Information on EC 1.3.1.33 - protochlorophyllide reductase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.3.1.33
-
RECOMMENDED NAME
GeneOntology No.
protochlorophyllide reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
chlorophyllide a + NADP+ = protochlorophyllide + NADPH + H+
show the reaction diagram
light; 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+
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
-
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
Synechocystis sp. PCC6803
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
B0F840
-
oxidation
B0F835 and B0F841 and B0F842
-
oxidation
B0F833 and B0F836 and B0F837
-
oxidation
B0F838 and B0F839
-
oxidation
Q01289
-
oxidation
Fremyella diplosiphon
A9UGZ2, C6KHP5 and Q6H056 and Q6H058
;
redox reaction
-
-
-
-
reduction
B0F840
-
reduction
B0F835 and B0F841 and B0F842
-
reduction
B0F833 and B0F836 and B0F837
-
reduction
B0F838 and B0F839
-
reduction
Q01289
-
reduction
Fremyella diplosiphon
A9UGZ2, C6KHP5 and Q6H056 and Q6H058
;
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
chlorophyllide a biosynthesis I (aerobic, light-dependent)
-
Metabolic pathways
-
Porphyrin and chlorophyll metabolism
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dark active protochlorophyllide oxidoreductase
B0F840
-
dark active protochlorophyllide oxidoreductase
B0F835 and B0F841 and B0F842
-
dark active protochlorophyllide oxidoreductase
B0F833 and B0F836 and B0F837
-
dark active protochlorophyllide oxidoreductase
B0F838 and B0F839
-
dark operative protochlorophyllide oxidoreductase
-
-
dark-operative protochlorophyllide oxidoreductase
-
-
dark-operative protochlorophyllide oxidoreductase
Fremyella diplosiphon
C6KHP5 and Q6H056 and Q6H058
-
dark-operative protochlorophyllide oxidoreductase
Q7VD39
-
dark-operative protochlorophyllide oxidoreductase
-
consists of the two components, L-protein (BchL-dimer) and NB-protein (BchN-BchBheterotetramer)
DPOR
B0F835 and B0F841 and B0F842
-
DPOR
Fremyella diplosiphon
C6KHP5 and Q6H056 and Q6H058
-
DPOR
B0F833 and B0F836 and B0F837
-
DPOR
B0F838 and B0F839
-
DPOR
-
consists of the homodimeric protein complex ChlL2 and a heterotetrameric protein complex (ChlNB)2
LHPP
-
the light-harvesting NADPH:protochlorophyllide (Pchlide) oxidoreductase:Pchlide complex of etiolated plants, is developmentally expressed across the barley leaf gradient
light-dependent NADPH: protochlorophyllide oxidoreductase
-
-
Light-dependent protochlorophyllide oxidoreductase
Fremyella diplosiphon
A9UGZ2
-
light-independent (dark) Pchlide oxidoreductase
-
-
light-independent NADPH:protochlorophyllide oxidoreductase
-
-
light-independent protochlorophyllide oxidoreductase
-
-
light-independent protochlorophyllide oxidoreductase
B0F840
-
light-independent protochlorophyllide oxidoreductase
B0F835 and B0F841 and B0F842
-
light-independent protochlorophyllide oxidoreductase
Fremyella diplosiphon
C6KHP5 and Q6H056 and Q6H058
-
light-independent protochlorophyllide oxidoreductase
B0F833 and B0F836 and B0F837
-
light-independent protochlorophyllide oxidoreductase
B0F838 and B0F839
-
LIPOR
B0F835 and B0F841 and B0F842
-
LIPOR
B0F833 and B0F836 and B0F837
-
LIPOR
B0F838 and B0F839
-
LPOR
-
-
-
-
LPOR
Fremyella diplosiphon
A9UGZ2
-
NADPH-Pchlide oxidoreductase
-
-
NADPH-Pchlide oxidoreductase
-
-
NADPH-protochlorophyllide oxidoreductase
-
-
-
-
NADPH-protochlorophyllide oxidoreductase
-
-
NADPH-protochlorophyllide oxidoreductase (POR)-like protein
-
-
NADPH-protochlorophyllide oxidoreductase A
-
-
NADPH-protochlorophyllide oxidoreductase B
-
-
NADPH-protochlorophyllide reductase
-
-
-
-
NADPH2-protochlorophyllide oxidoreductase
-
-
-
-
NADPH: protochlorophyllide oxidoreductase
-
-
NADPH: protochlorophyllide oxidoreductase A
-
-
NADPH: protochlorophyllide oxidoreductase A
-
-
NADPH: protochlorophyllide oxidoreductase B
-
-
NADPH:Pchlide oxidoreductase
-
-
NADPH:Pchlide oxidoreductase
-
-
NADPH:Pchlide oxidoreductase A
-
-
NADPH:protochlorophyllide (Pchlide) oxidoreductase
-
-
NADPH:protochlorophyllide oxidoreductase
-
-
NADPH:protochlorophyllide oxidoreductase
-
-
NADPH:protochlorophyllide oxidoreductase
-
-
NADPH:protochlorophyllide oxidoreductase
-
-
NADPH:protochlorophyllide oxidoreductase
-
-
NADPH:protochlorophyllide oxidoreductase A
-
-
NADPH:protochlorophyllide oxidoreductase A
-
-
NADPH:protochlorophyllide oxidoreductase A
-
-
NADPH:protochlorophyllide oxidoreductase B
-
-
OsPORA
-
-
OsPORB
-
-
Pchilde reductase
-
-
Pchlide oxidoreductase
-
-
POR
O48741, P21218, Q42536
-
POR
B0F835 and B0F841 and B0F842
-
POR
Fremyella diplosiphon
A9UGZ2
-
POR
B0F833 and B0F836 and B0F837
-
POR
B0F838 and B0F839
-
POR
Synechocystis sp. PCC6803
-
-
-
POR pPm1
-
-
POR pPm2
Q41203
-
POR-PChlide640
-
-
POR-PChlide650
-
-
POR1
Q9SDT1
-
POR1
Q8LSZ3
-
POR1
Q41578
-
POR2
Q8LSZ2
-
POR2
Q41578
-
PORA
P13653
-
PORA
-
-
PORB
Q42850
-
protochlorophyllide oxidoreductase
-
-
-
-
protochlorophyllide oxidoreductase
O48741, P21218, Q42536
-
protochlorophyllide oxidoreductase
B0F840
-
protochlorophyllide oxidoreductase
B0F835 and B0F841 and B0F842
-
protochlorophyllide oxidoreductase
Fremyella diplosiphon
A9UGZ2, C6KHP5 and Q6H056 and Q6H058
-
protochlorophyllide oxidoreductase
-
-
protochlorophyllide oxidoreductase
B0F833 and B0F836 and B0F837
-
protochlorophyllide oxidoreductase
B0F838 and B0F839
-
protochlorophyllide oxidoreductase
-
-
protochlorophyllide oxidoreductase
-
-
protochlorophyllide oxidoreductase A
-
-
protochlorophyllide oxidoreductase A
Q42536
-
protochlorophyllide oxidoreductase B
P21218
-
protochlorophyllide oxidoreductase C
-
-
protochlorophyllide oxidoreductase C
O48741
-
protochlorophyllide oxidoreductase POR-PChlide640
-
-
protochlorophyllide oxidoreductase POR-PChlide650
-
-
protochlorophyllide photooxidoreductase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
68518-04-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
