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Information on EC 1.3.7.7 - ferredoxin:protochlorophyllide reductase (ATP-dependent)
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EC Tree
1.3.7.7 ferredoxin:protochlorophyllide reductase (ATP-dependent)IUBMB Comments
Occurs in photosynthetic bacteria, cyanobacteria, green algae and gymnosperms. The enzyme catalyses trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration. Unlike EC 1.3.1.33 (protochlorophyllide reductase), light is not required. The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase (EC 1.18.6.1), which catalyses an ATP-driven reduction.
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Word Map
- 1.3.7.7
-
light-dependent
-
rhodobacter
- capsulatus
- angiosperms
- nitrogenase
- bacteriochlorophyll
-
gymnosperm
-
nitrogenase-like
-
phototrophs
-
dark-grown
-
nb-protein
-
anoxygenic
-
marchantia
-
etioplasts
-
prolamellar
-
light-grown
-
dinitrogen
-
plectonema
- boryanum
- liverwort
-
photosynthesis-related
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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2
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2
+
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2
Synonyms
light-independent protochlorophyllide reductase, dark protochlorophyllide reductase, light-independent pchlide reductase, dark-operative pchlide oxidoreductase, light-independent (dark-operative) pchlide oxidoreductase, dark-operative protochlorophyllide reductase, protochlorophyllide oxidoreductase complex, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bchB
bchL
bchN
dark operative protochlorophyllide oxidoreductase
dark-operative Pchlide oxidoreductase
dark-operative protochlorophyllide oxidoreductase
dark-operative protochlorophyllide reductase
DPOR
light-independent (dark-operative) Pchlide oxidoreductase
light-independent Pchlide oxidoreductase
light-independent Pchlide reductase
light-independent protochlorophyllide oxidoreductase
light-independent protochlorophyllide oxidoreductases
-
light-independent protochlorophyllide reductase
dark-operative protochlorophyllide oxidoreductase
-
dark-operative protochlorophyllide oxidoreductase
-
dark-operative protochlorophyllide oxidoreductase
-
-
DPOR
the DPOR holoenzyme is comprised of two component proteins, the dimeric protein L and the heterotetrameric NB-protein
DPOR
-
DPOR consists of two components, the L-protein and the NB-protein
light-independent protochlorophyllide oxidoreductase
-
light-independent protochlorophyllide reductase
-
light-independent protochlorophyllide reductase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
-
-
-
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chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
reaction mechanism for trans-specific reduction, overview
-
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
dynamic switch mechanism of DPOR, catalytic mechanism and structure-function analysis, detailed overview
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
reaction mechanism and structure-function relationship, overview
-
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
reaction mechanism and structure-function relationship, overview
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chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
reaction mechanism and structure-function relationship, overview
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chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
reaction mechanism and structure-function relationship, overview
-
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
reaction mechanism and structure-function relationship, overview
-
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
reaction mechanism and structure-function relationship, overview
-
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
reaction mechanism for trans-specific reduction, overview
-
-
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PATHWAY SOURCE
PATHWAYS
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,
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SYSTEMATIC NAME
IUBMB Comments
ATP-dependent ferredoxin:protochlorophyllide-a 7,8-oxidoreductase
Occurs in photosynthetic bacteria, cyanobacteria, green algae and gymnosperms. The enzyme catalyses trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration. Unlike EC 1.3.1.33 (protochlorophyllide reductase), light is not required. The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase (EC 1.18.6.1), which catalyses an ATP-driven reduction.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
chlorophyllide a + reduced ferredoxin + ATP
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
protochlorophyllide a + reduced ferredoxin + 4 ATP + 4 H2O
chlorophyllide a + oxidized ferredoxin + 4 ADP + 4 phosphate
chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
-
-
-
-
?
chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
-
-
-
-
?
chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
Thermosynechococcus vestitus
-
-
-
-
?
chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
Thermosynechococcus vestitus
-
ferredoxin provides a single electron to ChlL2, which in turn transfers an electron to (ChlN/ChlB)2. Hydrolysis of the two ATP molecules results in the dissociation of ChlL2 from reduced (ChlN/ChlB)2. Protochlorophyllide reduction is completed after two sequential catalytic redox cycles. Substrate recognition by (ChlN/ChlB)2 essentially involves all functional groups of the substrate, modeling of the substrate binding site of (ChlN/ChlB)2, overview. Electron transfer pathway via the various redox centers of DPOR to the substrate, overview
-
-
?
chlorophyllide a + reduced ferredoxin + ATP
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
-
-
-
?
chlorophyllide a + reduced ferredoxin + ATP
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
-
-
-
-
?
chlorophyllide a + reduced ferredoxin + ATP
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
-
-
-
-
?
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
-
-
-
?
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
-
-
-
-
?
