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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
-
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
B0F838; B0F839
-
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
A0A2M6VWJ9
-
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-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
B0F838; B0F839
-
light-independent protochlorophyllide oxidoreductase
-
LIPOR

-
-
LPOR

-
-
-
-
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 A

-
-
NADPH:protochlorophyllide oxidoreductase A
-
-
NADPH:protochlorophyllide oxidoreductase A
-
-
NADPH:protochlorophyllide oxidoreductase B

-
-
NADPH:protochlorophyllide oxidoreductase B
-
-
PCR

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POR

-
-
POR A

-
-
POR B

-
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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
B0F838; B0F839
-
protochlorophyllide oxidoreductase
-
protochlorophyllide oxidoreductase
-
-
protochlorophyllide oxidoreductase
-
-
protochlorophyllide oxidoreductase
-
-
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
A0A2M6VWJ9
-
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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+
-
Substrates: -
Products: -
?
8-ethyl-chlorophyll b + NADPH + H+
? + NADP+
-
Substrates: -
Products: -
?
8-vinyl-chlorophyll a + NADPH + H+
? + NADP+
-
Substrates: -
Products: -
?
8-vinyl-chlorophyll b + NADPH + H+
? + NADP+
-
Substrates: -
Products: -
?
C8-ethyl-C13(2)-(r)-protochlorophyllide + NADPH
? + NADP+
-
Substrates: stereoisomer of the substrate
Products: -
?
chlorophyllide a + NADP+
protochlorophyllide + NADPH + H+
divinyl protochlorophyllide a + NADPH
divinyl chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
monovinyl protochlorophyllide a + NADPH
monovinyl chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + dithionite
chlorophyllide + SO2
-
Substrates: -
Products: -
?
protochlorophyllide + dithiothreitol
chlorophyllide + oxidized dithiothreitol
-
Substrates: -
Products: -
?
protochlorophyllide + NADH + H+
chlorophyllide a + NAD+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
protochlorophyllide + reduced ferredoxin
chlorophyllide + oxidized ferredoxin
-
Substrates: ferredoxin is the natural electron donor
Products: -
?
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
protochlorophyllide b + NADPH + H+
chlorophyllide b + NADP+
-
Substrates: -
Products: -
?
Zn-protopheophorbide a + NADPH + H+
? + NADP+
-
Substrates: efficient substrate
Products: -
?
additional information
?
-
chlorophyllide a + NADP+

protochlorophyllide + NADPH + H+
Substrates: -
Products: -
r
chlorophyllide a + NADP+
protochlorophyllide + NADPH + H+
Substrates: -
Products: -
r
chlorophyllide a + NADP+
protochlorophyllide + NADPH + H+
Substrates: -
Products: -
?
chlorophyllide a + NADP+
protochlorophyllide + NADPH + H+
-
Substrates: POR catalyzes the NADPH-dependent reduction of the C17-C18 double bond of protochlorophyllide to form chlorophyllide
Products: -
r
protochlorophyllide + NADPH

chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: 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
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: key enzyme of chlorophyll biosynthesis
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Substrates: constitutive enzyme
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: 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
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Substrates: light-dependent reaction
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: light-dependent reaction
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
393835, 393836, 393837, 393838, 393839, 393841, 393843, 393845, 393848, 393852, 393853, 393858, 393859, 393861, 393866 Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: key enzyme for light-dependent chlorophyll biosynthesis
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: light-dependent reaction
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
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 Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: biosynthetic pathway leading to chlorophyll a
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: chlorophyll-biosynthetic pathway
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: key enzyme for the light-induced greening of etiolated angiosperm plants
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Substrates: constitutive enzyme
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: important regulatory step in chlorophyll biosynthesis
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: chlorophyll-biosynthetic pathway
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: constitutive enzyme
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: the enzyme might be directly involved in the regulation of the metabolism of other porphyrins
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: 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
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Substrates: constitutive enzyme
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: key regulatory step in chlorophyll biosynthesis pathway
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: 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
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: light-driven enzyme. The catalytic mechanism involves two additional steps, which do not require light
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
393842, 393843, 393844, 393846, 393847, 393848, 393851, 393853, 393855, 393857, 393858 Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Substrates: constitutive enzyme
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+

chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
B0F838; B0F839
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
Substrates: activation by light
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
Substrates: activation by light
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
Substrates: activation by light
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+

chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: the enzyme (LPOR) catalyzes a photocatalytic reaction
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: -
Products: -
r
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: the enzyme (LPOR) catalyzes a photocatalytic reaction
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: -
Products: -
r
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: -
Products: -
r
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: -
Products: -
r
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: the enzyme (LPOR) catalyzes a photocatalytic reaction
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: the enzyme (LPOR) catalyzes a photocatalytic reaction
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
A0A2M6VWJ9
Substrates: -
Products: -
r
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: the enzyme (LPOR) catalyzes a photocatalytic reaction
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: the enzyme (LPOR) catalyzes a photocatalytic reaction
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: light-dependent reaction of chlorophyll biosynthesis
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: 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
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: the enzyme (LPOR) catalyzes a photocatalytic reaction
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide a + NADPH + H+

chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
Substrates: -
Products: -
?
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
Substrates: -
Products: -
?
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: light-dependent reaction
Products: -
?
additional information

?
-
-
Substrates: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: the inhibition of por gene expression by continous far red light is mediated by phytochrome A
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: individual steps of the reaction catalyzed by the light-activated enzyme protochlorophyllide oxidoreductase couple with solvent dynamics, temperature-dependent UV-visible microspectrophotometry study, overview
Products: -
?
additional information
?
-
-
Substrates: does not accept protochlorophyllide a' or any other compounds with substituents at C-13-2 different from protochlorophyllide a
Products: -
?
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+
-
Substrates: -
Products: -
?
monovinyl protochlorophyllide a + NADPH
monovinyl chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADH + H+
chlorophyllide a + NAD+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
protochlorophyllide + reduced ferredoxin
chlorophyllide + oxidized ferredoxin
-
Substrates: ferredoxin is the natural electron donor
Products: -
?
protochlorophyllide a + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
additional information
?
-
chlorophyllide a + NADP+

protochlorophyllide + NADPH + H+
Substrates: -
Products: -
r
chlorophyllide a + NADP+
protochlorophyllide + NADPH + H+
Substrates: -
Products: -
r
chlorophyllide a + NADP+
protochlorophyllide + NADPH + H+
-
Substrates: POR catalyzes the NADPH-dependent reduction of the C17-C18 double bond of protochlorophyllide to form chlorophyllide
Products: -
r
protochlorophyllide + NADPH

chlorophyllide + NADP+
-
Substrates: 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
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: key enzyme of chlorophyll biosynthesis
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Substrates: constitutive enzyme
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: 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
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
393835, 393836, 393837, 393838, 393839, 393841, 393843, 393845, 393848, 393852, 393853, 393858, 393861, 393866 Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: key enzyme for light-dependent chlorophyll biosynthesis
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
393833, 393836, 393838, 393839, 393841, 393842, 393843, 393844, 393851, 393852, 393853, 393855, 393857, 393858, 393859, 393860, 393865 Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: biosynthetic pathway leading to chlorophyll a
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: chlorophyll-biosynthetic pathway
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: key enzyme for the light-induced greening of etiolated angiosperm plants
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Substrates: constitutive enzyme
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: important regulatory step in chlorophyll biosynthesis
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: chlorophyll-biosynthetic pathway
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: constitutive enzyme
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: the enzyme might be directly involved in the regulation of the metabolism of other porphyrins
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: 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
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Substrates: constitutive enzyme
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: key regulatory step in chlorophyll biosynthesis pathway
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
393842, 393843, 393844, 393846, 393847, 393848, 393851, 393853, 393855, 393857, 393858 Substrates: -
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
Substrates: constitutive enzyme
Products: -
?
protochlorophyllide + NADPH
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+

chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
B0F838; B0F839
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
Substrates: activation by light
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
Substrates: activation by light
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide + NADP+
-
Substrates: activation by light
Products: -
?
protochlorophyllide + NADPH + H+

chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: the enzyme (LPOR) catalyzes a photocatalytic reaction
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: -
Products: -
r
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: -
Products: -
r
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: -
Products: -
r
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: -
Products: -
r
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: the enzyme (LPOR) catalyzes a photocatalytic reaction
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: the enzyme (LPOR) catalyzes a photocatalytic reaction
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
A0A2M6VWJ9
Substrates: -
Products: -
r
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: the enzyme (LPOR) catalyzes a photocatalytic reaction
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: -
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: light-dependent reaction of chlorophyll biosynthesis
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
Substrates: the enzyme (LPOR) catalyzes a photocatalytic reaction
Products: -
?
protochlorophyllide + NADPH + H+
chlorophyllide a + NADP+
-
Substrates: -
Products: -
?
additional information

?
-
-
Substrates: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
additional information
?
-
-
Substrates: the inhibition of por gene expression by continous far red light is mediated by phytochrome A
Products: -
?
additional information
?
-
-
Substrates: does not accept protochlorophyllide a' or any other compounds with substituents at C-13-2 different from protochlorophyllide a
Products: -
?
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
-
pH 7.5
0.00136
monovinyl protochlorophyllide a
-
pH 7.5
0.00015 - 0.035
protochlorophyllide
0.00027 - 0.0086
protochlorophyllide a
additional information
additional information
-
0.000012
NADPH

-
0.000013
NADPH
-
50°C, pH 7.5
0.0008
NADPH
-
pH 7.5, 40°C, mutant enzyme P158F
0.0009
NADPH
-
pH 7.5, 40°C, wild-type enzyme
0.001
NADPH
-
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
-
pH 7.5, 40°C, mutant enzyme K156N/I157V
0.0025
NADPH
-
pH 7.5, 40°C, mutant enzyme F237Y
0.0029
NADPH
-
pH 7.5, 40°C, mutant enzyme K156N
0.0029
NADPH
-
pH 7.5, 40°C, mutant enzyme I157V
0.0029
NADPH
-
pH 7.5, 40°C, mutant enzyme F233L
0.0033
NADPH
-
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
-
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
-
pH 7.5, 40°C, mutant enzyme F237Y
0.0075
protochlorophyllide
-
pH 7.5, 40°C, mutant enzyme F233L
0.0077
protochlorophyllide
-
pH and temperature not specified in the publication
0.0078
protochlorophyllide
-
pH and temperature not specified in the publication
0.0078
protochlorophyllide
-
pH 7.5, 40°C, wild-type enzyme
0.0078
protochlorophyllide
pH 7.5, 30°C
0.0081
protochlorophyllide
-
pH 7.5, 40°C, mutant enzyme F233Y
0.0106
protochlorophyllide
-
pH 7.4, 34°C
0.0107
protochlorophyllide
-
pH 7.5, 40°C, mutant enzyme I157V
0.01083
protochlorophyllide
-
-
0.0135
protochlorophyllide
-
pH 7.5, 40°C, mutant enzyme P158A
0.0151
protochlorophyllide
-
pH 7.5, 40°C, mutant enzyme K156N
0.0166
protochlorophyllide
-
pH 7.5, 40°C, mutant enzyme K156N/I157V
0.0181
protochlorophyllide
-
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

