Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
bchL
-
gene name of subunit
bchN
-
gene name of subunit
dark active protochlorophyllide oxidoreductase
dark operative protochlorophyllide oxidoreductase
-
-
dark-operative protochlorophyllide oxidoreductase
LHPP
-
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
-
light-dependent NADPH-protochlorophyllide oxidoreductase
-
-
light-dependent NADPH: protochlorophyllide oxidoreductase
-
-
light-dependent NADPH:Pchlide oxidoreductase
-
-
light-dependent NADPH:protochlorophyllide oxidoreductase
light-dependent Pchlide oxidoreductase
Light-dependent protochlorophyllide oxidoreductase
light-driven enzyme protochlorophyllide oxidoreductase
light-independent (dark) Pchlide oxidoreductase
-
-
light-independent NADPH:protochlorophyllide oxidoreductase
-
-
light-independent protochlorophyllide oxidoreductase
NADPH Pchlide oxidoreductase
-
-
NADPH-Pchlide 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 B
-
NADPH:Pchlide oxidoreductase
NADPH:Pchlide oxidoreductase A
-
-
NADPH:protochlorophyllide (Pchlide) oxidoreductase
NADPH:protochlorophyllide oxidoreductase
NADPH:protochlorophyllide oxidoreductase A
NADPH:protochlorophyllide oxidoreductase B
Pchlide oxidoreductase
-
-
protochlorophyllide oxidoreductase
protochlorophyllide oxidoreductase A
protochlorophyllide oxidoreductase B
-
protochlorophyllide oxidoreductase C
protochlorophyllide oxidoreductase POR-PChlide640
-
-
protochlorophyllide oxidoreductase POR-PChlide650
-
-
protochlorophyllide photooxidoreductase
-
-
-
-
protochlorophyllide reductase
bchB
-
-
bchB
-
gene name of subunit
dark active protochlorophyllide oxidoreductase
-
dark active protochlorophyllide oxidoreductase
-
dark active protochlorophyllide oxidoreductase
-
dark active protochlorophyllide oxidoreductase
-
dark-operative protochlorophyllide oxidoreductase
-
-
dark-operative protochlorophyllide oxidoreductase
-
dark-operative protochlorophyllide oxidoreductase
-
dark-operative protochlorophyllide oxidoreductase
-
-
dark-operative protochlorophyllide oxidoreductase
-
consists of the two components, L-protein (BchL-dimer) and NB-protein (BchN-BchBheterotetramer)
DPOR
-
-
DPOR
-
consists of the homodimeric protein complex ChlL2 and a heterotetrameric protein complex (ChlNB)2
light-dependent NADPH:protochlorophyllide oxidoreductase
-
-
light-dependent NADPH:protochlorophyllide oxidoreductase
-
light-dependent NADPH:protochlorophyllide oxidoreductase
-
light-dependent NADPH:protochlorophyllide oxidoreductase
-
light-dependent NADPH:protochlorophyllide oxidoreductase
-
-
light-dependent NADPH:protochlorophyllide oxidoreductase
-
light-dependent NADPH:protochlorophyllide oxidoreductase
-
light-dependent NADPH:protochlorophyllide oxidoreductase
-
-
light-dependent NADPH:protochlorophyllide oxidoreductase
-
light-dependent Pchlide oxidoreductase
-
light-dependent Pchlide oxidoreductase
-
-
Light-dependent protochlorophyllide oxidoreductase
-
-
Light-dependent protochlorophyllide oxidoreductase
-
Light-dependent protochlorophyllide oxidoreductase
-
-
Light-dependent protochlorophyllide oxidoreductase
-
-
Light-dependent protochlorophyllide oxidoreductase
-
Light-dependent protochlorophyllide oxidoreductase
-
-
Light-dependent protochlorophyllide oxidoreductase
-
-
-
Light-dependent protochlorophyllide oxidoreductase
-
Light-dependent protochlorophyllide oxidoreductase
-
Light-dependent protochlorophyllide oxidoreductase
-
Light-dependent protochlorophyllide oxidoreductase
-
Light-dependent protochlorophyllide oxidoreductase
-
-
Light-dependent protochlorophyllide oxidoreductase
-
-
Light-dependent protochlorophyllide oxidoreductase
-
Light-dependent protochlorophyllide oxidoreductase
-
-
Light-dependent protochlorophyllide oxidoreductase
Thermosynechococcus vestitus
-
light-driven enzyme protochlorophyllide oxidoreductase
-
-
light-driven enzyme protochlorophyllide oxidoreductase
-
-
light-driven enzyme protochlorophyllide oxidoreductase
-
-
light-driven enzyme protochlorophyllide oxidoreductase
-
-
light-driven enzyme protochlorophyllide oxidoreductase
-
-
light-driven enzyme protochlorophyllide oxidoreductase
-
-
light-driven enzyme protochlorophyllide oxidoreductase
-
-
light-driven enzyme protochlorophyllide oxidoreductase
-
-
light-driven enzyme protochlorophyllide oxidoreductase
-
-
light-driven enzyme protochlorophyllide oxidoreductase
-
-
light-independent protochlorophyllide oxidoreductase
-
-
light-independent protochlorophyllide oxidoreductase
-
-
-
light-independent protochlorophyllide oxidoreductase
-
light-independent protochlorophyllide oxidoreductase
-
light-independent protochlorophyllide oxidoreductase
-
light-independent protochlorophyllide oxidoreductase
-
light-independent protochlorophyllide oxidoreductase
-
LIPOR
-
-
LPOR
-
-
-
-
LPOR
Thermosynechococcus vestitus
-
NADPH-Pchlide oxidoreductase
-
-
NADPH-Pchlide oxidoreductase
-
-
NADPH-protochlorophyllide oxidoreductase
-
-
-
-
NADPH-protochlorophyllide oxidoreductase
-
-
NADPH: protochlorophyllide oxidoreductase
-
-
NADPH: protochlorophyllide oxidoreductase
-
NADPH: protochlorophyllide oxidoreductase A
-
-
NADPH: protochlorophyllide oxidoreductase A
-
NADPH:Pchlide oxidoreductase
-
NADPH:Pchlide oxidoreductase
-
NADPH:Pchlide oxidoreductase
-
-
NADPH:Pchlide oxidoreductase
-
NADPH:Pchlide oxidoreductase
-
-
NADPH:Pchlide oxidoreductase
-
NADPH:Pchlide oxidoreductase
-
NADPH:Pchlide oxidoreductase
-
-
NADPH:Pchlide oxidoreductase
-
NADPH:protochlorophyllide (Pchlide) oxidoreductase
-
-
NADPH:protochlorophyllide (Pchlide) oxidoreductase
-
-
NADPH:protochlorophyllide oxidoreductase
-
-
NADPH:protochlorophyllide oxidoreductase
-
NADPH:protochlorophyllide oxidoreductase
-
-
NADPH:protochlorophyllide oxidoreductase
-
NADPH:protochlorophyllide oxidoreductase
-
-
NADPH:protochlorophyllide oxidoreductase
-
NADPH:protochlorophyllide oxidoreductase
-
-
NADPH:protochlorophyllide 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
-
-
NADPH:protochlorophyllide oxidoreductase B
-
-
PCR
-
-
POR
-
-
POR
Thermosynechococcus vestitus
-
-
POR
Thermosynechococcus vestitus
-
POR A
-
-
POR B
-
-
POR C
-
-
POR-A
-
POR-B
-
POR1
-
-
POR2
-
-
PORA
-
-
PORB
-
-
PORC
-
-
protochlorophyllide oxidoreductase
-
-
-
-
protochlorophyllide oxidoreductase
-
protochlorophyllide oxidoreductase
-
protochlorophyllide oxidoreductase
-
protochlorophyllide oxidoreductase
-
-
protochlorophyllide oxidoreductase
-
protochlorophyllide oxidoreductase
-
protochlorophyllide oxidoreductase
-
protochlorophyllide oxidoreductase
-
-
protochlorophyllide oxidoreductase
-
-
protochlorophyllide oxidoreductase
Thermosynechococcus vestitus
-
-
protochlorophyllide oxidoreductase A
-
-
protochlorophyllide oxidoreductase A
-
protochlorophyllide oxidoreductase C
-
-
protochlorophyllide oxidoreductase C
-
protochlorophyllide reductase
-
protochlorophyllide reductase
-
-
protochlorophyllide reductase
-
protochlorophyllide reductase
-
-
protochlorophyllide reductase
-
protochlorophyllide reductase
-
protochlorophyllide reductase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
?
chlorophyllide a + NADP+
protochlorophyllide + NADPH + H+
divinyl protochlorophyllide a + NADPH
divinyl chlorophyllide a + NADP+
Thermosynechococcus vestitus
-
-
-
-
?
monovinyl protochlorophyllide a + NADPH
monovinyl chlorophyllide a + NADP+
Thermosynechococcus vestitus
-
-
-
-
?
protochlorophyllide + dithionite
chlorophyllide + SO2
-
-
-
-
?
protochlorophyllide + dithiothreitol
chlorophyllide + oxidized dithiothreitol
-
-
-
-
?
protochlorophyllide + NADH + H+
chlorophyllide a + NAD+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
protochlorophyllide + reduced ferredoxin
chlorophyllide + oxidized ferredoxin
-
ferredoxin is the natural electron donor
-
-
?