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
-
-
-
?
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
-
-
-
-
?
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
-
-
-
?
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
-
DPOR catalyzes the stereo-specific reduction of C17-C18 double bond on the D-ring of protochlorophyllide
-
-
?
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
DPOR catalyzes the formation of chlorophyllide a through ATP-dependent, stereospecific reduction of the C-17=C-18 double bond of Pchlide ring D
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
the homodimeric ChlL2 subunit carrying a [4Fe-4S] cluster transfers electrons to the corresponding heterotetrameric catalytic subunit (ChlN/ChlB)2, which also possesses a redox active [4Fe-4S] cluster
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 4 ATP + 4 H2O
chlorophyllide a + oxidized ferredoxin + 4 ADP + 4 phosphate
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 4 ATP + 4 H2O
chlorophyllide a + oxidized ferredoxin + 4 ADP + 4 phosphate
-
-
-
?
additional information
?
-
-
proposed catalytic redox cycle of DPOR, overview
-
-
?
additional information
?
-
-
although chlorophyllide c binds to the substrate-binding pocket in the NB-protein, the C17-C18 double bond on the D-ring of chlorophyllide c is not reduced by the DPOR
-
-
?
additional information
?
-
-
DPOR is a nitrogenase-like enzyme consisting of two components, L-protein (a BchL dimer) and NB-protein (a BchN-BchB heterotetramer)
-
-
?
additional information
?
-
-
each catalytic BchN-BchB unit contains one protochlorophyllidee and one iron-sulfur NB-cluster coordinated uniquely by one aspartate and three cysteines. Unique aspartate ligation is not necessarily needed for the cluster assembly but is essential for the catalytic activity. Specific protochlorophyllide-binding accompanies the partial unwinding of an alpha-helix that belongs to the next catalytic BchN-BchB unit, unique trans-specific reduction mechanism in which the distorted C17-propionate of protochlorophyllid and an aspartate from BchB serve as proton donors for C18 and C17 of protochlorophyllide, respectively, overview
-
-
?
additional information
?
-
-
the C175C18 double bond of chlorophyll c is not reduced by DPOR
-
-
?
additional information
?
-
The reaction mechanism begins with single-electron reduction of the substrate by the (Cys)3Asp-ligated [4Fe-4S]-center, yielding a negatively-charged intermediate. Depending on the rate of Fe-S cluster re-reduction, the reaction either proceeds through double protonation of the single-electron-reduced substrate, or by alternating proton/electron transfer. The Fe-S cluster rereduction should be the rate-limiting stage of the process
-
-
?
additional information
?
-
The reaction mechanism begins with single-electron reduction of the substrate by the (Cys)3Asp-ligated [4Fe-4S]-center, yielding a negatively-charged intermediate. Depending on the rate of Fe-S cluster re-reduction, the reaction either proceeds through double protonation of the single-electron-reduced substrate, or by alternating proton/electron transfer. The Fe-S cluster rereduction should be the rate-limiting stage of the process
-
-
?
additional information
?
-
-
DPOR is a nitrogenase-like enzyme consisting of two components, L-protein (a BchL dimer) and NB-protein (a BchN-BchB heterotetramer)
-
-
?
additional information
?
-
-
each catalytic BchN-BchB unit contains one protochlorophyllidee and one iron-sulfur NB-cluster coordinated uniquely by one aspartate and three cysteines. Unique aspartate ligation is not necessarily needed for the cluster assembly but is essential for the catalytic activity. Specific protochlorophyllide-binding accompanies the partial unwinding of an alpha-helix that belongs to the next catalytic BchN-BchB unit, unique trans-specific reduction mechanism in which the distorted C17-propionate of protochlorophyllid and an aspartate from BchB serve as proton donors for C18 and C17 of protochlorophyllide, respectively, overview
-
-
?
additional information
?
-
-
the C175C18 double bond of chlorophyll c is not reduced by DPOR
-
-
?
additional information
?
-
Thermosynechococcus vestitus
-
the invitro assay is performed with purified recombinant GST-tagged (ChlN/ChlB)2 complex and a ChlL2 subunit purified from Prochlorococcus marinus
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
chlorophyllide a + reduced ferredoxin + ATP
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
-
-
-
?
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
additional information
?
-
-
proposed catalytic redox cycle of DPOR, overview
-
-
?
chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
-
-
-
-
?
chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
-
-
-
-
?
chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
Thermosynechococcus vestitus
-
-
-
-
?
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
-
-
-
-
?
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
-
-
-
?
