Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.3.1.33 - protochlorophyllide reductase and Organism(s) Triticum aestivum and UniProt Accession Q41578

for references in articles please use BRENDA:EC1.3.1.33
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The enzyme catalyses a light-dependent trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Triticum aestivum
UNIPROT: Q41578
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Triticum aestivum
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
light-dependent NADPH:protochlorophyllide oxidoreductase
-
NADPH:Pchlide oxidoreductase
-
NADPH:protochlorophyllide oxidoreductase
-
LPOR
-
-
-
-
NADPH-protochlorophyllide oxidoreductase
-
-
-
-
NADPH-protochlorophyllide reductase
-
-
-
-
NADPH2-protochlorophyllide oxidoreductase
-
-
-
-
NADPH:Pchlide oxidoreductase
-
-
NADPH:protochlorophyllide oxidoreductase A
-
-
protochlorophyllide oxidoreductase
-
-
-
-
protochlorophyllide photooxidoreductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
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 hide
68518-04-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
show the reaction diagram
the enzyme (LPOR) catalyzes a photocatalytic reaction
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
does not accept protochlorophyllide a' or any other compounds with substituents at C-13-2 different from protochlorophyllide a
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
show the reaction diagram
the enzyme (LPOR) catalyzes a photocatalytic reaction
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
does not accept protochlorophyllide a' or any other compounds with substituents at C-13-2 different from protochlorophyllide a
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
additional information
light-dependent enzyme. Enzyme (LPOR) activity is induced by light and is fully inhibited in the dark
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
1760 pmol/mg/flash in prolamellar bodies
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
high expression in, no light-response during greening
Manually annotated by BRENDA team
additional information
isoenzymes LPOR-A and LPOR-B are present in etiolated material, while LPOR-C is expressed typically in green tissues
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
the enzyme (LPOR) binds more strongly to etioplast inner membranes than to thylakoid membranes
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PORA_WHEAT
388
0
41156
Swiss-Prot
Chloroplast (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
112000
-
substrate-enzyme complex, gel filtration
34000
-
SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable membrane-bound protein
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Valera, V.; Fung, M.; Wessler, A.N.; Richards, W.R.
Synthesis of 4R- and 4S-tritium labeled NADPH for the determination of the coenzyme stereospecificity of NADPH: protochlorophyllide oxidoreductase
Biochem. Biophys. Res. Commun.
148
515-520
1987
Triticum aestivum
Manually annotated by BRENDA team
Walker, C.J.; Griffiths, W.T.
Protochlorophyllide reductase: a flavoprotein?
FEBS Lett.
239
259-262
1988
Triticum aestivum
-
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Lenti, K.; Fodor, F.; Boddi, B.
Mercury inhibits the activity of the NADPH:protochlorophyllide oxidoreductase (POR)
Photosynthetica
40
145-151
2002
Triticum aestivum
-
Manually annotated by BRENDA team
Solymosi, K.; Lenti, K.; Mysliwa-Kurdziel, B.; Fidy, J.; Strzalka, K.; Boddi, B.
Hg2+ reacts with different components of the NADPH: protochlorophyllide oxidoreductase macrodomains
Plant Biol.
6
358-368
2004
Triticum aestivum
Manually annotated by BRENDA team
Denev, I.D.; Yahubyan, G.T.; Minkov, I.N.; Sundqvist, C.
Organization of protochlorophyllide oxidoreductase in prolamellar bodies isolated from etiolated carotenoid-deficient wheat leaves as revealed by fluorescence probes
Biochim. Biophys. Acta
1716
97-103
2005
Triticum aestivum
Manually annotated by BRENDA team
Blomqvist, L.A.; Ryberg, M.; Sundqvist, C.
Proteomic analysis of highly purified prolamellar bodies reveals their significance in chloroplast development
Photosynth. Res.
96
37-50
2008
Triticum aestivum
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team