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
protochlorophyllide b + NADPH + H+
chlorophyllide b + NADP+
-
-
-
-
?
Zn-protopheophorbide a + NADPH + H+
? + NADP+
-
efficient substrate
-
-
?
additional information
?
-
chlorophyllide a + NADP+
protochlorophyllide + NADPH + H+
-
-
-
r
chlorophyllide a + NADP+
protochlorophyllide + NADPH + H+
-
-
-
r
chlorophyllide a + NADP+
protochlorophyllide + NADPH + H+
-
-
-
?
chlorophyllide a + NADP+
protochlorophyllide + NADPH + H+
Thermosynechococcus vestitus
-
POR catalyzes the NADPH-dependent reduction of the C17-C18 double bond of protochlorophyllide to form chlorophyllide
-
-
r
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
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+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
key enzyme of chlorophyll biosynthesis
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
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+
-
light-dependent reaction
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
light-dependent reaction
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
393835, 393836, 393837, 393838, 393839, 393841, 393843, 393845, 393848, 393852, 393853, 393858, 393859, 393861, 393866 -
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
key enzyme for light-dependent chlorophyll biosynthesis
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
light-dependent reaction
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
393832, 393833, 393834, 393836, 393838, 393839, 393841, 393842, 393843, 393844, 393848, 393851, 393852, 393853, 393855, 393856, 393857, 393858, 393859, 393860, 393865, 657112 -
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
biosynthetic pathway leading to chlorophyll a
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
chlorophyll-biosynthetic pathway
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
key enzyme for the light-induced greening of etiolated angiosperm plants
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
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+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
important regulatory step in chlorophyll biosynthesis
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
chlorophyll-biosynthetic pathway
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
the enzyme might be directly involved in the regulation of the metabolism of other porphyrins
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
key regulatory step in chlorophyll biosynthesis pathway
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
light-driven enzyme. The catalytic mechanism involves two additional steps, which do not require light
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
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+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Thermosynechococcus vestitus
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Thermosynechococcus vestitus BP-1
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
393842, 393843, 393844, 393846, 393847, 393848, 393851, 393853, 393855, 393857, 393858, 656911 -
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
activation by light
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
activation by light
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
Thermosynechococcus vestitus
-
activation by light
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
the enzyme (LPOR) catalyzes a photocatalytic reaction
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
r
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
the enzyme (LPOR) catalyzes a photocatalytic reaction
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
r
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
r
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
r
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
the enzyme (LPOR) catalyzes a photocatalytic reaction
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
r
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
the enzyme (LPOR) catalyzes a photocatalytic reaction
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
the enzyme (LPOR) catalyzes a photocatalytic reaction
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
the enzyme (LPOR) catalyzes a photocatalytic reaction
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Thermosynechococcus vestitus
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Thermosynechococcus vestitus
-
light-dependent reaction of chlorophyll biosynthesis
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Thermosynechococcus vestitus
stepwise hydride transfer. The enzyme catalyzes the stereospecific trans addition of a hydride anion and a proton across the C17-C18 double bond of protochlorophyllide
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
the enzyme (LPOR) catalyzes a photocatalytic reaction
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
Thermosynechococcus vestitus
-
light-dependent reaction
-
-
?
additional information
?
-
-
-
-
-
?
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
?
-
-
the enzyme consists of an ATP-dependent reductase component, L-protein (a BchL dimer), and a catalytic component, NB-protein (a BchNeBchB heterotetramer). The L-protein transfers electrons to the NB-protein to reduce Pchlide, which is coupled with ATP hydrolysis
-
-
?
additional information
?
-
Thermosynechococcus vestitus
-
individual steps of the reaction catalyzed by the light-activated enzyme protochlorophyllide oxidoreductase couple with solvent dynamics, temperature-dependent UV-visible microspectrophotometry study, overview
-
-
?
additional information
?
-
-
does not accept protochlorophyllide a' or any other compounds with substituents at C-13-2 different from protochlorophyllide a
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
chlorophyllide a + NADP+
protochlorophyllide + NADPH + H+
divinyl protochlorophyllide a + NADPH
divinyl chlorophyllide a + NADP+
Thermosynechococcus vestitus
-
-
-
-
?
monovinyl protochlorophyllide a + NADPH
monovinyl chlorophyllide a + NADP+
Thermosynechococcus vestitus
-
-
-
-
?
protochlorophyllide + NADH + H+
chlorophyllide a + NAD+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
protochlorophyllide + reduced ferredoxin
chlorophyllide + oxidized ferredoxin
-
ferredoxin is the natural electron donor
-
-
?
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
additional information
?
-
chlorophyllide a + NADP+
protochlorophyllide + NADPH + H+
-
-
-
r
chlorophyllide a + NADP+
protochlorophyllide + NADPH + H+
-
-
-
r
chlorophyllide a + NADP+
protochlorophyllide + NADPH + H+
Thermosynechococcus vestitus
-
POR catalyzes the NADPH-dependent reduction of the C17-C18 double bond of protochlorophyllide to form chlorophyllide
-
-
r
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
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+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
key enzyme of chlorophyll biosynthesis
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
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+
-
-
393835, 393836, 393837, 393838, 393839, 393841, 393843, 393845, 393848, 393852, 393853, 393858, 393861, 393866 -
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
key enzyme for light-dependent chlorophyll biosynthesis
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
393833, 393836, 393838, 393839, 393841, 393842, 393843, 393844, 393851, 393852, 393853, 393855, 393857, 393858, 393859, 393860, 393865 -
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
biosynthetic pathway leading to chlorophyll a
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
chlorophyll-biosynthetic pathway
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
key enzyme for the light-induced greening of etiolated angiosperm plants
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
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+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
important regulatory step in chlorophyll biosynthesis
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
chlorophyll-biosynthetic pathway
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
the enzyme might be directly involved in the regulation of the metabolism of other porphyrins
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
key regulatory step in chlorophyll biosynthesis pathway
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Thermosynechococcus vestitus
-
-
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
393842, 393843, 393844, 393846, 393847, 393848, 393851, 393853, 393855, 393857, 393858 -
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
constitutive enzyme
-
-
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
activation by light
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
activation by light
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
Thermosynechococcus vestitus
-
activation by light
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
the enzyme (LPOR) catalyzes a photocatalytic reaction
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
r
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
r
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
r
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
r
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
the enzyme (LPOR) catalyzes a photocatalytic reaction
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
r
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
the enzyme (LPOR) catalyzes a photocatalytic reaction
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
the enzyme (LPOR) catalyzes a photocatalytic reaction
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Thermosynechococcus vestitus
-
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Thermosynechococcus vestitus
-
light-dependent reaction of chlorophyll biosynthesis
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
the enzyme (LPOR) catalyzes a photocatalytic reaction
-
-
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
-
-
-
?
additional information
?
-
-
-
-
-
?
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
?
