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Information on EC 1.3.1.33 - protochlorophyllide reductase and Organism(s) Pisum sativum and UniProt Accession Q01289
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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
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dark-grown
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angiosperm
- thylakoids
- tetrapyrrole
- bacteriochlorophyll
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light-harvesting
- plb
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photoreduction
-
lpors
-
nitrogenase-like
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phytochrome
-
photoactive
- chelatase
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phototransformation
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1.6.99.1
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photoconversion
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mg-chelatase
- mg-protoporphyrin
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pigment-protein
- chls
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photoenzyme
- l-protein
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de-etiolation
-
shibata
- analysis
The taxonomic range for the selected organisms is: Pisum sativum
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, light-dependent nadph:protochlorophyllide oxidoreductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
LPOR
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-
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NADPH-protochlorophyllide oxidoreductase
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-
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NADPH-protochlorophyllide reductase
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-
-
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NADPH2-protochlorophyllide oxidoreductase
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-
-
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protochlorophyllide oxidoreductase
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-
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protochlorophyllide photooxidoreductase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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-
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
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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
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-
?
C8-ethyl-C13(2)-(r)-protochlorophyllide + NADPH
? + NADP+
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stereoisomer of the substrate
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-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
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-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
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important regulatory step in chlorophyll biosynthesis
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-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
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chlorophyll-biosynthetic pathway
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-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
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the enzyme might be directly involved in the regulation of the metabolism of other porphyrins
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-
?
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+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
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important regulatory step in chlorophyll biosynthesis
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-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
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chlorophyll-biosynthetic pathway
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-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
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the enzyme might be directly involved in the regulation of the metabolism of other porphyrins
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-
?
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes
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nuclear-encoded cytoplasmically sythesized, posttranslationally processed on import into plastids
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
key enzyme of chlorophyll biosynthesis in angiosperms. Photoenzyme, which catalyzes the light-activated trans-reduction of the C17-C18 double bond of the porphyrin ring of protochlorophyllides. Due to the light requirement, dark-grown angiosperms cannot synthesize chlorophyll
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). POR_PEA
399
0
42962
Swiss-Prot
Chloroplast (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimerization and binding of ligands (both the cofactor NADPH and substrate protochlorophyllide) are computationally investigated the sequence and structural relationships among homologous proteins are identified through database searches. The results indicate that alpha4 and alpha7 helices of monomers form the interface of NADPH:protochlorophyllide oxidoreductase dimers. On the basis of conserved residues, 11 functionally important amino acids that play important roles in binding of the enzyme to NADPH are predicted
monomer
the structure of enzyme (POR) protein is predicted in its monomeric and dimeric form
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type and recombinant pea enzyme, heterologously expressed in Escherichia coli
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Rhodobacter capsulatus mutant deficient in Bchl biosynthesis. The NADPH:protochlorophyllide oxidoreductase is integrated in the porphyrin biosynthesis network and its activity leads to the formation of photosynthetic chlorophyll proteins
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mature pea POR cloned into the pAlter-1 mutagenesis vector, expressed in Escherichia coli JM109
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overexpressed as a fusion with maltose-binding protein in Escherichia coli using expression plasmid pKK233-2
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overexpression in Escherichia coli as a fusion protein with maltose-binding protein
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Wilks, H.M.; Timko, M.P.
A light-dependent complementation system for analysis of NADPH:protochlorophyllide oxidoreductase: identification and mutagenesis of two conserved residues that are essential for enzyme activity
Proc. Natl. Acad. Sci. USA
92
724-728
1995
Pisum sativum, Rhodobacter capsulatus
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.; Karginova, O.; McIvor, W.; Timko, M.P.
Tyr275 and Lys279 Stabilize NADPH within the Catalytic Site of NADPH:Protochlorophyllide Oxidoreductase and Are Involved in the Formation of the Enzyme Photoactive State
Biochemistry
40
12562-12574
2001
Pisum sativum
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
Selstam, E.; Schelin, J.; Brain, T.; Williams, W.P.
The effects of low pH on the properties of protochlorophyllide oxidoreductase and the organization of prolamellar bodies of maize (Zea mays)
Eur. J. Biochem.
269
2336-2346
2002
Avena sativa, Pisum sativum, Zea mays
Lebedev, N.; Timko, M.P.
POR structural domains important for the enzyme activity in R. capsulatus complementation system
Photosynth. Res.
74
153-163
2002
Pisum sativum
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)
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
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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