyllide binding site
C276A
-
decrease in mature enzyme protein present in plastid and decrease in the amount of protochlorophyllide bound to enzyme. C276 constitutes the protochlorophyllide binding site in the active centre of enzyme
C303A
-
decrease in mature enzyme protein present in plastid and decrease in the amount of protochlorophyllide bound to enzyme. C303 constitutes a low affinity protochlorophyllide binding site involved in assembly and stabilization of imported enzyme inside etioplasts
C33A
-
mutant, constructed for the identification of the protochlorophyllide binding site
C85A
-
mutant, constructed for the identification of the protochlorophyllide binding site
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
active enzyme is protected by NADPH, protochlorophyllide and glycerol
-
rapid breakdown of the enzyme protein in vitro, caused by a membrane-bound proteolytic activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, can be kept in elution buffer for at least 3h without any detectable loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
barley POR expressed in Escherichia coli as a beta-galactosidase fusion protein
-
cDNA library constructed in pBR322, full-length cDNA cloned, cDNA inserts subcloned in the M13 phage and expressed in Escherichia coli
-
overexpressed in Escherichia coli as a fusion protein with the maltose-binding protein
-
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
Griffiths, W.T.
Reconstitution of chlorophyllide formation by isolated etioplast membranes
Biochem. J.
174
681-692
1978
Hordeum vulgare
Apel, K.; Santel, H.J.; Redlinger, T.E.; Falk, H.
The protochlorophyllide holochrome of barley (Hordeum vulgare L.). Isolation and characterization of the NADPH: protochlorophyllide oxidoreductase
Eur. J. Biochem.
111
251-258
1980
Hordeum vulgare
Griffiths, W.T.
Substrate-specificity studies on protochlorophyllide reductase in barley (Hordeum vulgare) etioplast membranes
Biochem. J.
186
267-278
1980
Hordeum vulgare
Beer, N.S.; Griffiths, W.T.
Purification of the enzyme NADPH: protochlorophyllide oxidoreductase
Biochem. J.
195
83-92
1981
Avena sativa, Hordeum vulgare, Phaseolus vulgaris
Oliver, R.P.; Griffiths, W.T.
Covalent labelling of the NADPH: protochlorophyllide oxidoreductase from etioplast membranes with [3H]N-phenylmaleimide
Biochem. J.
195
93-101
1981
Avena sativa, Hordeum vulgare, Phaseolus vulgaris
Griffiths, W.T.; Beer, N.S.
Site of synthesis of NADPH protochlorophyllide oxidoreductase in rye (Secale cereale)
Plant Physiol.
70
1014-1018
1982
Avena sativa, Hordeum vulgare, Secale cereale
Haeuser, I.; Dehesh, K.; Apel, K.
The proteolytic degradation in vitro of the NADPH-protochlorophyllide oxidoreductase of barley (Hordeum vulgare L.)
Arch. Biochem. Biophys.
228
577-586
1984
Avena sativa, Hordeum vulgare
Dehesh, K.; Ryberg, M.
The NADPH-protochlorophyllide oxidoreductase is the major protein constituent of prolamellar bodies in wheat (Triticum aestivum L.)
Planta
164
396-399
1985
Hordeum vulgare, Phaseolus vulgaris, Triticum aestivum
Dehesh, K.; Klaas, M.; Haeuser, I.; Apel, K.
Light-induced changes in the distribution of the 36000-Mr polypeptide of NADPH-protochlorophyllide oxidoreductase within different cellular compartments of barley (Hordeum vulgare L.) I. Localization by immunoblotting in isolated plastids and total leaf extracts
Planta
169
162-171
1986
Avena sativa, Cucurbita pepo, Hordeum vulgare, Triticum aestivum
Dehesh, K.; Van Cleve, B.; Ryberg, H.; Apel, K.
Light-induced changes in the distribution of the 36000-Mr polypeptide of NADPH-protochlorophyllide oxidoreductase within different cellular compartments of barley (Hordeum vulgare L.) II. Lacalization by immunogold labelling in ultrathin sections
Planta
169
172-183
1986
Hordeum vulgare, Secale cereale, Triticum aestivum, Zea mays
Begley, T.P.; Young, H.