-
-
does not accept protochlorophyllide a' or any other compounds with substituents at C-13-2 different from protochlorophyllide a
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0527
Dithionite
-
in 100 mM HEPES-NaOH (pH 7.5), 2 mM ATP, 5 mM MgCl2
0.00083
divinyl protochlorophyllide a
Thermosynechococcus vestitus
-
pH 7.5
0.00136
monovinyl protochlorophyllide a
Thermosynechococcus vestitus
-
pH 7.5
0.00015 - 0.035
protochlorophyllide
0.00027 - 0.0086
protochlorophyllide a
additional information
additional information
-
0.000012
NADPH
-
0.000013
NADPH
Thermosynechococcus vestitus
-
50°C, pH 7.5
0.0008
NADPH
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme P158F
0.0009
NADPH
Thermosynechococcus vestitus
-
pH 7.5, 40°C, wild-type enzyme
0.001
NADPH
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme F233Y
0.0013
NADPH
-
pH and temperature not specified in the publication
0.0022
NADPH
-
pH and temperature not specified in the publication
0.0022
NADPH
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme K156N/I157V
0.0025
NADPH
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme F237Y
0.0029
NADPH
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme F233L
0.0029
NADPH
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme I157V
0.0029
NADPH
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme K156N
0.0033
NADPH
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme P158A
0.0048
NADPH
-
pH and temperature not specified in the publication
0.0059
NADPH
-
pH and temperature not specified in the publication
0.0085
NADPH
pH 7.5, 30°C
0.0087
NADPH
-
fusion protein with maltose-binding protein
0.0098
NADPH
-
pH and temperature not specified in the publication
0.0578
NADPH
-
pH and temperature not specified in the publication
0.124
NADPH
-
pH and temperature not specified in the publication
0.138
NADPH
-
pH and temperature not specified in the publication
0.157
NADPH
-
pH and temperature not specified in the publication
0.172
NADPH
-
pH and temperature not specified in the publication
0.00015
protochlorophyllide
-
0.00018
protochlorophyllide
-
-
0.00019
protochlorophyllide
-
-
0.00027
protochlorophyllide
-
-
0.00039
protochlorophyllide
-
0.00046
protochlorophyllide
-
-
0.0005
protochlorophyllide
-
-
0.0012
protochlorophyllide
-
pH and temperature not specified in the publication
0.0017
protochlorophyllide
-
pH and temperature not specified in the publication
0.0018
protochlorophyllide
Thermosynechococcus vestitus
-
50°C, pH 7.5
0.002
protochlorophyllide
-
pH and temperature not specified in the publication
0.0023
protochlorophyllide
-
pH and temperature not specified in the publication
0.0023
protochlorophyllide
-
pH and temperature not specified in the publication
0.0024
protochlorophyllide
-
pH and temperature not specified in the publication
0.0043
protochlorophyllide
-
pH and temperature not specified in the publication
0.0055
protochlorophyllide
-
pH and temperature not specified in the publication
0.0061
protochlorophyllide
-
in 100 mM HEPES-NaOH (pH 7.5), 2 mM ATP, 5 mM MgCl2
0.0069
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme F237Y
0.0075
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme F233L
0.0077
protochlorophyllide
-
pH and temperature not specified in the publication
0.0078
protochlorophyllide
pH 7.5, 30°C
0.0078
protochlorophyllide
-
pH and temperature not specified in the publication
0.0078
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 40°C, wild-type enzyme
0.0081
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme F233Y
0.0106
protochlorophyllide
-
pH 7.4, 34°C
0.0107
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme I157V
0.01083
protochlorophyllide
-
-
0.0135
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme P158A
0.0151
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme K156N
0.0166
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme K156N/I157V
0.0181
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme P158F
0.035
protochlorophyllide
-
-
0.00027
protochlorophyllide a
-
fusion protein with maltose-binding protein
0.00047
protochlorophyllide a
-
0.0086
protochlorophyllide a
-
additional information
additional information
Thermosynechococcus vestitus
-
detailed steady-state kinetics characterization of enzyme
-
additional information
additional information
-
EPR and Stark spectroscopies analysis of enzyme reaction
-
additional information
additional information
Thermosynechococcus vestitus
-
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
Thermosynechococcus vestitus
-
kinetic model with thermodynamic parameters governing catalytic interconversion rates, overview
-
additional information
protochlorophyllide
Thermosynechococcus vestitus
-
mutant C199/C226S, relative activity 6.6%
additional information
protochlorophyllide
Thermosynechococcus vestitus
-
mutant C199S, relative activity 98.2%
additional information
protochlorophyllide
Thermosynechococcus vestitus
-
mutant C226S, relative activity 7.2%
additional information
protochlorophyllide
Thermosynechococcus vestitus
-
mutant C37S, relative activity 99.4%
additional information
protochlorophyllide
Thermosynechococcus vestitus
-
mutant C37S/C199S, relative activity 98.8%
additional information
protochlorophyllide
Thermosynechococcus vestitus
-
mutant C37S/C199S/C226S, relative activity 7.1%
additional information
protochlorophyllide
Thermosynechococcus vestitus
-
mutant C37S/C226S, relative activity 6.8%
additional information
protochlorophyllide
Thermosynechococcus vestitus
-
mutant K197A, relative activity 2.7%
additional information
protochlorophyllide
Thermosynechococcus vestitus
-
mutant K197Q, relative activity 2.0%
additional information
protochlorophyllide
Thermosynechococcus vestitus
-
mutant K197R, relative activity 2.3%
additional information
protochlorophyllide
Thermosynechococcus vestitus
-
mutant Y193A, relative activity 5.5%
additional information
protochlorophyllide
Thermosynechococcus vestitus
-
mutant Y193F, relative activity 19.5%
additional information
protochlorophyllide
Thermosynechococcus vestitus
-
mutant Y193S, relative activity 2.4%
additional information
protochlorophyllide
Thermosynechococcus vestitus
-
wild type enzyme, relative activity 100%
additional information
protochlorophyllide
Thermosynechococcus vestitus
-
wild type enzyme, relative activity 100%
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.003 - 0.17
protochlorophyllide
0.011
NADPH
Thermosynechococcus vestitus
-
pH 7.5, 25°C, mutant C199S/C226S, co-substrate: protochlorophyllide
0.0113
NADPH
Thermosynechococcus vestitus
-
pH 7.5, 25°C, mutant C37S/C226S, co-substrate: protochlorophyllide
0.0117
NADPH
Thermosynechococcus vestitus
-
pH 7.5, 25°C, mutant C37S/C199S/C226S, co-substrate: protochlorophyllide
0.0118
NADPH
Thermosynechococcus vestitus
-
pH 7.5, 25°C, mutant C226S, co-substrate: protochlorophyllide
0.017
NADPH
-
pH and temperature not specified in the publication
0.019
NADPH
-
pH and temperature not specified in the publication
0.019
NADPH
-
pH and temperature not specified in the publication
0.02
NADPH
-
pH and temperature not specified in the publication
0.026
NADPH
-
pH and temperature not specified in the publication
0.035
NADPH
-
pH and temperature not specified in the publication
0.042
NADPH
-
pH and temperature not specified in the publication
0.043
NADPH
-
pH and temperature not specified in the publication
0.058
NADPH
-
pH and temperature not specified in the publication
0.102
NADPH
-
pH and temperature not specified in the publication
0.162
NADPH
Thermosynechococcus vestitus
-
pH 7.5, 25°C, mutant C199S, co-substrate: protochlorophyllide
0.164
NADPH
Thermosynechococcus vestitus
-
pH 7.5, 25°C, mutant C37S, co-substrate: protochlorophyllide
0.165
NADPH
Thermosynechococcus vestitus
-
pH 7.5, 25°C, wild-type, co-substrate: protochlorophyllide
0.003
protochlorophyllide
Thermosynechococcus vestitus
-
mutant K197Q
0.004
protochlorophyllide
Thermosynechococcus vestitus
-
mutant K197A
0.004
protochlorophyllide
Thermosynechococcus vestitus
-
mutant K197R
0.004
protochlorophyllide
Thermosynechococcus vestitus
-
mutant Y193S
0.007
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme F233L
0.009
protochlorophyllide
Thermosynechococcus vestitus
-
mutant Y193A
0.01
protochlorophyllide
Thermosynechococcus vestitus
mutant enzyme N149V, at 25°C, pH not specified in the publication
0.01
protochlorophyllide
Thermosynechococcus vestitus
mutant enzyme T145A, at 25°C, pH not specified in the publication
0.01
protochlorophyllide
Thermosynechococcus vestitus
