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) Chlamydomonas reinhardtii and UniProt Accession Q39617

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:
Chlamydomonas reinhardtii
UNIPROT: Q39617
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: Chlamydomonas reinhardtii
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 protochlorophyllide oxidoreductase
-
protochlorophyllide reductase
-
light-driven enzyme protochlorophyllide oxidoreductase
-
-
LPOR
-
-
-
-
NADPH-Pchlide oxidoreductase
-
-
NADPH-protochlorophyllide oxidoreductase
-
-
-
-
NADPH-protochlorophyllide reductase
-
-
-
-
NADPH2-protochlorophyllide oxidoreductase
-
-
-
-
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
chlorophyllide a + NADP+
protochlorophyllide + NADPH + H+
show the reaction diagram
-
-
-
r
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
show the reaction diagram
-
-
-
-
?
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
chlorophyllide a + NADP+
protochlorophyllide + NADPH + H+
show the reaction diagram
-
-
-
r
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
NADPH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
protochlorophyllide
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
protochlorophyllide
-
stringent requirement
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.157
NADPH
-
pH and temperature not specified in the publication
0.0017
protochlorophyllide
-
pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.043
NADPH
-
pH and temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
ferredoxin-dependent biliverdin reductase, PCYA1 (EC 1.3.7.5), is a key enzyme involved in the biosynthesis of bilins, mechanism of bilin-mediated regulation of chlorophyll biosynthesis, and regulatory mechanisms of tetrapyrrole biosynthesis in Chlamydomonas reinhardtii, overview. Chlamydomonas PCYA1 uniquely interacts with light-dependent protochlorophyllide oxidoreductase LPOR (protochlorophyllide reductase, EC 1.3.1.33) via its FDBR domain, but not with ferredoxin:protochlorophyllide reductase DPOR (EC 1.3.7.7). This interaction is specific to Chlamydomonas since the Arabidopsis thaliana homologous proteins do not interact with each other, yeast two-hybrid and pull down assay analyses of protein-protein interaction
physiological function
light-dependent protochlorophyllide oxidoreductase (LPOR) is a rate-limiting key chlorophyll biosynthetic enzyme
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
POR_CHLRE
397
0
41871
Swiss-Prot
Chloroplast (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
-
gel filtration
36000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 36000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the coding regions of LPOR (amino acids 35-397) is amplified from pBDCrPCYA1-FDBR vector, cloned into pGADT7 vector, and introduced into Y187 yeast cells, recombinant expression of MBP-tagged enzyme LPOR. Yeast two-hybrid and pull down assay analyses of protein-protein interaction
expressed in Escherichia coli BL21(DE3) pLysS cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ford, C.; Mitchell, S.; Wang, W.
Characterization of NADPH: Protochlorophyllide oxidoreductase in the y-7 and pc-1 y-7 mutants of Chlamydomonas reinhardtii
Mol. Gen. Genet.
192
290-292
1983
Chlamydomonas reinhardtii
-
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
Fujita, Y.; Bauer, C.E.
Reconstitution of light-independent protochlorophyllide reductase from purified bchl and BchN-BchB subunits. In vitro confirmation of nitrogenase-like features of a bacteriochlorophyll biosynthesis enzyme
J. Biol. Chem.
275
23583-23588
2000
Chlamydomonas reinhardtii, Leptolyngbya boryana, Rhodobacter capsulatus
Manually annotated by BRENDA team
Heyes, D.J.; Martin, G.E.M.; Reid, R.J.; Hunter, C.N.; Wilks, H.M.
NADPH:protochlorophyllide oxidoreductase from Synechocystis: overexpression, purification and preliminary characterization
FEBS Lett.
483
47-51
2000
Synechocystis sp., Chlamydomonas reinhardtii
Manually annotated by BRENDA team
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
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
Hoeven, R.; Hardman, S.J.; Heyes, D.J.; Scrutton, N.S.
Cross-species analysis of protein dynamics associated with hydride and proton transfer in the catalytic cycle of the light-driven enzyme protochlorophyllide oxidoreductase
Biochemistry
55
903-913
2016
Chlamydomonas reinhardtii, Cyanidioschyzon merolae, Daucus carota, Marchantia paleacea, Nicotiana tabacum, Nostoc punctiforme, Physcomitrium patens, Pinus mugo, Zea mays, Lyngbya majuscula
Manually annotated by BRENDA team
Zhang, W.; Zhong, H.; Lu, H.; Zhang, Y.; Deng, X.; Huang, K.; Duanmu, D.
Characterization of ferredoxin-dependent biliverdin reductase PCYA1 reveals the dual function in retrograde bilin biosynthesis and interaction with light-dependent protochlorophyllide oxidoreductase LPOR in Chlamydomonas reinhardtii
Front. Plant Sci.
9
676
2018
Chlamydomonas reinhardtii (Q39617), Chlamydomonas reinhardtii, Chlamydomonas reinhardtii 4A+ (Q39617)
Manually annotated by BRENDA team