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Information on EC 1.3.1.33 - protochlorophyllide reductase and Organism(s) Avena sativa and UniProt Accession P15904

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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:
Avena sativa
UNIPROT: P15904
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The taxonomic range for the selected organisms is: Avena sativa
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
-
-
-
-
NADPH-protochlorophyllide oxidoreductase
-
-
-
-
NADPH-protochlorophyllide reductase
-
-
-
-
NADPH2-protochlorophyllide oxidoreductase
-
-
-
-
NADPH: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
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
show the reaction diagram
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
protochlorophyllide a + 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
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
IMAGE
5,5'-dithiobis-(2-nitrobenzoic acid)
-
inhibits the regeneration of the enzyme-substrates complex, but has no effect on the photoconversion of the preformed complex
chlorophyll c1
-
competitive
N-ethylmaleimide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00047
protochlorophyllide a
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.7
-
prolamellar body
0.8
-
sonicated membranes
3.3
-
prothylakoid
additional information
-
1.49 chlorophyllide synthesis/flash per mg protein
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
POR_AVESA
313
0
33797
Swiss-Prot
Secretory Pathway (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
35000
37000
37800
-
amino acid composition
41000
-
identified with monospecific polyclonal antibody
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
active enzyme is protected by NADPH, protochlorophyllide and glycerol
-
unstable membrane-bound protein
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Oliver, R.P.; Griffiths, W.T.
Identification of the polypeptides of NADPH--protochlorophyllide oxidoreductase
Biochem. J.
191
277-280
1980
Avena sativa
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Luetz, C.; Roeper, U.; Beer, N.S.; Griffiths, T.
Sub-etioplast localization of the enzyme NADPH: protochlorophyllide oxidoreductase
Eur. J. Biochem.
118
347-353
1981
Avena sativa
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
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
Roeper, U.; Prinz, H.; Luetz, C.
Amino acid composition of the enzyme NADPH: protochlorophyllide oxidoreductase
Plant Sci.
52
15-19
1987
Avena sativa
-
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
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
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
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
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
Manually annotated by BRENDA team
Franck, F.; Sperling, U.; Frick, G.; Pochert, B.; Van Cleve, B.; Apel, K.; Armstrong, G.A.
Regulation of etioplast pigment-protein complexes, inner membrane architecture, and protochlorophyllide a chemical heterogeneity by light-dependent NADPH:protochlorophyllide oxidoreductases A and B
Plant Physiol.
124
1678-1696
2000
Arabidopsis thaliana, Avena sativa
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Helfrich, M.; Bommer, B.; Oster, U.; Klement, H.; Mayer, K.; Larkum, A.W.; Rudiger, W.
Chlorophylls of the c family: absolute configuration and inhibition of NADPH:protochlorophyllide oxidoreductase
Biochim. Biophys. Acta
1605
97-103
2003
Avena sativa
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