PCC 7120
-
-
Manually annotated by BRENDA team
ecotype Columbia
-
-
Manually annotated by BRENDA team
strain CS-41, enzyme components protein L, protein N and protein B are all transcribed constitutively independent of illumination and presence of glucose. Steady-state amounts of proteins in the light-grown cells are two- to threefold greater than in dark-grown cells. Approximately the same amount of protein is present in cultures grown mixtrophically or heterotrophically both containing glucose. Much less protein is present in photoautotrophic cells. Therefore light-independent enzyme activity depends on post-transcriptional and post-translational regulation and switches on both in light and dark
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
L., var Peniarth; oat
-
-
Manually annotated by BRENDA team
L., var. Flaemmingskrone; L., var. Pennal; oat
-
-
Manually annotated by BRENDA team
L., var. Pennal; oat
-
-
Manually annotated by BRENDA team
L.cv. Pirol, var. Irlbad
-
-
Manually annotated by BRENDA team
unicellular green alga, mutant y-7
-
-
Manually annotated by BRENDA team
strain ATCC 49652
-
-
Manually annotated by BRENDA team
subunit L, fragment
UniProt
Manually annotated by BRENDA team
subunit B, subunit L, subunit N, fragments
B0F835 and B0F841 and B0F842
UniProt
Manually annotated by BRENDA team
Fremyella diplosiphon
subunits B, L and N; UTEX 481, also called Calothrix sp. PCC7601 and Tolypothrix sp. PCC 7601
C6KHP5 and Q6H056 and Q6H058
UniProt
Manually annotated by BRENDA team
Fremyella diplosiphon
UTEX 481, also called Calothrix sp. PCC7601 and Tolypothrix sp. PCC 7601
UniProt
Manually annotated by BRENDA team
subunit B, subunit L, subunit N, fragments
B0F833 and B0F836 and B0F837
UniProt
Manually annotated by BRENDA team
subunit L, subunit N, fragments
B0F838 and B0F839
UniProt
Manually annotated by BRENDA team
barley; L cv. carina
-
-
Manually annotated by BRENDA team
barley; L., cultivar Proctor
-
-
Manually annotated by BRENDA team
barley; mutants xantha-l81 and xantha-f10
-
-
Manually annotated by BRENDA team
cultivar Chapais
-
-
Manually annotated by BRENDA team
cv. Carina
-
-
Manually annotated by BRENDA team
Hordeum vulgare L.
SwissProt
Manually annotated by BRENDA team
isoform PorB
-
-
Manually annotated by BRENDA team
L., cultivar Proctor
-
-
Manually annotated by BRENDA team
cyanobacterium
-
-
Manually annotated by BRENDA team
liverwort, var. diptera
-
-
Manually annotated by BRENDA team
runner bean, L., cultivar Streamline
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
mountain pine
-
-
Manually annotated by BRENDA team
white pine
-
-
Manually annotated by BRENDA team
loblolly pine
-
-
Manually annotated by BRENDA team
cv. Kelvedon Wonder; pea
-
-
Manually annotated by BRENDA team
CCMP1375, MED4 and MIT9313
-
-
Manually annotated by BRENDA team
L. cv Rheidol; rye
-
-
Manually annotated by BRENDA team
ATCC27144 = Synechococcus PCC6301
-
-
Manually annotated by BRENDA team
ATCC27144 = Synechococcus PCC6301; Synechococcus sp. PCC 6301 or ATCC 27144
-
-
Manually annotated by BRENDA team
PCC 6803, PCC 7942 and WH8102
SwissProt
Manually annotated by BRENDA team
strain PCC6803
-
-
Manually annotated by BRENDA team
Synechocystis sp. PCC6803
PCC6803
-
-
Manually annotated by BRENDA team
Synechocystis sp. PCC6803
strain PCC6803
-
-
Manually annotated by BRENDA team
comparison of proteins from plants treated with norflurazon to those isolated from plants with normal carotinoid amount
-
-
Manually annotated by BRENDA team
cultivar Kosack
-
-
Manually annotated by BRENDA team
L. cv. Minaret, Clovis-Maton, Avelgem-Kerkhove, Belgium; wheat
-
-
Manually annotated by BRENDA team
L. cv. Starke II, Weibuell; wheat
-
-
Manually annotated by BRENDA team
var. Avalon; wheat
-
-
Manually annotated by BRENDA team
; maize, corn L. cv. Apache
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
map-based cloning of the faded green leaf (fgl) locus in Oryza sativa is performed, and reveals that fgl harbors a 1-bp deletion in the coding region of OsPORB, resulting in a frameshift mutation and premature translational termination. Mutant is complemented by OsPORB
malfunction
-
a PORA null mutant (porA-1) and PORA RNAi lines display severe photoautotrophic growth defects, which can be partially rescued on sucrose-supplemented growth media. Elimination of PORA during skotomorphogenesis results in reductions in the volume and frequency of prolamellar bodies, and in photoactive Pchlide conversion; it is shown that an Arabidopsis thaliana porB-1 porC-1 double mutant can be functionally rescued by the addition of ectopically expressed PORA, which suffices in the absence of either PORB or PORC to direct bulk chlorophyll synthesis and normal plant development
malfunction
-
it is shown that a porA-1 null mutant (porA mutant) carries a second dissociation insertion in another gene closely linked to the PORA gene that is expected to affect the phenotype of the porA mutant
malfunction
-
overexpression of PORC in Arabidopsis thaliana reduces the accumulation of protochlorophyllide in high light-grown plants that results in minimal generation of 1O2 and plants are protected from 1O2-mediated oxidative damage caused by high light. PORC overexpression protects the plants from oxidative herbicidal action of 5-aminolevulinicacid. Overexpression of PORC results in coordinated upregulation of gene/protein expression of several Chl biosynthetic pathway enzymes resulting in enhanced Chl synthesis in light-grown plants
physiological function
-
LHPP (light-harvesting POR:Pchlide complexes) assembly is indispensable for barley POR functions and seedling greening
physiological function
-
OsPORA mainly functions in the early stages of leaf development; OsPORB is essential for maintaining light-dependent chlorophyll synthesis throughout leaf development, especially under high-light conditions