mutant enzyme T147F, at 25°C, pH not specified in the publication
0.01
protochlorophyllide
Thermosynechococcus vestitus
mutant enzyme T230F, at 25°C, pH not specified in the publication
0.011
protochlorophyllide
Thermosynechococcus vestitus
-
mutant C199/C226S
0.011
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 25°C, mutant C199S/C226S, co-substrate: NADPH
0.0113
protochlorophyllide
Thermosynechococcus vestitus
-
mutant C37S/C226S
0.0113
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 25°C, mutant C37S/C226S, co-substrate: NADPH
0.0117
protochlorophyllide
Thermosynechococcus vestitus
-
mutant C37S/C199S/C226S
0.0117
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 25°C, mutant C37S/C199S/C226S, co-substrate: NADPH
0.0118
protochlorophyllide
Thermosynechococcus vestitus
-
mutant C226S
0.0118
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 25°C, mutant C226S, co-substrate: NADPH
0.013
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme F233Y
0.013
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme P158F
0.02
protochlorophyllide
Thermosynechococcus vestitus
mutant enzyme N39V, at 25°C, pH not specified in the publication
0.02
protochlorophyllide
Thermosynechococcus vestitus
mutant enzyme T147S, at 25°C, pH not specified in the publication
0.022
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme K156N/I157V
0.027
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 40°C, wild-type enzyme
0.03
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme F237Y
0.032
protochlorophyllide
Thermosynechococcus vestitus
-
mutant Y193F
0.035
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme K156N
0.037
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme I157V
0.037
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 40°C, mutant enzyme P158A
0.07
protochlorophyllide
Thermosynechococcus vestitus
mutant enzyme N90A, at 25°C, pH not specified in the publication
0.1
protochlorophyllide
Thermosynechococcus vestitus
mutant enzyme H236A, at 25°C, pH not specified in the publication
0.16
protochlorophyllide
Thermosynechococcus vestitus
mutant enzyme G19A, at 25°C, pH not specified in the publication
0.16
protochlorophyllide
Thermosynechococcus vestitus
mutant enzyme K42A, at 25°C, pH not specified in the publication
0.16
protochlorophyllide
Thermosynechococcus vestitus
mutant enzyme R38V, at 25°C, pH not specified in the publication
0.16
protochlorophyllide
Thermosynechococcus vestitus
mutant enzyme S16C, at 25°C, pH not specified in the publication
0.16
protochlorophyllide
Thermosynechococcus vestitus
mutant enzyme S189A, at 25°C, pH not specified in the publication
0.16
protochlorophyllide
Thermosynechococcus vestitus
mutant enzyme T230A, at 25°C, pH not specified in the publication
0.16
protochlorophyllide
Thermosynechococcus vestitus
mutant enzyme T230S, at 25°C, pH not specified in the publication
0.162
protochlorophyllide
Thermosynechococcus vestitus
-
mutant C199S
0.162
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 25°C, mutant C199S, co-substrate: NADPH
0.163
protochlorophyllide
Thermosynechococcus vestitus
-
mutant C37S/C199S
0.164
protochlorophyllide
Thermosynechococcus vestitus
-
wild type enzyme
0.164
protochlorophyllide
Thermosynechococcus vestitus
-
mutant C37S
0.164
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 25°C, mutant C37S, co-substrate: NADPH
0.165
protochlorophyllide
Thermosynechococcus vestitus
-
wild type enzyme
0.165
protochlorophyllide
Thermosynechococcus vestitus
-
pH 7.5, 25°C, wild-type, co-substrate: NADPH
0.17
protochlorophyllide
Thermosynechococcus vestitus
wild type enzyme, at 25°C, pH not specified in the publication
0.17
protochlorophyllide
Thermosynechococcus vestitus
mutant enzyme Y94F, at 25°C, pH not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
translocon constituent toc33 is indispensable for the import of isoform PorB
brenda
low expression, light-response during greening, expression in mature cells
brenda
-
brenda
-
-
brenda
high expression in dark-grown cells, no light response during greening. Constitutive enzym, expression in mature cells
brenda
high expression in dark-grown cells, no light response during greening. Very low expression in mature cells
brenda
high expression in, no light-response during greening
brenda
-
high expression in, no light-response during greening
brenda
-
brenda
high expression in, constitutive enzyme
brenda
very high expression in, no light-response during greening, undetectable in mature cells
brenda
high expression in, light-response during greening, expression in mature cells
brenda
medium expression in, light-response during greening, expression in mature cells
brenda
high expression in dark-grown cell, constitutive enzyme
brenda
high expression in dark-grown cell, no light-response during greening
brenda
-
high expression in dark-grown cell, light-resonse during greening
brenda
high expression in, no light-response during greening
brenda
high expression in, constitutive enzyme
brenda
undetectable in dark-grown cells, light response during greening. Expression in mature cells
brenda
undetectable in dark-grown cell, light-response during greening
brenda
LPOR-A is present in etiolated tissue. LPOR-A is expressed during early phases of development when large amounts of pigments need to be synthesized quickly, while LPOR-B and LPOR-C are responsible for the bulk chlorophyll synthesis of adult or green plants
brenda
LPOR-B is present in etiolated tissue. LPOR-A is expressed during early phases of development when large amounts of pigments need to be synthesized quickly, while LPOR-B and LPOR-C are responsible for the bulk chlorophyll synthesis of adult or green plants
brenda
-
-
brenda
-
translocon constituent toc33 is indispensable for the import of isoform PorB
brenda
-
-
brenda
-
-
393832, 393833, 393836, 393839, 393841, 393842, 393843, 393844, 393855, 393857, 657112, 689396 brenda
-
-
brenda
-
isoform POR1 and POR2 are active
brenda
-
-
brenda
expressed at high levels in developing leaves, expression decreases dramatically in fully mature leaves
brenda
expression is relatively constant throughout leaf development
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
dark-grown
brenda
-
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
brenda
-
-
brenda
-
brenda
-
brenda
-
brenda
-
-
brenda
-
strong expression of enzyme isoforms PorA, PorB in early seedling development
brenda
-
-
brenda
-
-
393841, 393843, 393844, 393848, 393851, 393853, 393855, 393858, 393859, 393865, 657112 brenda
-
-
brenda
-
POR1 is active in dark-grown seedlings
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
-
-
brenda
additional information
LPOR-C is expressed typically in green tissues
brenda
additional information
LPOR-C is expressed typically in green tissues
brenda
additional information
LPOR-C is expressed typically in green tissues
brenda
additional information
isoenzyme LPOR-A is present in etiolated tissue
brenda
additional information
isoenzyme LPOR-A is present in etiolated tissue
brenda
additional information
LPOR-B is responsible for the bulk chlorophyll synthesis of adult or green plants
brenda
additional information
LPOR-B is responsible for the bulk chlorophyll synthesis of adult or green plants
brenda
additional information
-
isoenzymes LPOR-A and LPOR-B are present in etiolated material, while LPOR-C is expressed typically in green tissues
brenda
additional information
-
photosynthetic active tissue
brenda
additional information
isoenzymes LPOR-A and LPOR-B are present in etiolated material, while LPOR-C is expressed typically in green tissues
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
all modern sequences of light-dependent protochlorophyllide oxidoreductase POR diverged from a single sequence about 1.36 billlion years ago. The LPOR gene was then duplicated at least 10 times in angiosperms, leading to the formation of two or even more LPOR isoforms in multiple species. In the case of Arabidopsis thaliana, isoforms PORA and PORB originated in one duplication event, in contrary to the isoform PORC, which diverged first
evolution