-
stable enzyme assay system by mixing recombinant enzyme components L-protein and NB-protein under anaerobic conditiions
-
additional information
additional information
-
detailed steady-state kinetics characterization of enzyme
-
additional information
additional information
-
spectroscopic and detailed kinetic characterization of reaction
-
additional information
additional information
-
EPR and Stark spectroscopies analysis of enzyme reaction
-
additional information
additional information
-
kinetic model with thermodynamic parameters governing catalytic interconversion rates, overview
-
additional information
protochlorophyllide
-
wild type enzyme, relative activity 100%
additional information
protochlorophyllide
-
mutant C37S, relative activity 99.4%
additional information
protochlorophyllide
-
mutant C199S, relative activity 98.2%
additional information
protochlorophyllide
-
mutant C226S, relative activity 7.2%
additional information
protochlorophyllide
-
mutant C37S/C199S, relative activity 98.8%
additional information
protochlorophyllide
-
mutant C37S/C226S, relative activity 6.8%
additional information
protochlorophyllide
-
mutant C199/C226S, relative activity 6.6%
additional information
protochlorophyllide
-
mutant C37S/C199S/C226S, relative activity 7.1%
additional information
protochlorophyllide
-
wild type enzyme, relative activity 100%
additional information
protochlorophyllide
-
mutant Y193F, relative activity 19.5%
additional information
protochlorophyllide
-
mutant Y193A, relative activity 5.5%
additional information
protochlorophyllide
-
mutant Y193S, relative activity 2.4%
additional information
protochlorophyllide
-
mutant K197A, relative activity 2.7%
additional information
protochlorophyllide
-
mutant K197R, relative activity 2.3%
additional information
protochlorophyllide
-
mutant K197Q, relative activity 2.0%
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0.003 - 0.17
protochlorophyllide
0.011
NADPH

-
pH 7.5, 25°C, mutant C199S/C226S, co-substrate: protochlorophyllide
0.0113
NADPH
-
pH 7.5, 25°C, mutant C37S/C226S, co-substrate: protochlorophyllide
0.0117
NADPH
-
pH 7.5, 25°C, mutant C37S/C199S/C226S, co-substrate: protochlorophyllide
0.0118
NADPH
-
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
-
pH 7.5, 25°C, mutant C199S, co-substrate: protochlorophyllide
0.164
NADPH
-
pH 7.5, 25°C, mutant C37S, co-substrate: protochlorophyllide
0.165
NADPH
-
pH 7.5, 25°C, wild-type, co-substrate: protochlorophyllide
0.003
protochlorophyllide