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
8-ethyl-chlorophyll a + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
-
?
8-ethyl-chlorophyll b + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
-
?
8-vinyl-chlorophyll a + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
-
?
8-vinyl-chlorophyll b + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
-
?
C8-ethyl-C13(2)-(r)-protochlorophyllide + NADPH
? + NADP+
show the reaction diagram
-
stereoisomer of the substrate
-
-
?
chlorophyllide a + NADP+
protochlorophyllide + NADPH + H+
show the reaction diagram
-
POR catalyzes the NADPH-dependent reduction of the C17-C18 double bond of protochlorophyllide to form chlorophyllide
-
-
r
divinyl protochlorophyllide a + NADPH
divinyl chlorophyllide a + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + dithionite
chlorophyllide + SO2
show the reaction diagram
-
-
-
-
?
protochlorophyllide + dithiothreitol
chlorophyllide + oxidized dithiothreitol
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
O48741
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
Q39617
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
O80333
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-, Q41203
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
P21218, Q42536
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
Q9LKH8
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
Q8LSZ2, Q8LSZ3
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
Q41249
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
Q9SDT1
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
Q41578
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
P13653, Q42850
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
Q41203
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
P21218, Q42536
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
Q9LKH8
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
P13653, Q42850
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
important regulatory step in chlorophyll biosynthesis
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
biosynthetic pathway leading to chlorophyll a
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
chlorophyll-biosynthetic pathway
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
chlorophyll-biosynthetic pathway
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
key enzyme for light-dependent chlorophyll biosynthesis
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
key enzyme for the light-induced greening of etiolated angiosperm plants
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
key enzyme of chlorophyll biosynthesis
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
key regulatory step in chlorophyll biosynthesis pathway
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
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
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
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
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
the enzyme might be directly involved in the regulation of the metabolism of other porphyrins
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
the expression of both isoforms, POR1 and POR2, is not negatively regulated by light and persists in matured green tissues. The expression of both genes appears to be regulated by a diurnal regulation
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
O48741
light-dependent reaction
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
light-dependent reaction
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
light-dependent reaction
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
light-driven enzyme. The catalytic mechanism involves two additional steps, which do not require light
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
light-driven reaction initiated with a 50-fs laser pulse. Catalytic mechsism involves proton and hydride transfers, proceeds with time constants of 3 ps and 400 ps. Molecular motions occur on an ultrafast timescale
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
Synechocystis sp. PCC6803
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
Synechocystis sp. PCC6803
-
key regulatory step in chlorophyll biosynthesis pathway, light-driven enzyme. The catalytic mechanism involves two additional steps, which do not require light
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
Synechocystis sp. PCC6803
-
light-driven reaction initiated with a 50-fs laser pulse. Catalytic mechsism involves proton and hydride transfers, proceeds with time constants of 3 ps and 400 ps. Molecular motions occur on an ultrafast timescale
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
Q42850
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
Q01289
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
B0F833 and B0F836 and B0F837
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
B0F835 and B0F841 and B0F842
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
B0F838 and B0F839
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
B0F840
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
-
activation by light
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
-
activation by light
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
Fremyella diplosiphon
A9UGZ2, C6KHP5 and Q6H056 and Q6H058
activation by light
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + reduced ferredoxin
chlorophyllide + oxidized ferredoxin
show the reaction diagram
-
ferredoxin is the natural electron donor
-
-
?
protochlorophyllide a + NADPH
chlorophyllide a + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide a + NADPH
chlorophyllide a + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide a + NADPH
chlorophyllide a + NADP+
show the reaction diagram
P15904
-
-
-
?
protochlorophyllide a + NADPH
chlorophyllide a
show the reaction diagram
Q59987
-
-
-
?
