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Information on EC 1.3.1.33 - protochlorophyllide reductase and Organism(s) Synechocystis sp. and UniProt Accession Q59987

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IUBMB 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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This record set is specific for:
Synechocystis sp.
UNIPROT: Q59987
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The taxonomic range for the selected organisms is: Synechocystis sp.
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
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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-
-
-
NADPH2-protochlorophyllide oxidoreductase
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-
-
-
protochlorophyllide oxidoreductase
protochlorophyllide photooxidoreductase
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
chlorophyllide a + NADP+ = protochlorophyllide + NADPH + H+
show the reaction diagram
catalytic mechanism suggested: protochlorophillide absorbs a photon, creating a transient charge separtaion across the C17-C18 double bond, which promotes ultrafast hydride transfer from the pro-S face of NADPH to the C17 of protochlorophillide. The resulting A696 charge transfer intermediate facilitates transfer of a proton to the C18 of protochlorophillide during the subsequent first dark reaction
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
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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 hide
68518-04-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
show the reaction diagram
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-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
-
activation by light
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-
?
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
chlorophyllide + NADP+
show the reaction diagram
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
-
activation by light
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-ethylmaleimide
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000012
NADPH
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0.0086
protochlorophyllide a
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additional information
additional information
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EPR and Stark spectroscopies analysis of enzyme reaction
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PCC 6803, PCC 7942 and WH8102
SwissProt
Manually annotated by BRENDA team
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y189F
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mutant, the putative proton donor, Tyr 189, is replaced by a phenylalanine residue
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
overexpression in Escherichia coli as a His6-tagged protein
cloned and overproduced in Escherichia coli with a hexahistidine tag at the N-terminus
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
Heyes, D.J.; Ruban, A.V.; Hunter, C.N.
Protochlorophyllide oxidoreductase: "dark" reactions of a light-driven enzyme
Biochemistry
42
523-528
2003
Synechocystis sp.
Manually annotated by BRENDA team
Heyes, D.J.; Hunter, C.N.; van Stokkum, I.H.; van Grondelle, R.; Groot, M.L.
Ultrafast enzymatic reaction dynamics in protochlorophyllide oxidoreductase
Nat. Struct. Biol.
10
491-492
2003
Synechocystis sp.
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
Heyes, D.J.; Heathcote, P.; Rigby, S.E.; Palacios, M.A.; van Grondelle, R.; Hunter, C.N.
The first catalytic step of the light-driven enzyme protochlorophyllide oxidoreductase proceeds via a charge transfer complex
J. Biol. Chem.
281
26847-26853
2006
Synechocystis sp.
Manually annotated by BRENDA team
Heyes, D.J.; Scrutton, N.S.
Conformational changes in the catalytic cycle of protochlorophyllide oxidoreductase: what lessons can be learnt from dihydrofolate reductase?
Biochem. Soc. Trans.
37
354-357
2009
Synechocystis sp.
Manually annotated by BRENDA team
Sytina, O.A.; Heyes, D.J.; Hunter, C.N.; Groot, M.L.
Ultrafast catalytic processes and conformational changes in the light-driven enzyme protochlorophyllide oxidoreductase (POR)
Biochem. Soc. Trans.
37
387-391
2009
Synechocystis sp.
Manually annotated by BRENDA team