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[4Fe-4S]-center
reaction potential of the FeâS cluster shows pH-dependence
4Fe-4S-center
-
NB-protein of DPOR carries two oxygen-tolerant [4Feâ4S] clusters
4Fe-4S-center
the enzyme contains an Fe-S cluster as redox center in all subunits
4Fe-4S-center
-
the L-protein carries a [4Fe-4S] cluster between the protomers that is very similar to that of the nitrogenase Fe protein. The NB-protein also carries a [4Fe-4S] cluster that mediates electrons from the L-cluster to the protochlorophyllide molecule
ATP
Thermosynechococcus vestitus
-
dependent on, the homodimeric ChlL2 bearing an intersubunit [4Fe-4S] cluster is an ATP-dependent reductase
ATP
subunit L contains the ATP-binding motif
ATP
-
dependent on, the homodimeric subunit ChlL2 functions as an ATP-dependent switch protein, triggering the transient interaction of ChlL2 and heterotetrameric catalytic subunit (ChlN/ChlB)2
Ferredoxin
-
each catalytic BchN-BchB unit contains one protochlorophyllidee and one iron-sulfur NB-cluster coordinated uniquely by one aspartate and three cysteines. Unique aspartate ligation is not necessarily needed for the cluster assembly but is essential for the catalytic activity, overview
-
Ferredoxin
Thermosynechococcus vestitus
-
the enzyme contains intersubunit [4Fe-4S] cluster in the homodimer formed by two ChlL subunits. The [4Fe-4S] cluster coordinated by an aspartate oxygen alongside three cysteine ligands, structure, overview. Iron-sulfur cluster coordination in DPOR compared to nitrogenase, overview
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Mg2+
Fe2+
the purified, recombinant protein L contains 3.6 mol of Fe/mol of protein L homodimer, consistent with the presence of a [4Fe-4S] cluster
Fe2+
-
transfer of a single electron from the [4Fe-4S] cluster of ChlL2 onto a second [4Fe-4S] cluster located on (ChlN/ChlB)2
Fe2+
two redox-active [4Fe-4S] clusters, both [4Fe-4S] clusters are centered around the 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 subunit N and one aspartate residue from subunit B
Fe2+
Thermosynechococcus vestitus
-
the enzyme contains intersubunit [4Fe-4S] cluster in the homodimer formed by two ChlL subunits. The [4Fe-4S] cluster coordinated by an aspartate oxygen alongside three cysteine ligands, structure, overview
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Dithionite
-
dark protochlorophyllide reductase activity is dependent on the reductant dithionite
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0106
protochlorophyllide
-
in 100 mM HEPES-KOH (pH 7.4), 5 mM MgCl2, 5 mM dithiothreitol, at 34°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.026
-
purified recombinant protochlorophyllide-bound NB-protein, recovered from crystals, pH not specified in the publication, temperature not specified in the publication
0.0262
-
purified enzyme, pH not specified in the publication, at 34°C
0.05
-
purified recombinant protochlorophyllide-free NB-protein, recovered from crystals, pH not specified in the publication, temperature not specified in the publication
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunit B, subunit L, and subunit N; strain CS-41, also named Auxenochlorella protothecoides strain CS-41
UniProt
brenda
subunit B, subunit L, and subunit N
UniProt
brenda
subunit B, subunit L, and subunit N
UniProt
brenda
subunit B, subunit L, and subunit N
UniProt
brenda
three subunits of DPOR, encoded by genes bchL, bchN and bchB
-
-
brenda
three subunits of DPOR, encoded by genes bchL, bchN and bchB
-
-
brenda
subunit B, subunit L, and subunit N
UniProt
brenda
subunit B, subunit L, and subunit N
UniProt
brenda
subunit B, subunit L, and subunit N
UniProt
brenda
subunit B, subunit L, and subunit N
UniProt
brenda
three subunits of DPOR, encoded by genes bchL, bchN and bchB
-
-
brenda
subunit B, subunit L, and subunit N; variant Juniperus chinensis procumbens
UniProt
brenda
subunit B, subunit L, and subunit N
UniProt
brenda
gene chlB; three constitutive plastid genes chlL, chlN, and chlB
UniProt
brenda
gene chlB; three constitutive plastid genes chlL, chlN, and chlB
UniProt
brenda
subunit B, subunit L and subunit N
UniProt
brenda
subunit B, subunit L, and subunit N
UniProt
brenda
subunit B, subunit L, and subunit N
UniProt
brenda
three subunits of DPOR, encoded by genes bchL, bchN and bchB
-
-
brenda
DPOR subunit B; strain UTEX 481, also called Calothrix sp. PCC 7601 and Tolypothrix sp. PCC 7601
UniProt
brenda
DPOR subunit L; strain UTEX 481, also called Calothrix sp. PCC 7601 and Tolypothrix sp. PCC 7601
UniProt
brenda
DPOR subunit N; strain UTEX 481, also called Calothrix sp. PCC 7601 and Tolypothrix sp. PCC 7601
UniProt
brenda
three subunits of DPOR, encoded by genes bchL, bchN and bchB
-
-
brenda