DPOR (EC 1.3.7.7) and LPOR (EC 1.3.1.33) initially evolved in the ancestral prokaryotic genome perhaps at different times. DPOR originated in the anoxygenic environment of the Earth from nitrogenase-like enzyme of methanogenic archaea. Due to the transition from anoxygenic to oxygenic photosynthesis in the prokaryote, the DPOR was mostly inactivated in the daytime by photosynthetic O2 leading to the evolution of oxygen-insensitive LPOR that could function in the light. The primary endosymbiotic event transferred the DPOR and LPOR genes to the eukaryotic phototroph, the DPOR remained in the genome of the ancestor that turned into the plastid, whereas LPOR was transferred to the host nuclear genome. Despite the evolution of its nonhomologous isofunctional counterpart LPOR, the DPOR continues to be functional in both oxygenic and anoxygenic photosynthetic organisms. Thus, DPOR was not exactly replaced but supplemented with the LPOR. Limnohabitans sp. strain 15K has acquired LPOR through horizontal gene transfer
evolution
DPOR (EC 1.3.7.7) and LPOR (EC 1.3.1.33) initially evolved in the ancestral prokaryotic genome perhaps at different times. DPOR originated in the anoxygenic environment of the Earth from nitrogenase-like enzyme of methanogenic archaea. Due to the transition from anoxygenic to oxygenic photosynthesis in the prokaryote, the DPOR was mostly inactivated in the daytime by photosynthetic O2 leading to the evolution of oxygen-insensitive LPOR that could function in the light. The primary endosymbiotic event transferred the DPOR and LPOR genes to the eukaryotic phototroph, the DPOR remained in the genome of the ancestor that turned into the plastid, whereas LPOR was transferred to the host nuclear genome. Despite the evolution of its nonhomologous isofunctional counterpart LPOR, the DPOR continues to be functional in both oxygenic and anoxygenic photosynthetic organisms. Thus, DPOR was not exactly replaced but supplemented with the LPOR. LPOR protein phylogeny further corroborates the horizontal gene transfer from cyanobacteria
evolution
DPOR (EC 1.3.7.7) and LPOR (EC 1.3.1.33) initially evolved in the ancestral prokaryotic genome perhaps at different times. DPOR originated in the anoxygenic environment of the Earth from nitrogenase-like enzyme of methanogenic archaea. Due to the transition from anoxygenic to oxygenic photosynthesis in the prokaryote, the DPOR was mostly inactivated in the daytime by photosynthetic O2 leading to the evolution of oxygen-insensitive LPOR that could function in the light. The primary endosymbiotic event transferred the DPOR and LPOR genes to the eukaryotic phototroph, the DPOR remained in the genome of the ancestor that turned into the plastid, whereas LPOR was transferred to the host nuclear genome. Despite the evolution of its nonhomologous isofunctional counterpart LPOR, the DPOR continues to be functional in both oxygenic and anoxygenic photosynthetic organisms. Thus, DPOR was not exactly replaced but supplemented with the LPOR. LPOR protein phylogeny further corroborates the horizontal gene transfer from cyanobacteria
evolution
DPOR (EC 1.3.7.7) and LPOR (EC 1.3.1.33) initially evolved in the ancestral prokaryotic genome perhaps at different times. DPOR originated in the anoxygenic environment of the Earth from nitrogenase-like enzyme of methanogenic archaea. Due to the transition from anoxygenic to oxygenic photosynthesis in the prokaryote, the DPOR was mostly inactivated in the daytime by photosynthetic O2 leading to the evolution of oxygen-insensitive LPOR that could function in the light. The primary endosymbiotic event transferred the DPOR and LPOR genes to the eukaryotic phototroph, the DPOR remained in the genome of the ancestor that turned into the plastid, whereas LPOR was transferred to the host nuclear genome. Despite the evolution of its nonhomologous isofunctional counterpart LPOR, the DPOR continues to be functional in both oxygenic and anoxygenic photosynthetic organisms. Thus, DPOR was not exactly replaced but supplemented with the LPOR. LPOR protein phylogeny further corroborates the horizontal gene transfer from cyanobacteria
evolution
-
oxygen-sensitive dark-operative NADPH:Pchlide oxidoreductase enzyme (DPOR) and light-dependent NADPH:protochlorophyllide oxidoreductase (LPOR) show very low sequence homology. In most organisms they occur simultaneously. However, angiosperms lack LPOR and became unable to synthesize chlorophyllides and chlorophylls (Chls) in the absence of light
evolution
oxygen-sensitive dark-operative NADPH:Pchlide oxidoreductase enzyme (DPOR) and light-dependent NADPH:protochlorophyllide oxidoreductase (LPOR) show very low sequence homology. In most organisms they occur simultaneously. However, angiosperms lack LPOR and became unable to synthesize chlorophyllides and chlorophylls (Chls) in the absence of light
evolution
-
DPOR (EC 1.3.7.7) and LPOR (EC 1.3.1.33) initially evolved in the ancestral prokaryotic genome perhaps at different times. DPOR originated in the anoxygenic environment of the Earth from nitrogenase-like enzyme of methanogenic archaea. Due to the transition from anoxygenic to oxygenic photosynthesis in the prokaryote, the DPOR was mostly inactivated in the daytime by photosynthetic O2 leading to the evolution of oxygen-insensitive LPOR that could function in the light. The primary endosymbiotic event transferred the DPOR and LPOR genes to the eukaryotic phototroph, the DPOR remained in the genome of the ancestor that turned into the plastid, whereas LPOR was transferred to the host nuclear genome. Despite the evolution of its nonhomologous isofunctional counterpart LPOR, the DPOR continues to be functional in both oxygenic and anoxygenic photosynthetic organisms. Thus, DPOR was not exactly replaced but supplemented with the LPOR. LPOR protein phylogeny further corroborates the horizontal gene transfer from cyanobacteria
-
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
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
-
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
-
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
-
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
malfunction
-
an enzyme-less mutant grows photoautotrophically in moderate light and contains a maximum of 20% of the wild type chlorophyll level
malfunction
-
RNAi based simultaneous silencing of all forms of light-dependent NADPH:protochlorophyllide oxidoreductase genes results in the accumulation of protochlorophyllide in tobacco
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
metabolism
-
the enzyme allows for the rapid formation of chlorophyll after illumination while avoiding photodamage. The formation of protochlorophyllide-enzyme(LPOR) complexes is an initial step of etioplast development. the formation of pigment-LPOR complexes in prolamellar bodies is essential for the rapid and safe conversion of etioplasts to chloroplasts during the dark-to-light transition
metabolism
the nonhomologous enzymes, the light-independent protochlorophyllide reductase (DPOR, EC 1.3.7.7) and the light-dependent protochlorophyllide oxidoreductase (LPOR), catalyze the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) in the penultimate step of biosynthesis of chlorophyll (Chl) required for photosynthetic light absorption and energy conversion. The two enzymes differ with respect to the requirement of light for catalysis and oxygen sensitivity. Stereospecific reduction of the D ring of Pchlide (protochlorophyllide) to Chlide (chlorophyllide) catalyzed by light-independent protochlorophyllide a reductase (DPOR) occurs in anoxygenic phototrophs and photosynthetic eukaryotes except most gnetophytes and all angiosperms. The reduction of the D ring Pchlide to Chlide is brought about by light-dependent protochlorophyllide oxidoreductase (LPOR) in light in oxygenic phototrophs. The reduction of Chlide a to Bchlide a in anoxygenic phototrophs is catalyzed by the stereospecific reduction of ring B by chlorophyllide a oxidoreductase (COR, EC 1.3.7.15). Both MV Pchlide and DV Pchlide are phototransformed to MV Chlide a and DV Chlide a, respectively, by light-dependent Pchlide oxidoreductase (LPOR) in oxygenic phototrophs. In the absence of light, anoxygenic photosynthetic bacteria and oxygen evolving phototrophs catalyze Pchlide reduction by the light-independent Pchlide oxidoreductase (DPOR). The DV Chlide a is immediately converted to MV Chlide a by DV reductase
metabolism