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
show the reaction diagram
-
light-dependent reaction
-
-
?
protochlorophyllide b + NADPH + H+
chlorophyllide b + NADP+
show the reaction diagram
-
-
-
-
?
Zn-protopheophorbide a + NADPH + H+
? + NADP+
show the reaction diagram
-
efficient substrate
-
-
?
monovinyl protochlorophyllide a + NADPH
monovinyl chlorophyllide a + NADP+
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
does not accept protochlorophyllide a' or any other compounds with substituents at C-13-2 different from protochlorophyllide a
-
-
-
additional information
?
-
-
naturally occurring esterified protochlorophyllide and chemically prepared protochlorophyllide methyl ester are not substrates for the enzyme, removal of Mg2+ from the protochlorophyllide leads to inactivity of the compound as a substrate
-
-
-
additional information
?
-
-
the inhibition of por gene expression by continous far red light is mediated by phytochrome A
-
-
-
additional information
?
-
-
individual steps of the reaction catalyzed by the light-activated enzyme protochlorophyllide oxidoreductase couple with solvent dynamics, temperature-dependent UV-visible microspectrophotometry study, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
chlorophyllide a + NADP+
protochlorophyllide + NADPH + H+
show the reaction diagram
-
POR catalyzes the NADPH-dependent reduction of the C17-C18 double bond of protochlorophyllide to form chlorophyllide
-
-
r
divinyl protochlorophyllide a + NADPH
divinyl chlorophyllide a + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
O48741
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
Q41203
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
P21218, Q42536
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
Q9LKH8
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
P13653, Q42850
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
important regulatory step in chlorophyll biosynthesis
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
biosynthetic pathway leading to chlorophyll a
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
chlorophyll-biosynthetic pathway
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
chlorophyll-biosynthetic pathway
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
key enzyme for light-dependent chlorophyll biosynthesis
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
key enzyme for the light-induced greening of etiolated angiosperm plants
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
key enzyme of chlorophyll biosynthesis
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
key regulatory step in chlorophyll biosynthesis pathway
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
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
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
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
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
the enzyme might be directly involved in the regulation of the metabolism of other porphyrins
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
-
the expression of both isoforms, POR1 and POR2, is not negatively regulated by light and persists in matured green tissues. The expression of both genes appears to be regulated by a diurnal regulation
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
Synechocystis sp. PCC6803
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
show the reaction diagram
Synechocystis sp. PCC6803
-
key regulatory step in chlorophyll biosynthesis pathway
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
Q42850
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
Q01289
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
B0F833 and B0F836 and B0F837
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
B0F835 and B0F841 and B0F842
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
B0F838 and B0F839
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
B0F840
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
-
activation by light
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
-
activation by light
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
show the reaction diagram
Fremyella diplosiphon
A9UGZ2, C6KHP5 and Q6H056 and Q6H058
activation by light
-
-
?
protochlorophyllide + reduced ferredoxin
chlorophyllide + oxidized ferredoxin
show the reaction diagram
-
ferredoxin is the natural electron donor
-
-
?
protochlorophyllide a + NADPH
chlorophyllide a + NADP+
show the reaction diagram
-
-
-
-
?
monovinyl protochlorophyllide a + NADPH
monovinyl chlorophyllide a + NADP+
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
does not accept protochlorophyllide a' or any other compounds with substituents at C-13-2 different from protochlorophyllide a
-
-
-
additional information
?
-
-
naturally occurring esterified protochlorophyllide and chemically prepared protochlorophyllide methyl ester are not substrates for the enzyme, removal of Mg2+ from the protochlorophyllide leads to inactivity of the compound as a substrate
-
-
-
additional information
?
-
-
the inhibition of por gene expression by continous far red light is mediated by phytochrome A
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Ferredoxin
-
-
-
NADPH
-
no reaction with NADH
NADPH
-
no reaction with NADH
NADPH
-
stringent requirement
NADPH
-
no reaction with NADH
NADPH
-
no reaction with NADH; stringent requirement
NADPH
-
enzyme from etiolated wheat is specific for the pro-S hydrogen of NADPH
NADPH
Q9SDT1
-
NADPH
Q41203
-
NADPH
Q9LKH8
-
NADPH
B0F835 and B0F841 and B0F842
-
NADPH
B0F833 and B0F836 and B0F837
-
NADPH
B0F838 and B0F839
-
NADPH
Fremyella diplosiphon
A9UGZ2, C6KHP5 and Q6H056 and Q6H058
;
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
specifically stimulated by Ca2+
Fe2+
-
contains two 4Fe-4S clusters
Iron
-
enzyme component L-protein contains an oxygen-sensitive 4Fe-4S cluster similar to nitrogenase Fe protein. Activity quickly disappears upon exposure to air with a half-life of 20 s
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
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
Mg2+
-
required for 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
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
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2',5'-ADP
