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Information on EC 1.3.1.33 - protochlorophyllide reductase
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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
-
dark-grown
-
angiosperm
- thylakoids
- tetrapyrrole
- bacteriochlorophyll
-
light-harvesting
- plb
-
photoreduction
-
lpors
-
nitrogenase-like
-
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
-
pigment-protein
- chls
-
photoenzyme
- l-protein
-
de-etiolation
-
shibata
- analysis
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bchB
dark active protochlorophyllide oxidoreductase
dark operative protochlorophyllide oxidoreductase
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-
dark-operative protochlorophyllide oxidoreductase
DPOR
LHPP
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the light-harvesting NADPH:protochlorophyllide (Pchlide) oxidoreductase:Pchlide complex of etiolated plants, is developmentally expressed across the barley leaf gradient
light-activated enzyme protochlorophyllide oxidoreductase
Thermosynechococcus vestitus
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light-dependent NADPH:protochlorophyllide oxidoreductase
light-dependent Pchlide oxidoreductase
Light-dependent protochlorophyllide oxidoreductase
light-driven enzyme protochlorophyllide oxidoreductase
light-independent NADPH:protochlorophyllide oxidoreductase
-
-
light-independent protochlorophyllide oxidoreductase
LIPOR
LPOR
NADPH-Pchlide oxidoreductase
NADPH-protochlorophyllide oxidoreductase
NADPH-protochlorophyllide reductase
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-
-
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NADPH2-protochlorophyllide oxidoreductase
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-
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NADPH: protochlorophyllide oxidoreductase
NADPH: protochlorophyllide oxidoreductase A
NADPH:Pchlide oxidoreductase
NADPH:protochlorophyllide (Pchlide) oxidoreductase
NADPH:protochlorophyllide oxidoreductase
NADPH:protochlorophyllide oxidoreductase A
NADPH:protochlorophyllide oxidoreductase B
PCR
POR
POR A
POR B
POR C
POR-A
POR-B
POR1
POR2
PORA
PORB
PORC
protochlorophyllide oxidoreductase
protochlorophyllide oxidoreductase A
protochlorophyllide oxidoreductase C
protochlorophyllide photooxidoreductase
-
-
-
-
protochlorophyllide reductase
dark active protochlorophyllide oxidoreductase
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dark active protochlorophyllide oxidoreductase
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dark-operative protochlorophyllide oxidoreductase
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dark-operative protochlorophyllide oxidoreductase
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consists of the two components, L-protein (BchL-dimer) and NB-protein (BchN-BchBheterotetramer)
DPOR
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consists of the homodimeric protein complex ChlL2 and a heterotetrameric protein complex (ChlNB)2
light-dependent NADPH:protochlorophyllide oxidoreductase
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light-independent protochlorophyllide oxidoreductase
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light-independent protochlorophyllide oxidoreductase
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light-independent protochlorophyllide oxidoreductase
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LPOR
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-
-
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NADPH-protochlorophyllide oxidoreductase
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-
-
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protochlorophyllide oxidoreductase
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-
-
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protochlorophyllide oxidoreductase
Thermosynechococcus vestitus
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chlorophyllide a + NADP+ = protochlorophyllide + NADPH + H+
The enzyme catalyses a light-dependent trans-reduction of the D-ring of protochlorophyllide. The product has the (7S,8S)-configuration
-
-
-
chlorophyllide a + NADP+ = protochlorophyllide + NADPH + H+
light
-
-
-
chlorophyllide a + NADP+ = protochlorophyllide + NADPH + H+
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
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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.
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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
8-ethyl-chlorophyll a + NADPH + H+
? + NADP+
-
-
-
-
?
8-ethyl-chlorophyll b + NADPH + H+
? + NADP+
-
-
-
-
?
8-vinyl-chlorophyll a + NADPH + H+
? + NADP+
-
-
-
-
?
8-vinyl-chlorophyll b + NADPH + H+
? + NADP+
-
-
-
-
?
C8-ethyl-C13(2)-(r)-protochlorophyllide + NADPH
? + NADP+
-
stereoisomer of the substrate
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-
?
divinyl protochlorophyllide a + NADPH
divinyl chlorophyllide a + NADP+
Thermosynechococcus vestitus
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-
-
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?
monovinyl protochlorophyllide a + NADPH
monovinyl chlorophyllide a + NADP+
Thermosynechococcus vestitus
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-
-
-
?
protochlorophyllide + dithiothreitol
chlorophyllide + oxidized dithiothreitol
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-
-
-
?
protochlorophyllide + reduced ferredoxin
chlorophyllide + oxidized ferredoxin
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ferredoxin is the natural electron donor
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-
?
protochlorophyllide b + NADPH + H+
chlorophyllide b + NADP+
-
-
-
-
?
Zn-protopheophorbide a + NADPH + H+
? + NADP+
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efficient substrate
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-
?
chlorophyllide a + NADP+
protochlorophyllide + NADPH + H+
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-
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r
chlorophyllide a + NADP+
protochlorophyllide + NADPH + H+
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-
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r
chlorophyllide a + NADP+
protochlorophyllide + NADPH + H+
Thermosynechococcus vestitus
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POR catalyzes the NADPH-dependent reduction of the C17-C18 double bond of protochlorophyllide to form chlorophyllide
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r
protochlorophyllide + NADPH
chlorophyllide + NADP+
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PORB and PORC seem to play redundant roles in maintaining light-dependent chlorophyll biosynthesis in green plants and are together essential for growth and development
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-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
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-
-
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?
protochlorophyllide + NADPH
chlorophyllide + NADP+
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-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
constitutive enzyme
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-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
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key enzyme of chlorophyll biosynthesis
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-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
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light-dependent reaction. Isoform PORB and PORC are interchangeable and functionally redundant in developed plants. PORB as well as PORA, functions in assembly of prolamellar bodies and in photoactive protochlorophylluide formation in etiolated seedlings. At the onset of greening, prolamellar bodies are important for efficient capture of light energy for photoconversion under various light conditions, and PORC, which is induced by light irradiation, contributes to photoprotection during greening of the etiolated seedlings
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-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
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light-dependent reaction
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-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
light-dependent reaction
-
-
?