the nonhomologous enzymes, the light-independent protochlorophyllide reductase (DPOR, EC 1.3.7.7) and the light-dependent protochlorophyllide oxidoreductase (LPOR), catalyze the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) in the penultimate step of biosynthesis of chlorophyll (Chl) required for photosynthetic light absorption and energy conversion. The two enzymes differ with respect to the requirement of light for catalysis and oxygen sensitivity. Stereospecific reduction of the D ring of Pchlide (protochlorophyllide) to Chlide (chlorophyllide) catalyzed by light-independent protochlorophyllide a reductase (DPOR) occurs in anoxygenic phototrophs and photosynthetic eukaryotes except most gnetophytes and all angiosperms. The reduction of the D ring Pchlide to Chlide is brought about by light-dependent protochlorophyllide oxidoreductase (LPOR) in light in oxygenic phototrophs. The reduction of Chlide a to Bchlide a in anoxygenic phototrophs is catalyzed by the stereospecific reduction of ring B by chlorophyllide a oxidoreductase (COR, EC 1.3.7.15). Both MV Pchlide and DV Pchlide are phototransformed to MV Chlide a and DV Chlide a, respectively, by light-dependent Pchlide oxidoreductase (LPOR) in oxygenic phototrophs. In the absence of light, anoxygenic photosynthetic bacteria and oxygen evolving phototrophs catalyze Pchlide reduction by the light-independent Pchlide oxidoreductase (DPOR). The DV Chlide a is immediately converted to MV Chlide a by DV reductase
metabolism
the nonhomologous enzymes, the light-independent protochlorophyllide reductase (DPOR, EC 1.3.7.7) and the light-dependent protochlorophyllide oxidoreductase (LPOR), catalyze the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) in the penultimate step of biosynthesis of chlorophyll (Chl) required for photosynthetic light absorption and energy conversion. The two enzymes differ with respect to the requirement of light for catalysis and oxygen sensitivity. Stereospecific reduction of the D ring of Pchlide (protochlorophyllide) to Chlide (chlorophyllide) catalyzed by light-independent protochlorophyllide a reductase (DPOR) occurs in anoxygenic phototrophs and photosynthetic eukaryotes except most gnetophytes and all angiosperms. The reduction of the D ring Pchlide to Chlide is brought about by light-dependent protochlorophyllide oxidoreductase (LPOR) in light in oxygenic phototrophs. The reduction of Chlide a to Bchlide a in anoxygenic phototrophs is catalyzed by the stereospecific reduction of ring B by chlorophyllide a oxidoreductase (COR, EC 1.3.7.15). Both MV Pchlide and DV Pchlide are phototransformed to MV Chlide a and DV Chlide a, respectively, by light-dependent Pchlide oxidoreductase (LPOR) in oxygenic phototrophs. In the absence of light, anoxygenic photosynthetic bacteria and oxygen evolving phototrophs catalyze Pchlide reduction by the light-independent Pchlide oxidoreductase (DPOR). The DV Chlide a is immediately converted to MV Chlide a by DV reductase
metabolism
the nonhomologous enzymes, the light-independent protochlorophyllide reductase (DPOR, EC 1.3.7.7) and the light-dependent protochlorophyllide oxidoreductase (LPOR), catalyze the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) in the penultimate step of biosynthesis of chlorophyll (Chl) required for photosynthetic light absorption and energy conversion. The two enzymes differ with respect to the requirement of light for catalysis and oxygen sensitivity. Stereospecific reduction of the D ring of Pchlide (protochlorophyllide) to Chlide (chlorophyllide) catalyzed by light-independent protochlorophyllide a reductase (DPOR) occurs in anoxygenic phototrophs and photosynthetic eukaryotes except most gnetophytes and all angiosperms. The reduction of the D ring Pchlide to Chlide is brought about by light-dependent protochlorophyllide oxidoreductase (LPOR) in light in oxygenic phototrophs. The reduction of Chlide a to Bchlide a in anoxygenic phototrophs is catalyzed by the stereospecific reduction of ring B by chlorophyllide a oxidoreductase (COR, EC 1.3.7.15). Both MV Pchlide and DV Pchlide are phototransformed to MV Chlide a and DV Chlide a, respectively, by lightdependent Pchlide oxidoreductase (LPOR) in oxygenic phototrophs. In the absence of light, anoxygenic photosynthetic bacteria and oxygen evolving phototrophs catalyze Pchlide reduction by the light-independent Pchlide oxidoreductase (DPOR). The DV Chlide a is immediately converted to MV Chlide a by DV reductase
metabolism
-
the nonhomologous enzymes, the light-independent protochlorophyllide reductase (DPOR, EC 1.3.7.7) and the light-dependent protochlorophyllide oxidoreductase (LPOR), catalyze the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) in the penultimate step of biosynthesis of chlorophyll (Chl) required for photosynthetic light absorption and energy conversion. The two enzymes differ with respect to the requirement of light for catalysis and oxygen sensitivity. Stereospecific reduction of the D ring of Pchlide (protochlorophyllide) to Chlide (chlorophyllide) catalyzed by light-independent protochlorophyllide a reductase (DPOR) occurs in anoxygenic phototrophs and photosynthetic eukaryotes except most gnetophytes and all angiosperms. The reduction of the D ring Pchlide to Chlide is brought about by light-dependent protochlorophyllide oxidoreductase (LPOR) in light in oxygenic phototrophs. The reduction of Chlide a to Bchlide a in anoxygenic phototrophs is catalyzed by the stereospecific reduction of ring B by chlorophyllide a oxidoreductase (COR, EC 1.3.7.15). Both MV Pchlide and DV Pchlide are phototransformed to MV Chlide a and DV Chlide a, respectively, by light-dependent Pchlide oxidoreductase (LPOR) in oxygenic phototrophs. In the absence of light, anoxygenic photosynthetic bacteria and oxygen evolving phototrophs catalyze Pchlide reduction by the light-independent Pchlide oxidoreductase (DPOR). The DV Chlide a is immediately converted to MV Chlide a by DV reductase
-
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
-
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
physiological function
-
OsPORB is essential for maintaining light-dependent chlorophyll synthesis throughout leaf development, especially under high-light conditions
physiological function
-
isoform POR1 supports photoacclimation, whereas isoform POR2 is responsible for daily chlorophyll synthesis
physiological function
-
the enzyme is essential for chlorophyll synthesis
physiological function
in leaf of etiolated seedlings, prolamellar bodies are smaller in the etioplasts of mutant plants than in the wild type. In field-grown seedlings, the chloroplasts in the light-green sectors of mutant leaves exhibit decreased thylakoid stacking with a few plastglobules. PorB is essential for both prolamellar bodies and photoactive protochlorophyllide formation in dark conditions for light-dependent chlorophyll synthesis
physiological function
low levels of isoform PorA are sufficient for leaf greening in rice, even in the absence of isoform PorB activity
physiological function
key enzyme of chlorophyll biosynthesis in angiosperms. Photoenzyme, which catalyzes the light-activated trans-reduction of the C17-C18 double bond of the porphyrin ring of protochlorophyllides. Due to the light requirement, dark-grown angiosperms cannot synthesize chlorophyll
physiological function
light-dependent protochlorophyllide oxidoreductase (LPOR) is a rate-limiting key chlorophyll biosynthetic enzyme
physiological function
Thermosynechococcus vestitus
-
light-dependent reaction of chlorophyll biosynthesis. The enzyme (POR) is also important in plant development as it is the main constituent of prolamellar bodies in etioplast membranes
physiological function
the enzyme (LPOR) exhibits an intrinsic ability to form prolamellar body-like ultrastructures in the presence of the co-accumulation of protochlorophyllide. However, the prolamellar body-like structure differs from the authentic prolamellar bodies regarding NADPH deficiency
physiological function
the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) a is of crucial importance in the chlorophyll biosynthetic pathway as this step regulates the synthesis of Chl by feedback control. Pchlide reduction takes place by two nonhomologous enzymes DPOR and LPOR which differ with respect to their requirement of light. LPOR evolved in an independent evolutionary event immediately after the GOE on earth. However, unlike DPOR, LPOR uses NADPH as the reductant for the reduction of the double bond of Pchlide in the presence of light and is insensitive to oxygen attack. Due to the functional convergence, the two Pchlide reducing enzymes may be referred as nonhomologous isofunctional enzymes, mechanism of reduction of Pchlide to Chlide in the absence or presence of light by DPOR or LPOR
physiological function