-
mutant K197Q
0.004
protochlorophyllide
-
mutant Y193S
0.004
protochlorophyllide
-
mutant K197A
0.004
protochlorophyllide
-
mutant K197R
0.007
protochlorophyllide
-
pH 7.5, 40°C, mutant enzyme F233L
0.009
protochlorophyllide
-
mutant Y193A
0.01
protochlorophyllide
mutant enzyme T145A, at 25°C, pH not specified in the publication
0.01
protochlorophyllide
mutant enzyme T147F, at 25°C, pH not specified in the publication
0.01
protochlorophyllide
mutant enzyme N149V, at 25°C, pH not specified in the publication
0.01
protochlorophyllide
mutant enzyme T230F, at 25°C, pH not specified in the publication
0.011
protochlorophyllide
-
mutant C199/C226S
0.011
protochlorophyllide
-
pH 7.5, 25°C, mutant C199S/C226S, co-substrate: NADPH
0.0113
protochlorophyllide
-
mutant C37S/C226S
0.0113
protochlorophyllide
-
pH 7.5, 25°C, mutant C37S/C226S, co-substrate: NADPH
0.0117
protochlorophyllide
-
mutant C37S/C199S/C226S
0.0117
protochlorophyllide
-
pH 7.5, 25°C, mutant C37S/C199S/C226S, co-substrate: NADPH
0.0118
protochlorophyllide
-
mutant C226S
0.0118
protochlorophyllide
-
pH 7.5, 25°C, mutant C226S, co-substrate: NADPH
0.013
protochlorophyllide
-
pH 7.5, 40°C, mutant enzyme F233Y
0.013
protochlorophyllide
-
pH 7.5, 40°C, mutant enzyme P158F
0.02
protochlorophyllide
mutant enzyme N39V, at 25°C, pH not specified in the publication
0.02
protochlorophyllide
mutant enzyme T147S, at 25°C, pH not specified in the publication
0.022
protochlorophyllide
-
pH 7.5, 40°C, mutant enzyme K156N/I157V
0.027
protochlorophyllide
-
pH 7.5, 40°C, wild-type enzyme
0.03
protochlorophyllide
-
pH 7.5, 40°C, mutant enzyme F237Y
0.032
protochlorophyllide
-
mutant Y193F
0.035
protochlorophyllide
-
pH 7.5, 40°C, mutant enzyme K156N
0.037
protochlorophyllide
-
pH 7.5, 40°C, mutant enzyme I157V
0.037
protochlorophyllide
-
pH 7.5, 40°C, mutant enzyme P158A
0.07
protochlorophyllide
mutant enzyme N90A, at 25°C, pH not specified in the publication
0.1
protochlorophyllide
mutant enzyme H236A, at 25°C, pH not specified in the publication
0.16
protochlorophyllide
mutant enzyme S16C, at 25°C, pH not specified in the publication
0.16
protochlorophyllide
mutant enzyme G19A, at 25°C, pH not specified in the publication
0.16
protochlorophyllide
mutant enzyme R38V, at 25°C, pH not specified in the publication
0.16
protochlorophyllide
mutant enzyme K42A, at 25°C, pH not specified in the publication
0.16
protochlorophyllide
mutant enzyme S189A, at 25°C, pH not specified in the publication
0.16
protochlorophyllide
mutant enzyme T230A, at 25°C, pH not specified in the publication
0.16
protochlorophyllide
mutant enzyme T230S, at 25°C, pH not specified in the publication
0.162
protochlorophyllide
-
mutant C199S
0.162
protochlorophyllide
-
pH 7.5, 25°C, mutant C199S, co-substrate: NADPH
0.163
protochlorophyllide
-
mutant C37S/C199S
0.164
protochlorophyllide
-
mutant C37S
0.164
protochlorophyllide
-
wild type enzyme
0.164
protochlorophyllide
-
pH 7.5, 25°C, mutant C37S, co-substrate: NADPH
0.165
protochlorophyllide
-
wild type enzyme
0.165
protochlorophyllide
-
pH 7.5, 25°C, wild-type, co-substrate: NADPH
0.17
protochlorophyllide
wild type enzyme, at 25°C, pH not specified in the publication
0.17
protochlorophyllide
mutant enzyme Y94F, at 25°C, pH not specified in the publication
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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
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
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
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
A0A2M6VWJ9
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
-
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
-
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
-
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
-
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
-
RNAi based simultaneous silencing of all forms of light-dependent NADPH:protochlorophyllide oxidoreductase genes results in the accumulation of protochlorophyllide in tobacco
malfunction
-
an enzyme-less mutant grows photoautotrophically in moderate light and contains a maximum of 20% of the wild type chlorophyll level
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
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 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
A0A2M6VWJ9
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
-
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
-
physiological function

-
LHPP (light-harvesting POR:Pchlide complexes) assembly is indispensable for barley POR functions and seedling greening
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 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
light-dependent protochlorophyllide oxidoreductase (LPOR) is a rate-limiting key chlorophyll biosynthetic enzyme
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
A0A2M6VWJ9
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
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light-dependent protochlorophyllide oxidoreductase (LPOR) is a rate-limiting key chlorophyll biosynthetic enzyme
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physiological function
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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
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physiological function
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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
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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
A0A2M6VWJ9
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
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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
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112000
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substrate-enzyme complex, gel filtration
210000
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purified ChlNB complex, gel filtration
32395
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2 * 32395, purified ChlL subunit, deduced from amino acid sequence
36046
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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
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amino acid composition
40000
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determined by SDS-PAGE
40150
x * 40150, recombinant enzyme, SDS-PAGE
41000
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identified with monospecific polyclonal antibody
41200
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predicted from cDNA
42000
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determined by SDS-PAGE
45000
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2 * 45000, SDS-PAGE
46000
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x * 46000, precursor protein, x * 38000, mature protein
46199
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2 * 46199 + 2 * 58729, purified ChlNB complex, deduced from amino acid sequence
48671
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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
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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
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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
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2 * 46199 + 2 * 58729, purified ChlNB complex, deduced from amino acid sequence
78800
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recombinant fusion protein, gel filtration
34000

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34000
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2 related peptides of 34000/36000
34000
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2 related peptides of 34000/35000
35000

