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Literature summary for 1.3.7.7 extracted from

  • Broecker, M.J.; Waetzlich, D.; Saggu, M.; Lendzian, F.; Moser, J.; Jahn, D.
    Biosynthesis of (bacterio)chlorophylls: ATP-dependent transient subunit interaction and electron transfer of dark operative protochlorophyllide oxidoreductase (2010), J. Biol. Chem., 285, 8268-8277.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
additional information the ternary DPOR enzyme holocomplex comprising subunits ChlN, ChlB, and ChlL is trapped as an octameric (ChlN/ChlB)2(ChlL2)2 complex after incubation with the nonhydrolyzable ATP analogues adenosine 5'-(gamma-thio)triphosphate, adenosine 5'-(beta,gamma-imido)triphosphate, or MgADP in combination with AlF4-, complex structure, overview. A mutant ChlL2 protein, with a deleted Leu153 in the switch II region also allows for the formation of a stable octameric complex Prochlorococcus marinus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the homodimeric ChlL2 subunit carries a [4Fe-4S] cluster Prochlorococcus marinus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35000
-
octameric (ChlN/ChlB)2(ChlL2)2 subunit complex, 4 * 35000, subunit ChlL, + 2 * 45000, subunit ChlN, 2 * 60000, subunit ChlB, SDS-PAGE, 4 * 32395,subunit ChlL, + 2 * 46199, subunit ChlN, 2 * 58729, subunit ChlB, sequence calculation Prochlorococcus marinus
45000
-
octameric (ChlN/ChlB)2(ChlL2)2 subunit complex, 4 * 35000, subunit ChlL, + 2 * 45000, subunit ChlN, 2 * 60000, subunit ChlB, SDS-PAGE, 4 * 32395,subunit ChlL, + 2 * 46199, subunit ChlN, 2 * 58729, subunit ChlB, sequence calculation Prochlorococcus marinus
46199
-
octameric (ChlN/ChlB)2(ChlL2)2 subunit complex, 4 * 35000, subunit ChlL, + 2 * 45000, subunit ChlN, 2 * 60000, subunit ChlB, SDS-PAGE, 4 * 32395,subunit ChlL, + 2 * 46199, subunit ChlN, 2 * 58729, subunit ChlB, sequence calculation Prochlorococcus marinus
58729
-
octameric (ChlN/ChlB)2(ChlL2)2 subunit complex, 4 * 35000, subunit ChlL, + 2 * 45000, subunit ChlN, 2 * 60000, subunit ChlB, SDS-PAGE, 4 * 32395,subunit ChlL, + 2 * 46199, subunit ChlN, 2 * 58729, subunit ChlB, sequence calculation Prochlorococcus marinus
60000
-
octameric (ChlN/ChlB)2(ChlL2)2 subunit complex, 4 * 35000, subunit ChlL, + 2 * 45000, subunit ChlN, 2 * 60000, subunit ChlB, SDS-PAGE, 4 * 32395,subunit ChlL, + 2 * 46199, subunit ChlN, 2 * 58729, subunit ChlB, sequence calculation Prochlorococcus marinus
360000
-
enzyme complex, gel filtration Prochlorococcus marinus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Prochlorococcus marinus proposed catalytic redox cycle of DPOR, overview ?
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O Prochlorococcus marinus
-
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
?

Organism

Organism UniProt Comment Textmining
Prochlorococcus marinus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information proposed catalytic redox cycle of DPOR, overview Prochlorococcus marinus ?
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
-
Prochlorococcus marinus chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O 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 Prochlorococcus marinus chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
-
?

Subunits

Subunits Comment Organism
octamer octameric (ChlN/ChlB)2(ChlL2)2 subunit complex, 4 * 35000, subunit ChlL, + 2 * 45000, subunit ChlN, 2 * 60000, subunit ChlB, SDS-PAGE, 4 * 32395,subunit ChlL, + 2 * 46199, subunit ChlN, 2 * 58729, subunit ChlB, sequence calculation Prochlorococcus marinus

Synonyms

Synonyms Comment Organism
dark operative protochlorophyllide oxidoreductase
-
Prochlorococcus marinus
DPOR
-
Prochlorococcus marinus
protochlorophyllide oxidoreductase
-
Prochlorococcus marinus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Prochlorococcus marinus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Prochlorococcus marinus
Ferredoxin
-
Prochlorococcus marinus

General Information

General Information Comment Organism
additional information transient protein-protein interaction of ChlL2 and (ChlN/ChlB)2 is essential for the ATP-dependent electron transfer processes catalyzed by DPOR. Efficient octameric (ChlN/ChlB)2(ChlL2)2 enzyme complex formation required the presence of protochlorophyllide. Complete ATP hydrolysis is a prerequisite for intersubunit electron transfer Prochlorococcus marinus