Protochlorophyllide reductase. 1. Determination of the regiochemistry and the stereochemistry of the reduction of protochlorophyllide to chlorophyllide
J. Am. Chem. Soc.
111
3095-3096
1989
Avena sativa, Cucurbita pepo, Hordeum vulgare, Triticum aestivum
-
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
Darrah, P.M.; Kay, S.A.; Teakle, G.R.; Griffiths, W.T.
Cloning and sequencing of protochlorophyllide reductase
Biochem. J.
265
789-798
1990
Avena sativa, Hordeum vulgare
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
Helfrich, M.; Schoch, S.; Schaefer, W.; Ryberg, M.; Ruediger, W.
Absolute configuration of protochlorophyllide a and substrate specificity of NADPH-protochlorophyllide oxidoreductase
J. Am. Chem. Soc.
118
2606-2611
1996
Hordeum vulgare, Triticum aestivum
-
Martin, G.E.M.; Timko, M.P.; Wilks, H.M.
Purification and kinetic analysis of pea (Pisum sativum L.) NADPH:protochlorophyllide oxidoreductase expressed as a fusion with maltose-binding protein in Escherichia coli
Biochem. J.
325
139-145
1997
Hordeum vulgare, Pisum sativum, Tetradesmus obliquus
-
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
-
Dahlin, C.; Aronsson, H.; Wilks, H.M.; Lebedev, N.; Sundqvist, C.; Timko, M.P.
The role of protein surface charge in catalytic activity and chloroplast membrane association of the pea NADPH: protochlorophyllide oxidoreductase (POR) as revealed by alanine scanning mutagenesis
Plant Mol. Biol.
39
309-323
1999
Synechocystis sp., Avena sativa, Chlamydomonas reinhardtii, Hordeum vulgare, 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
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
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)
Reinbothe, C.; Pollmann, S.; Desvignes, C.; Weigele, M.; Beck, E.; Reinbothe, S.
LHPP, the light-harvesting NADPH:protochlorophyllide (Pchlide) oxidoreductase:Pchlide complex of etiolated plants, is developmentally expressed across the barley leaf gradient
Plant Sci.
167
1027-1041
2004
Hordeum vulgare
Reinbothe, C.; Buhr, F.; Bartsch, S.; Desvignes, C.; Quigley, F.; Pesey, H.; Reinbothe, S.
In vitro-mutagenesis of NADPH:protochlorophyllide oxidoreductase B: two distinctive protochlorophyllide binding sites participate in enzyme catalysis and assembly
Mol. Genet. Genomics
275
540-552
2006
Hordeum vulgare
Kovacevic, D.; Dewez, D.; Popovic, R.
Irradiation-induced in vivo re-localization of NADPH-protochlorophyllide oxidoreductase from prolamellar body to stroma of barley etioplast
Photosynthetica
45
105-109
2007
Hordeum vulgare
-
Ploescher, M.; Granvogl, B.; Reisinger, V.; Eichacker, L.A.
Identification of the N-termini of NADPH: protochlorophyllide oxidoreductase A and B from barley etioplasts (Hordeum vulgare L.)
FEBS J.
276
1074-1081
2009
Pisum sativum (Q01289), Pisum sativum, Hordeum vulgare (Q42850), Hordeum vulgare
Reinbothe, C.; Pollmann, S.; Phetsarath-Faure, P.; Quigley, F.; Weisbeek, P.; Reinbothe, S.
A pentapeptide motif related to a pigment binding site in the major light-harvesting protein of photosystem II, LHCII, governs substrate-dependent plastid import of NADPH:protochlorophyllide oxidoreductase A
Plant Physiol.
148
694-703
2008
Hordeum vulgare
Buhr, F.; El Bakkouri, M.; Valdez, O.; Pollmann, S.; Lebedev, N.; Reinbothe, S.; Reinbothe, C.
Photoprotective role of NADPH:protochlorophyllide oxidoreductase A
Proc. Natl. Acad. Sci. USA
105
12629-12634
2008
Hordeum vulgare
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
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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