-
competitive inhibition of NADPH binding
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
EGTA
-
the enzyme activity is abolished in the presence of 10 mM EGTA
Hg2+
-
inhibitor causes seripous alterations of the enzyme structure resulting in the trans-localisation of NADPH within the active site pf POR
N-ethylmaleimide
-
inhibits the regeneration of the enzyme-substrates complex, but has no effect on the photoconversion of the preformed complex
N-ethylmaleimide
-
-
N-ethylmaleimide
-
-
Hg2+
-
depending on concentration it can react with any component of the NADPH:PChlide oxidoreductase macrodomains
additional information
-
the reaction is completely insensitive to illumination (5-20 w/m2 tungsten light)
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ATP
-
the enzyme uses ATP to drive the production of chlorophyllide a
light
-
light-activated enzyme, activation is possible at cryogenic temperatures
-
protochlorophyllide
-
stringent requirement
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0527
-
Dithionite
-
in 100 mM HEPES-NaOH (pH 7.5), 2 mM ATP, 5 mM MgCl2
0.00083
-
divinyl protochlorophyllide a
-
pH 7.5
0.000012
-
NADPH
Q59987
-
0.000013
-
NADPH
-
50C, pH 7.5
0.00046
-
NADPH
-
-
0.0042
-
NADPH
-
-
0.00867
-
NADPH
-
-
0.0087
-
NADPH
-
fusion protein with maltose-binding protein
0.011
-
NADPH
-
-
0.0268
-
NADPH
-
-
0.035
-
NADPH
-
-
0.00015
-
protochlorophyllide
-
-
0.00018
-
protochlorophyllide
-
-
0.00019
-
protochlorophyllide
-
-
0.00027
-
protochlorophyllide
-
-
0.00039
-
protochlorophyllide
-
-
0.00046
-
protochlorophyllide
-
-
0.0005
-
protochlorophyllide
-
-
0.0018
-
protochlorophyllide
-
50C, pH 7.5
0.0061
-
protochlorophyllide
-
in 100 mM HEPES-NaOH (pH 7.5), 2 mM ATP, 5 mM MgCl2
0.0106
-
protochlorophyllide
-
pH 7.4, 34C
0.01083
-
protochlorophyllide
-
-
0.035
-
protochlorophyllide
-
-
0.00027
-
protochlorophyllide a
-
fusion protein with maltose-binding protein
0.00047
-
protochlorophyllide a
P15904
-
0.0086
-
protochlorophyllide a
Q59987
-
0.00136
-
monovinyl protochlorophyllide a
-
pH 7.5
additional information
-
additional information
-
spectroscopic and detailed kinetic characterization of reaction
-
additional information
-
additional information
-
stable enzyme assay system by mixing recombinant enzyme components L-protein and NB-protein under anaerobic conditiions
-
additional information
-
additional information
-
EPR and Stark spectroscopies analysis of enzyme reaction
-
additional information
-
additional information
-
detailed steady-state kinetics characterization of enzyme
-
additional information
-
additional information
-
kinetic model with thermodynamic parameters governing catalytic interconversion rates, overview
-
0.0595
-
NADPH
-
-
additional information
-
protochlorophyllide
-
mutant K197A, relative activity 2.7%; mutant K197Q, relative activity 2.0%; mutant K197R, relative activity 2.3%; mutant Y193A, relative activity 5.5%; mutant Y193F, relative activity 19.5%; mutant Y193S, relative activity 2.4%; wild type enzyme, relative activity 100%
additional information
-
protochlorophyllide
-
mutant C199/C226S, relative activity 6.6%; mutant C199S, relative activity 98.2%; mutant C226S, relative activity 7.2%; mutant C37S/C199S/C226S, relative activity 7.1%; mutant C37S/C199S, relative activity 98.8%; mutant C37S/C226S, relative activity 6.8%; mutant C37S, relative activity 99.4%; wild type enzyme, relative activity 100%
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.011
-
NADPH
-
pH 7.5, 25C, mutant C199S/C226S, co-substrate: protochlorophyllide
0.0113
-
NADPH
-
pH 7.5, 25C, mutant C37S/C226S, co-substrate: protochlorophyllide
0.0117
-
NADPH
-
pH 7.5, 25C, mutant C37S/C199S/C226S, co-substrate: protochlorophyllide
0.0118
-
NADPH
-
pH 7.5, 25C, mutant C226S, co-substrate: protochlorophyllide
0.162
-
NADPH
-
pH 7.5, 25C, mutant C199S, co-substrate: protochlorophyllide
0.164
-
NADPH
-
pH 7.5, 25C, mutant C37S, co-substrate: protochlorophyllide
0.165
-
NADPH
-
pH 7.5, 25C, wild-type, co-substrate: protochlorophyllide
0.003
-
protochlorophyllide
-
mutant K197Q
0.004
-
protochlorophyllide
-
mutant K197A; mutant K197R; mutant Y193S
0.009
-
protochlorophyllide
-
mutant Y193A
0.011
-
protochlorophyllide
-
mutant C199/C226S; pH 7.5, 25C, mutant C199S/C226S, co-substrate: NADPH
0.0113
-
protochlorophyllide
-
mutant C37S/C226S; pH 7.5, 25C, mutant C37S/C226S, co-substrate: NADPH
0.0117
-
protochlorophyllide
-
mutant C37S/C199S/C226S; pH 7.5, 25C, mutant C37S/C199S/C226S, co-substrate: NADPH
0.0118
-
protochlorophyllide
-
mutant C226S; pH 7.5, 25C, mutant C226S, co-substrate: NADPH
0.032
-
protochlorophyllide
-
mutant Y193F
0.162
-
protochlorophyllide
-
mutant C199S; pH 7.5, 25C, mutant C199S, co-substrate: NADPH
0.163
-
protochlorophyllide
-
mutant C37S/C199S
0.164
-
protochlorophyllide
-
wild type enzyme
0.164
-
protochlorophyllide
-
mutant C37S; pH 7.5, 25C, mutant C37S, co-substrate: NADPH
0.165
-
protochlorophyllide
-
pH 7.5, 25C, wild-type, co-substrate: NADPH; wild type enzyme
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00302
-
2',5'-ADP
-
calculated competitive inhibition constant
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00315
-
-
in 100 mM HEPES-NaOH (pH 7.5), 2 mM ATP, 5 mM MgCl2
0.5
-
-
etioplast membranes
0.7
-
-
prolamellar body
0.8
-
-
sonicated membranes
3.3
-
-
prothylakoid
13.9
-
-
-
additional information
-
-
1.6 nmol chlorophyllide/mg protein/flash
additional information
-
-
-
additional information
-
-
1760 pmol/mg/flash in prolamellar bodies
additional information
-
-
1.49 chlorophyllide synthesis/flash per mg protein
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
stopped-flow experiments
7.5
-
-
activity assay
7.5
-
-
activity assay; assay at
7.5
-
-
activity assay; activity assay
8.5
-
-
mutant y-7
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
23
-
-
activity assay at room temperature; activity assay at room temperature
23
-
-
activity assay at room temperature
25
-
-
stopped-flow experiments
25
-
-
activity assay
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10
60
-
linear drop of the relative concentration of the enzyme protein up to 30C
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
translocon constituent toc33 is indispensable for the import of isoform PorB
