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Literature summary for 1.3.1.33 extracted from

  • Nomata, J.; Terauchi, K.; Fujita, Y.
    Stoichiometry of ATP hydrolysis and chlorophyllide formation of dark-operative protochlorophyllide oxidoreductase from Rhodobacter capsulatus (2016), Biochem. Biophys. Res. Commun., 470, 704-709.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
protochlorophyllide + NADPH + H+ Rhodobacter capsulatus
-
chlorophyllide a + NADP+
-
?

Organism

Organism UniProt Comment Textmining
Rhodobacter capsulatus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Strep-Tactin column chromatography Rhodobacter capsulatus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme consists of an ATP-dependent reductase component, L-protein (a BchL dimer), and a catalytic component, NB-protein (a BchNeBchB heterotetramer). The L-protein transfers electrons to the NB-protein to reduce Pchlide, which is coupled with ATP hydrolysis Rhodobacter capsulatus ?
-
?
protochlorophyllide + NADPH + H+
-
Rhodobacter capsulatus chlorophyllide a + NADP+
-
?

Synonyms

Synonyms Comment Organism
bchB gene name of subunit Rhodobacter capsulatus
bchL gene name of subunit Rhodobacter capsulatus
bchN gene name of subunit Rhodobacter capsulatus
dark-operative protochlorophyllide oxidoreductase
-
Rhodobacter capsulatus
DPOR
-
Rhodobacter capsulatus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Rhodobacter capsulatus
NADPH
-
Rhodobacter capsulatus
[4Fe-4S]-center
-
Rhodobacter capsulatus