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Literature summary 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

Organism

EC Number Organism UniProt Comment Textmining
1.3.7.7 Rhodobacter capsulatus D5ANS3 and P26164 and P26163 D5ANS3 i.e. iron-sulfur ATP-binding protein BchL, P26164 i.e. subunit BchN, P26163 i.e. reductase subunit BchB
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1.3.7.7 Rhodobacter capsulatus ATCC BAA-309 D5ANS3 and P26164 and P26163 D5ANS3 i.e. iron-sulfur ATP-binding protein BchL, P26164 i.e. subunit BchN, P26163 i.e. reductase subunit BchB
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.7.7 protochlorophyllide a + reduced ferredoxin + 4 ATP + 4 H2O
-
 Rhodobacter capsulatus chlorophyllide a + oxidized ferredoxin + 4 ADP + 4 phosphate
-
 ?
1.3.7.7 protochlorophyllide a + reduced ferredoxin + 4 ATP + 4 H2O
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 Rhodobacter capsulatus ATCC BAA-309 chlorophyllide a + oxidized ferredoxin + 4 ADP + 4 phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.3.7.7 bchB
-
 Rhodobacter capsulatus
1.3.7.7 bchL
-
 Rhodobacter capsulatus
1.3.7.7 bchN
-
 Rhodobacter capsulatus
1.3.7.7 dark-operative protochlorophyllide oxidoreductase
-
 Rhodobacter capsulatus
1.3.7.7 DPOR
-
 Rhodobacter capsulatus