Manually annotated by BRENDA team
Q41249
low expression, light-response during greening, expression in mature cells
Manually annotated by BRENDA team
-
high expression in dark-grown cells, no light response during greening. Constitutive enzym, expression in mature cells; high expression in dark-grown cells, no light response during greening. Very low expression in mature cells
Manually annotated by BRENDA team
P15904
high expression in, no light-response during greening
Manually annotated by BRENDA team
-
high expression in, no light-response during greening
Manually annotated by BRENDA team
P13653, Q42850
high expression in, constitutive enzyme; very high expression in, no light-response during greening, undetectable in mature cells
Manually annotated by BRENDA team
Q8LSZ2, Q8LSZ3
high expression in, light-response during greening, expression in mature cells; medium expression in, light-response during greening, expression in mature cells
Manually annotated by BRENDA team
-, Q41203
high expression in dark-grown cell, constitutive enzyme; high expression in dark-grown cell, no light-response during greening
Manually annotated by BRENDA team
-
high expression in dark-grown cell, light-resonse during greening
Manually annotated by BRENDA team
Q41578
high expression in, no light-response during greening
Manually annotated by BRENDA team
Q9LKH8
high expression in, constitutive enzyme
Manually annotated by BRENDA team
-
undetectable in dark-grown cells, light response during greening. Expression in mature cells
Manually annotated by BRENDA team
O80333
undetectable in dark-grown cell, light-response during greening
Manually annotated by BRENDA team
-
isoform POR1 and POR2 are active
Manually annotated by BRENDA team
-
carotinoid deficiency in norflurazon-treated leaves leads to a loser attachment of enzyme molecules to the lipid phase and its early dissociation from the membranes during the light-induced transformation of prolamellar bodies
Manually annotated by BRENDA team
-
translocon constituent toc33 is indispensable for the import of isoform PorB
Manually annotated by BRENDA team
-
POR1 is active in dark-grown seedlings
Manually annotated by BRENDA team
-
strong expression of enzyme isoforms PorA, PorB in early seedling development
Manually annotated by BRENDA team
additional information
-
photosynthetic active tissue
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
B0F835 and B0F841 and B0F842
-
Manually annotated by BRENDA team
B0F833 and B0F836 and B0F837
-
Manually annotated by BRENDA team
-
nuclear-encoded cytoplasmically sythesized, posttranslationally processed on import into plastids
Manually annotated by BRENDA team
-
nuclear-encoded cytoplasmically sythesized, posttranslationally processed on import into plastids
Manually annotated by BRENDA team
-
PORA precursor, pPORA
Manually annotated by BRENDA team
-
etioplast internal membrane
Manually annotated by BRENDA team
-
etioplast internal membrane
Manually annotated by BRENDA team
-
etioplast membrane
Manually annotated by BRENDA team
-
prolamellar body
Manually annotated by BRENDA team
-
from prolamellar body to stroma of etioplast
Manually annotated by BRENDA team
-
peripheral membrane protein
Manually annotated by BRENDA team
-
; contains two photochemically active forms of the enzyme: protochlorophyllide oxidoreductase POR-PChlide640 and POR-PChlide650. Resuspension of prolamellar bodies in media with a pH below 6.8 leads to a rapid conversuion of POR-PChlide650 to POR-PChlide 640 and a dramatic reorganization of the membrane system of the prolamellar body. The disappearence of POR-PChlide 650 and the reorganization of the prolamellar body are irreversible
Manually annotated by BRENDA team
-
plastid membrane
Manually annotated by BRENDA team
-
outside the plastid in the area of the plasmalemma
Manually annotated by BRENDA team
-
inner plastid membrane
Manually annotated by BRENDA team
-
plastid membrane-associated
Manually annotated by BRENDA team
-
nucleus-encoded enzyme is synthesized as a larger precursor in the cytosol and imported into the plastid in a substrate-dependent manner. Plastid envelope membrane proteins, called protochlorophyllide-dependent translocon proteins, Ptcs, interact with pPORA during import. Partial suppression of pPORB import in white light
Manually annotated by BRENDA team
-
import of isoform PorA into plastids of cotyledons is substrate-dependent and organ-specific
Manually annotated by BRENDA team
-
thylakoid-membrane-bound
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
32000
-
-
gel filtration
34000
-
-
-
34000
-
-
2 related peptides of 34000/35000
34000
-
-
2 related peptides of 34000/36000
34000
-
-
SDS-PAGE
35000
-
-
covalent radioactive labelling technique, 2 labelled peptides identified, whether the 2 peptides are subunits of a polymeric reductase or represent 2 isoenzymes of the reductase remains to be established
35000
-
-
gel filtration; SDS-PAGE shows 2 closely related peptides of 35000 and 37000
35000
-
-
gel filtration
35000
-
-
SDS-PAGE shows 2 closely related peptides of 35000 and 37000
35000
-
-
-
35000
-
-
2 related peptides of 34000/35000
35000
-
-
-
35000
-
-
SDS-PAGE shows 2 closely related peptides of 35000 and 37000
36000
-
-
SDS-PAGE
36000
-
-
gel filtration
36000
-
-
predicted from amino acid composition
36000
-
-
2 related peptides of 36000/38000
37000
-
-
covalent radioactive labelling technique
37000
-
-
gel filtration, doublet of 2 peptides of 35000 and 37000 co-purified
37000
-
-
-
37000
-
-
gel filtration, doublet of 2 peptides of 35000 and 37000 co-purified
37000
-
-
-
37000
-
-
gel filtration, doublet of 2 peptides of 35000 and 37000 co-purified
37800
-
-
amino acid composition
38000
-
-
gel filtration
38000
-
-
-
40000
-
-
determined by SDS-PAGE
41000
-
-
identified with monospecific polyclonal antibody
41200
-
-
predicted from cDNA
42000
-
-
determined by SDS-PAGE
44000
-
-
precursor polypeptide, predicted from mRNA
44000
-
-
-
60000
-
-
purified ChlL subunit, gel filtration
63000
-
-
-
78800
-
-
recombinant fusion protein, gel filtration
100000
-
-
-
112000
-
-
substrate-enzyme complex, gel filtration
210000
-
-
purified ChlNB complex, gel filtration
360000
-
Q7VD39
-
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 40150, recombinant enzyme, SDS-PAGE
?