the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) a is of crucial importance in the chlorophyll biosynthetic pathway as this step regulates the synthesis of Chl by feedback control. Pchlide reduction takes place by two nonhomologous enzymes DPOR and LPOR which differ with respect to their requirement of light. LPOR evolved in an independent evolutionary event immediately after the GOE on earth. However, unlike DPOR, LPOR uses NADPH as the reductant for the reduction of the double bond of Pchlide in the presence of light and is insensitive to oxygen attack. Due to the functional convergence, the two Pchlide reducing enzymes may be referred as nonhomologous isofunctional enzymes, mechanism of reduction of Pchlide to Chlide in the absence or presence of light by DPOR or LPOR
physiological function
the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) a is of crucial importance in the chlorophyll biosynthetic pathway as this step regulates the synthesis of Chl by feedback control. Pchlide reduction takes place by two nonhomologous enzymes DPOR and LPOR which differ with respect to their requirement of light. LPOR evolved in an independent evolutionary event immediately after the GOE on earth. However, unlike DPOR, LPOR uses NADPH as the reductant for the reduction of the double bond of Pchlide in the presence of light and is insensitive to oxygen attack. Due to the functional convergence, the two Pchlide reducing enzymes may be referred as nonhomologous isofunctional enzymes, mechanism of reduction of Pchlide to Chlide in the absence or presence of light by DPOR or LPOR
physiological function
the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) a is of crucial importance in the chlorophyll biosynthetic pathway as this step regulates the synthesis of Chl by feedback control. Pchlide reduction takes place by two nonhomologous enzymes DPOR and LPOR which differ with respect to their requirement of light. LPOR evolved in an independent evolutionary event immediately after the GOE on earth. However, unlike DPOR, LPOR uses NADPH as the reductant for the reduction of the double bond of Pchlide in the presence of light and is insensitive to oxygen attack. Due to the functional convergence, the two Pchlide reducing enzymes may be referred as nonhomologous isofunctional enzymes, mechanism of reduction of Pchlide to Chlide in the absence or presence of light by DPOR or LPOR
physiological function
-
the reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) a is of crucial importance in the chlorophyll biosynthetic pathway as this step regulates the synthesis of Chl by feedback control. Pchlide reduction takes place by two nonhomologous enzymes DPOR and LPOR which differ with respect to their requirement of light. LPOR evolved in an independent evolutionary event immediately after the GOE on earth. However, unlike DPOR, LPOR uses NADPH as the reductant for the reduction of the double bond of Pchlide in the presence of light and is insensitive to oxygen attack. Due to the functional convergence, the two Pchlide reducing enzymes may be referred as nonhomologous isofunctional enzymes, mechanism of reduction of Pchlide to Chlide in the absence or presence of light by DPOR or LPOR
-
physiological function
-
light-dependent protochlorophyllide oxidoreductase (LPOR) is a rate-limiting key chlorophyll biosynthetic enzyme
-
physiological function
-
the enzyme (LPOR) exhibits an intrinsic ability to form prolamellar body-like ultrastructures in the presence of the co-accumulation of protochlorophyllide. However, the prolamellar body-like structure differs from the authentic prolamellar bodies regarding NADPH deficiency
-
additional information
a clear distinction of the DPOR and LPOR functions cannot be made as oxygen-sensitive DPOR, which is typically inactivated in the increased oxygen concentration, remains functional in Dinoroseobacter shibae. The TFT motif fragment from LPOR and BchL/ChlL is found to be absent from other SDR proteins and has no similarity with the Fe protein of nitrogenase NifH. The TFT motif is previously found to be present between the NAA motif,which is one of the NADPH binding sites, and the catalytic YxxxK motif. The mutation of conserved residues in TFT motif results in complete inhibition of the LPOR activity
additional information
the TFT motif fragment from LPOR and BchL/ChlL is found to be absent from other SDR proteins and has no similarity with the Fe protein of nitrogenase NifH. The TFT motif is previously found to be present between the NAA motif, which is one of the NADPH binding sites, and the catalytic YxxxK motif. The mutation of conserved residues in TFT motif results in complete inhibition of the LPOR activity
additional information
the TFT motif fragment from LPOR and BchL/ChlL is found to be absent from other SDR proteins and has no similarity with the Fe protein of nitrogenase NifH. The TFT motif is previously found to be present between the NAA motif,which is one of the NADPH binding sites, and the catalytic YxxxK motif. The mutation of conserved residues in TFT motif results in complete inhibition of the LPOR activity
additional information
the TFT motif fragment from LPOR and BchL/ChlL is found to be absent from other SDR proteins and has no similarity with the Fe protein of nitrogenase NifH. The TFT motif is previously found to be present between the NAA motif,which is one of the NADPH binding sites, and the catalytic YxxxK motif. The mutation of conserved residues in TFT motif results in complete inhibition of the LPOR activity
additional information
-
a clear distinction of the DPOR and LPOR functions cannot be made as oxygen-sensitive DPOR, which is typically inactivated in the increased oxygen concentration, remains functional in Dinoroseobacter shibae. The TFT motif fragment from LPOR and BchL/ChlL is found to be absent from other SDR proteins and has no similarity with the Fe protein of nitrogenase NifH. The TFT motif is previously found to be present between the NAA motif,which is one of the NADPH binding sites, and the catalytic YxxxK motif. The mutation of conserved residues in TFT motif results in complete inhibition of the LPOR activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
112000
-
substrate-enzyme complex, gel filtration
210000
-
purified ChlNB complex, gel filtration
32395
-
2 * 32395, purified ChlL subunit, deduced from amino acid sequence
36046
-
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
37800
-
amino acid composition
40000
-
determined by SDS-PAGE
40150
x * 40150, recombinant enzyme, SDS-PAGE
41000
-
identified with monospecific polyclonal antibody
41200
-
predicted from cDNA
42000
-
determined by SDS-PAGE
45000
-
2 * 45000, SDS-PAGE
46000
-
x * 46000, precursor protein, x * 38000, mature protein
46199
-
2 * 46199 + 2 * 58729, purified ChlNB complex, deduced from amino acid sequence
48671
-
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
52000
-
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
57191
-
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
58729
-
2 * 46199 + 2 * 58729, purified ChlNB complex, deduced from amino acid sequence
78800
-
recombinant fusion protein, gel filtration
34000
-
-
34000
-
2 related peptides of 34000/36000
34000
-
2 related peptides of 34000/35000
35000
-
-
35000
-
2 related peptides of 34000/35000
35000
-
SDS-PAGE shows 2 closely related peptides of 35000 and 37000
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
36000
-
-
36000
-
2 related peptides of 36000/38000
36000
-
predicted from amino acid composition
36000
-
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
37000
-
-
37000
-
gel filtration, doublet of 2 peptides of 35000 and 37000 co-purified
37000
-
covalent radioactive labelling technique
37000
-
x * 37000, SDS-PAGE
38000
-
-
38000
-
x * 46000, precursor protein, x * 38000, mature protein
44000
-
-
44000
-
precursor polypeptide, predicted from mRNA
60000
-
purified ChlL subunit, gel filtration
60000
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
heterotetramer
-
2 * 46199 + 2 * 58729, purified ChlNB complex, deduced from amino acid sequence
homodimer
-
2 * 32395, purified ChlL subunit, deduced from amino acid sequence
octamer
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
additional information
-
recombinant enzyme component L-protein forms a dimer, recombinant components NB-protein form a heterotetramer, gel filtration
?
-
x * 37000, SDS-PAGE
?
x * 40150, recombinant enzyme, SDS-PAGE
?
-
x * 46000, precursor protein, x * 38000, mature protein
?
-
x * 42500, isoform POR1, SDS-PAGE
?
-
x * 44000, isoform POR2, SDS-PAGE
?
-
x * 47000, isoform POR1, calculated from amino acid sequence
?
-
x * 61000, isoform POR2, calculated from amino acid sequence
?