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35000
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2 related peptides of 34000/35000
35000
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SDS-PAGE shows 2 closely related peptides of 35000 and 37000
35000
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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

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36000
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2 related peptides of 36000/38000
36000
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predicted from amino acid composition
36000
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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

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37000
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gel filtration, doublet of 2 peptides of 35000 and 37000 co-purified
37000
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covalent radioactive labelling technique
37000
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x * 37000, SDS-PAGE
38000

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38000
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x * 46000, precursor protein, x * 38000, mature protein
44000

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44000
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precursor polypeptide, predicted from mRNA
60000

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purified ChlL subunit, gel filtration
60000
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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
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C276A
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the mutant is hypersensitive to high-light conditions during greening
Cys303A
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the mutant is hypersensitive to high-light conditions during greening
C103S
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the BchN subunit variant shows 0.5% residual activity and is essentially inactive
C21S
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the BchN subunit variant shows 0.5% residual activity and is essentially inactive
C46S
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the BchN subunit variant shows 0.5% residual activity and is essentially inactive
C104A
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no detectable effect on the import of protein to plastid and processing in darkness
C166A
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no detectable effect on the import of protein to plastid and processing in darkness
C195A
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mutant, constructed for the identification of the protochlorophyllide binding site
C222A
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mutant, constructed for the identification of the protochlorophyllide binding site
C276A
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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
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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
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mutant, constructed for the identification of the protochlorophyllide binding site
C85A
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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
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mutant, the putative proton donor, Tyr 189, is replaced by a phenylalanine residue
C199/C226S
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mutant, mutation of the absolutely conserved cysteine residues
C199S/C226S
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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
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mutant enzyme shows around 40% of wild-type activity
F233Y
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mutant enzyme shows around 40% of wild-type activity
F237Y
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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
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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
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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
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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
the mutant shows wild type value for turnover number
H236A
the mutant shows reduced value for turnover number compared to the wild type enzyme
K197A
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mutant, constructed for analysing the role of the conserved active site lysine
K197Q
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mutant, constructed for analysing the role of the conserved active site lysine
K197R
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mutant, constructed for analysing the role of the conserved active site lysine
K42A
the mutant shows wild type value for turnover number
N149V
the mutant shows reduced value for turnover number compared to the wild type enzyme
N39V
the mutant shows reduced value for turnover number compared to the wild type enzyme
N90A
the mutant shows reduced value for turnover number compared to the wild type enzyme
R38V
the mutant shows wild type value for turnover number
S16C
the mutant shows wild type value for turnover number
S189A
the mutant shows wild type value for turnover number
T145A
the mutant shows reduced value for turnover number compared to the wild type enzyme
T147F
the mutant shows reduced value for turnover number compared to the wild type enzyme
T147S
the mutant shows reduced value for turnover number compared to the wild type enzyme
T230A
the mutant shows wild type value for turnover number
T230F
the mutant shows reduced value for turnover number compared to the wild type enzyme
T230S
the mutant shows wild type value for turnover number
Y193A
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mutant, constructed for analysing the role of the conserved active site tyrosine
Y193F
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mutant, constructed for analysing the role of the conserved active site tyrosine
Y193S
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mutant, constructed for analysing the role of the conserved active site tyrosine
Y94F
the mutant shows wild type value for turnover number
C199S

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mutant, Cys199 has a relatively minor role in catalysis
C199S
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kcat comparable to wild-type, relative activity comparable to wild-type, Kd (NADPH) comparable to wild-type, Kd (protochlorophyllide) comparable to wild-type
C226S

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mutant, mutation causes a remarkable change in the mechansim of the hydrogen transfer reactions
C226S
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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
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

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mutant, Cys37 has a relatively minor role in catalysis
C37S
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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

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mutant, mutation of the absolutely conserved cysteine residues
C37S/C199S
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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

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mutant, mutation of the absolutely conserved cysteine residues
C37S/C199S/C226S
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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

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mutant, mutation of the absolutely conserved cysteine residues
C37S/C226S
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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
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