-
x * 36000, SDS-PAGE, x * 36046, calculated, S-tagged L-protein, x * 52000, SDS-PAGE, x * 48671, calculated, S-tagged N-protein, x * 60000, SDS-PAGE, x * 57191, calculated, B-protein
?
-
x * 46000, precursor protein, x * 38000, mature protein
dimer
-
2 * 45000, SDS-PAGE
dimer
-
recombinant fusion protein, gel filtration
dimer
-
POR proteins in Arabidopsis consist of dimers
heterotetramer
-
2 * 46199 + 2 * 58729, purified ChlNB complex, deduced from amino acid sequence
homodimer
-
2 * 32395, purified ChlL subunit, deduced from amino acid sequence
monomer
-
1 * 36000, SDS-PAGE
octamer
Q7VD39
heterooctameric complex: subunits N and B are structurally homologous, generating a pseudo-2fold symmetry axis that is colinear with the molecular twofold axis of L2. Both [4Fe-4S] clusters are centered around this extended axis: the L2 cluster is symmetrically ligated by four cysteinyl ligands between the two subunits, whereas the NB cluster is asymmetrically ligated by three cysteine residues from N and one aspartate residue from B
oligomer
-
oligomeric PORA-PORB complex
oligomer
-
barley PORA can form a five-unit oligomer that interacts with a single PORB
monomer
-
1 * 36000, SDS-PAGE
additional information
-
recombinant enzyme component L-protein forms a dimer, recombinant components NB-protein form a heterotetramer, gel filtration
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
-
x * 46000 Da, precursor protein, x * 38000 Da, mature protein
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the X-ray crystallographic structure of the substrate-bound, ADP-aluminium fluoride-stabilized (ADP-AlF3-stabilized) transition state complex between the DPOR components L2 and (NB)2 from the marine cyanobacterium Prochlorococcus marinus is reported
Q7VD39
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
90
-
-
the enzyme activity is abolished after heating of the membranes (90C, 5 min)
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
active enzyme is protected by NADPH, protochlorophyllide and glycerol
-
unstable membrane-bound protein
-
active enzyme is protected by NADPH, protochlorophyllide and glycerol
-
protochlorophyllide and NADPH enhances the stability of the enzyme
-
rapid breakdown of the enzyme protein in vitro, caused by a membrane-bound proteolytic activity
-
unstable membrane-bound protein
-
active enzyme is protected by NADPH, protochlorophyllide and glycerol
-
rapid loss of activity during attempts to purify
-
unstable membrane-bound protein
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
0C, can be kept in elution buffer for at least 3h without any detectable loss of activity
-
4C, stored in elution buffer retains full activity for many weeks
-
enzyme in crude extracts stable for more than 6 months when maintained anaerobically at 4C, with no significant loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
using a chitin bead column, the chitin-intein tag is removed; using a chitin bead column, the chitin-intein tag is removed
-
glutathione-Sepharose column chromatography
-
using His-Bind resin
-
by Ni-NTA agarose chromatography
-
etioplasts are isolated
Q42850
PORb heterologously overexpressed in Escherichia coli
-
isolated from pea leaves
Q01289
recombinant fusion protein
-
wild-type and recombinant pea enzyme, heterologously expressed in Escherichia coli
-
glutathione Sepharose column chromatography
-
both activities of the components protein L and proteins NB are rapidly lost during purification procedures, such as affinity chromatography with S-protein agarose. Attempts to purify the active components have so far been unsuccessful
-
NB-protein component from Pchlide oxidoreductase
-
wild-type and recombinant pea enzyme, heterologously expressed in Escherichia coli
-
using His-Bind resin
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cDNAs and/or gens encoding POR, also referred to as LPCR or PCR in some studies isolated; full-length cDNA, coding for PCR
-
expressed in Escherichia coli strain SG13009
-
expression in Escherichia coli BL21
-
full-length cDNA, coding for PCR
-
full-length cDNA, coding for PCR; POR C cloned and expressed in Escherichia coli
-
yes into the vector pTYB for expression in Escherichia coli BL21DE3 cells; yes into the vector pTYB for expression in Escherichia coli BL21DE3 cells, for the construction of transgenic plants pDONR/ZeO and pGWB2 vectors are used
-
expressed in Escherichia coli BL21(DE3) Codon Plus RIL cells
-
for sequencing
B0F840
for sequencing
B0F835 and B0F841 and B0F842
a genomic library is constructed, the vector pZERO is used; a genomic library is constructed, the vector pZERO is used
Fremyella diplosiphon
A9UGZ2, C6KHP5 and Q6H056 and Q6H058
expression in Escherichia coli cells
-
for sequencing
B0F833 and B0F836 and B0F837
for sequencing
B0F838 and B0F839
barley POR expressed in Escherichia coli as a beta-galactosidase fusion protein
-
cDNA library constructed in pBR322, full-length cDNA cloned, cDNA inserts subcloned in the M13 phage and expressed in Escherichia coli
-
into the vector pQE30
-
overexpressed in Escherichia coli as a fusion protein with the maltose-binding protein
-
cloning of the gene encoding protochlorophyllide reductase
-
cloning of the nuclear gene
-
expressed in Rhodobacter capsulatus SB1003, JDA, JDB and ZY5
-
expression in Rhodobacter capsulatus mutant deficient in Bchl biosynthesis. The NADPH:protochlorophyllide oxidoreductase is integrated in the porphyrin biosynthesis network and its activity leads to the formation of photosynthetic chlorophyll proteins