-
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
dimer
-
POR proteins in Arabidopsis consist of dimers
dimer
-
2 * 45000, SDS-PAGE
dimer
-
recombinant fusion protein, gel filtration
dimer
dimerization and binding of ligands (both the cofactor NADPH and substrate protochlorophyllide) are computationally investigated the sequence and structural relationships among homologous proteins are identified through database searches. The results indicate that alpha4 and alpha7 helices of monomers form the interface of NADPH:protochlorophyllide oxidoreductase dimers. On the basis of conserved residues, 11 functionally important amino acids that play important roles in binding of the enzyme to NADPH are predicted
dimer
Thermosynechococcus vestitus
-
monomer
-
1 * 36000, SDS-PAGE
monomer
-
1 * 36000, SDS-PAGE
monomer
the structure of enzyme (POR) protein is predicted in its monomeric and dimeric form
oligomer
-
oligomeric PORA-PORB complex
oligomer
-
barley PORA can form a five-unit oligomer that interacts with a single PORB
oligomer
Thermosynechococcus vestitus
-
protochlorophyllide binding triggers formation of large oligomers of the enzyme (POR). Oligomer formation is most likely driven by the interaction of amino acid residues in the highly conserved lid regions. The lid residues position protochlorophyllide optimally to enable photocatalysis. Following protochlorophyllide binding, they also enable POR oligomerisation - a process that is reversed through subsequent photocatalysis in the early stages of chloroplast development
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
C276A
-
the mutant is hypersensitive to high-light conditions during greening
Cys303A
-
the mutant is hypersensitive to high-light conditions during greening
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
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
Thermosynechococcus vestitus
-
mutant, mutation of the absolutely conserved cysteine residues
C199S/C226S
Thermosynechococcus vestitus
-
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
F233L
Thermosynechococcus vestitus
-
mutant enzyme shows around 40% of wild-type activity
F233Y
Thermosynechococcus vestitus
-
mutant enzyme shows around 40% of wild-type activity
F237Y
Thermosynechococcus vestitus
-
as in the wild-type enzyme the visible spectrum of protochlorophyllide bound to the mutant enzyme is red-shifted by about 12 nm compared to free protochlorophyllide
F240Y
Thermosynechococcus vestitus
-
distinct from the wild-type enzyme the visible spectrum of protochlorophyllide bound to the mutant enzyme is not red-shifted as compared to free protochlorophyllide
F244Y
Thermosynechococcus vestitus
-
distinct from the wild-type enzyme the visible spectrum of protochlorophyllide bound to the mutant enzyme is not red-shifted as compared to free protochlorophyllide
F247Y
Thermosynechococcus vestitus
-
distinct from the wild-type enzyme the visible spectrum of protochlorophyllide bound to the mutant enzyme is not red-shifted as compared to free protochlorophyllide
G19A
Thermosynechococcus vestitus
the mutant shows wild type value for turnover number
H236A
Thermosynechococcus vestitus
the mutant shows reduced value for turnover number compared to the wild type enzyme
K197A
Thermosynechococcus vestitus
-
mutant, constructed for analysing the role of the conserved active site lysine
K197Q
Thermosynechococcus vestitus
-
mutant, constructed for analysing the role of the conserved active site lysine
K197R
Thermosynechococcus vestitus
-
mutant, constructed for analysing the role of the conserved active site lysine
K42A
Thermosynechococcus vestitus
the mutant shows wild type value for turnover number
N149V
Thermosynechococcus vestitus
the mutant shows reduced value for turnover number compared to the wild type enzyme
N39V
Thermosynechococcus vestitus
the mutant shows reduced value for turnover number compared to the wild type enzyme
N90A
Thermosynechococcus vestitus
the mutant shows reduced value for turnover number compared to the wild type enzyme
R38V
Thermosynechococcus vestitus
the mutant shows wild type value for turnover number
S16C
Thermosynechococcus vestitus
the mutant shows wild type value for turnover number
S189A
Thermosynechococcus vestitus
the mutant shows wild type value for turnover number
T145A
Thermosynechococcus vestitus
the mutant shows reduced value for turnover number compared to the wild type enzyme
T147F
Thermosynechococcus vestitus
the mutant shows reduced value for turnover number compared to the wild type enzyme
T147S
Thermosynechococcus vestitus
the mutant shows reduced value for turnover number compared to the wild type enzyme
T230A
Thermosynechococcus vestitus
the mutant shows wild type value for turnover number
T230F
Thermosynechococcus vestitus
the mutant shows reduced value for turnover number compared to the wild type enzyme
T230S
Thermosynechococcus vestitus
the mutant shows wild type value for turnover number
Y193A
Thermosynechococcus vestitus
-
mutant, constructed for analysing the role of the conserved active site tyrosine
Y193F
Thermosynechococcus vestitus
-
mutant, constructed for analysing the role of the conserved active site tyrosine
Y193S
Thermosynechococcus vestitus
-
mutant, constructed for analysing the role of the conserved active site tyrosine
Y94F
Thermosynechococcus vestitus
the mutant shows wild type value for turnover number
C199S
Thermosynechococcus vestitus
-
mutant, Cys199 has a relatively minor role in catalysis
C199S
Thermosynechococcus vestitus
-
kcat comparable to wild-type, relative activity comparable to wild-type, Kd (NADPH) comparable to wild-type, Kd (protochlorophyllide) comparable to wild-type
C226S
Thermosynechococcus vestitus
-
mutant, mutation causes a remarkable change in the mechansim of the hydrogen transfer reactions
C226S
Thermosynechococcus vestitus
-
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
C226S
Thermosynechococcus vestitus
the formed protochlorophyllide species in C226S must differ compared to those formed in wild-type enzyme, for example, by attachment of the hydride at C18 rather than C17
C37S
Thermosynechococcus vestitus
-
mutant, Cys37 has a relatively minor role in catalysis
C37S
Thermosynechococcus vestitus
-
kcat comparable to wild-type, relative activity comparable to wild-type, Kd (NADPH) increased compared to wild-type, Kd (protochlorophyllide) equal to wild-type
C37S/C199S
Thermosynechococcus vestitus
-
mutant, mutation of the absolutely conserved cysteine residues
C37S/C199S
Thermosynechococcus vestitus
-
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
C37S/C199S/C226S
Thermosynechococcus vestitus
-
mutant, mutation of the absolutely conserved cysteine residues
C37S/C199S/C226S
Thermosynechococcus vestitus
-
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
C37S/C226S
Thermosynechococcus vestitus
-
mutant, mutation of the absolutely conserved cysteine residues
C37S/C226S
Thermosynechococcus vestitus
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
a genomic library is constructed, the vector pZERO is used
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
-
cDNAs and/or gens encoding POR, also referred to as LPCR or PCR in some studies isolated
-
cloned and overproduced in Escherichia coli with a hexahistidine tag at the N-terminus
-
cloning of the gene encoding protochlorophyllide reductase
-
cloning of the nuclear gene
-
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
Thermosynechococcus vestitus
expressed in Escherichia coli BL21(DE3) Codon Plus RIL cells
-
expressed in Escherichia coli BL21(DE3) pLysS cells
expressed in Escherichia coli strain SG13009
-
expressed in Rhodobacter capsulatus SB1003, JDA, JDB and ZY5
-
expression in Escherichia coli BL21
expression in Escherichia coli cells
expression in Escherichia coli with a Strep-tag
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
-
full-length cDNA, coding for PCR
-
mature pea POR cloned into the pAlter-1 mutagenesis vector, expressed in Escherichia coli JM109
-
optimized and expressed in Escherichia coli
Thermosynechococcus vestitus
overexpressed as a fusion with maltose-binding protein in Escherichia coli using expression plasmid pKK233-2
-
overexpressed in Escherichia coli as a fusion protein with the maltose-binding protein
-
overexpression in Escherichia coli
Thermosynechococcus vestitus
-
overexpression in Escherichia coli as a fusion protein with maltose-binding protein
-
overexpression in Escherichia coli as a His6-tagged protein
POR C cloned and expressed in Escherichia coli
-
subcloned into the expression vector pRSETA and recombinantly expressed in Escherichia coli SoluBL21
Thermosynechococcus vestitus
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
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
Thermosynechococcus vestitus
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) pLysS cells
-
expressed in Escherichia coli BL21(DE3) pLysS cells
-
expressed in Escherichia coli BL21(DE3) pLysS cells
-
expressed in Escherichia coli BL21(DE3) pLysS cells
-
expressed in Escherichia coli BL21(DE3) pLysS cells
-
expressed in Escherichia coli BL21(DE3) pLysS cells
-
expressed in Escherichia coli BL21(DE3) pLysS cells
-
expressed in Escherichia coli BL21(DE3) pLysS cells
-
expressed in Escherichia coli BL21(DE3) pLysS cells
-
expressed in Escherichia coli BL21(DE3) pLysS cells
-
expression in Escherichia coli cells
-
expression in Escherichia coli cells
-
expression in Escherichia coli cells
Thermosynechococcus vestitus
-
for sequencing
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.