-
mature pea POR cloned into the pAlter-1 mutagenesis vector, expressed in Escherichia coli JM109
-
overexpressed as a fusion with maltose-binding protein in Escherichia coli using expression plasmid pKK233-2
-
overexpression in Escherichia coli as a fusion protein with maltose-binding protein
-
cloned and overproduced in Escherichia coli with a hexahistidine tag at the N-terminus
-
overexpression in Escherichia coli as a His6-tagged protein
Q59987
expression in Escherichia coli cells
-
expressed in Escherichia coli
-
expressed in Escherichia coli; expression in Escherichia coli cells
-
expression in Escherichia coli cells
-
overexpression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
down-regulated in green light and in the dark; down-regulated in the dark
Fremyella diplosiphon
A9UGZ2, C6KHP5 and Q6H056 and Q6H058
up-regulated in green light
Fremyella diplosiphon
A9UGZ2, C6KHP5 and Q6H056 and Q6H058
PORA represents the negatively light-regulated POR enzyme
-
OsPORA is decreased dramatically in fully mature leaves
-
OsPORB expression is regulated in a circadian rhythm in short-day conditions
-
OsPORA is expressed at high levels in developing leaves; OsPORB expression is rapidly upregulated by high light treatment
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C103S
-
the BchN subunit variant shows 0.5% residual activity and is essentially inactive
C21S
-
the BchN subunit variant shows 0.5% residual activity and is essentially inactive
C46S
-
the BchN subunit variant shows 0.5% residual activity and is essentially inactive
C104A
-
no detectable effect on the import of protein to plastid and processing in darkness
C166A
-
no detectable effect on the import of protein to plastid and processing in darkness
C195A
-
mutant, constructed for the identification of the protochlorophyllide binding site
C222A
-
mutant, constructed for the identification of the protochlorophyllide binding site
C276A
-
decrease in mature enzyme protein present in plastid and decrease in the amount of protochlorophyllide bound to enzyme. C276 constitutes the protochlorophyllide binding site in the active centre of enzyme
C303A
-
decrease in mature enzyme protein present in plastid and decrease in the amount of protochlorophyllide bound to enzyme. C303 constitutes a low affinity protochlorophyllide binding site involved in assembly and stabilization of imported enzyme inside etioplasts
C33A
-
mutant, constructed for the identification of the protochlorophyllide binding site
C85A
-
mutant, constructed for the identification of the protochlorophyllide binding site
H394A
Q7VD39
mutant retains only a moderate activity which points to a critical role of this residue in the specific protonation at C-18, probably by positioning a water molecule at a distance of 3.2 A from C-18 above the ring
Y189F
-
mutant, the putative proton donor, Tyr 189, is replaced by a phenylalanine residue
C199/C226S
-
mutant, mutation of the absolutely conserved cysteine residues
C199S
-
kcat comparable to wild-type, relative activity comparable to wild-type, Kd (NADPH) comparable to wild-type, Kd (protochlorophyllide) comparable to wild-type; mutant, Cys199 has a relatively minor role in catalysis
C199S/C226S
-
kcat more that 10fold decreased to wild-type, relative activity highly decreased compared to wild-type, Kd (NADPH) 2fold increased compared to wild-type, Kd (protochlorophyllide) 6fold increased compared to wild-type
C226S
-
kcat more that 10fold decreased to wild-type, relative activity highly decreased compared to wild-type, Kd (NADPH) comparable to wild-type, Kd (protochlorophyllide) 4fold increased compared to wild-type; mutant, mutation causes a remarkable change in the mechansim of the hydrogen transfer reactions
C37S
-
kcat comparable to wild-type, relative activity comparable to wild-type, Kd (NADPH) increased compared to wild-type, Kd (protochlorophyllide) equal to wild-type; mutant, Cys37 has a relatively minor role in catalysis
C37S/C199S
-
kcat comparable to wild-type, relative activity comparable to wild-type, Kd (NADPH) 10fold increased compared to wild-type, Kd (protochlorophyllide) comparable to wild-type; mutant, mutation of the absolutely conserved cysteine residues
C37S/C199S/C226S
-
kcat more that 10fold decreased to wild-type, relative activity highly decreased compared to wild-type, Kd (NADPH) 10fold increased compared to wild-type, Kd (protochlorophyllide) 6fold increased compared to wild-type; mutant, mutation of the absolutely conserved cysteine residues
C37S/C226S
-
kcat more that 10fold decreased to wild-type, relative activity highly decreased compared to wild-type, Kd (NADPH) 10fold increased compared to wild-type, Kd (protochlorophyllide) 6fold increased compared to wild-type; mutant, mutation of the absolutely conserved cysteine residues
K197A
-
mutant, constructed for analysing the role of the conserved active site lysine
K197Q
-
mutant, constructed for analysing the role of the conserved active site lysine
K197R
-
mutant, constructed for analysing the role of the conserved active site lysine
Y193A
-
mutant, constructed for analysing the role of the conserved active site tyrosine
Y193F
-
mutant, constructed for analysing the role of the conserved active site tyrosine
Y193S
-
mutant, constructed for analysing the role of the conserved active site tyrosine
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
POR is an ideal model for studying catalysis near the solvent glass transition