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Literature summary extracted from

  • Nomata, J.; Swem, L.R.; Bauer, C.E.; Fujita, Y.
    Overexpression and characterization of dark-operative protochlorophyllide reductase from Rhodobacter capsulatus (2005), Biochim. Biophys. Acta, 1708, 229-237.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.7.7 expressed in Rhodobacter capsulatus mutant DB176 cells Rhodobacter capsulatus

General Stability

EC Number General Stability Organism
1.3.1.33 rapid loss of activity during attempts to purify Rhodobacter capsulatus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.33 additional information
-
additional information stable enzyme assay system by mixing recombinant enzyme components L-protein and NB-protein under anaerobic conditiions Rhodobacter capsulatus
1.3.1.33 0.0106
-
protochlorophyllide pH 7.4, 34°C Rhodobacter capsulatus
1.3.7.7 0.0106
-
protochlorophyllide in 100 mM HEPES-KOH (pH 7.4), 5 mM MgCl2, 5 mM dithiothreitol, at 34°C Rhodobacter capsulatus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.1.33 36000
-
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 Rhodobacter capsulatus
1.3.1.33 36046
-
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 Rhodobacter capsulatus
1.3.1.33 48671
-
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 Rhodobacter capsulatus
1.3.1.33 52000
-
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 Rhodobacter capsulatus
1.3.1.33 57191
-
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 Rhodobacter capsulatus
1.3.1.33 60000
-
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 Rhodobacter capsulatus
1.3.7.7 36000
-
2 * 36000, S-tag subunit BchL, SDS-PAGE Rhodobacter capsulatus
1.3.7.7 36046
-
2 * 36046, subunit BchL calculated from amino acid sequence Rhodobacter capsulatus
1.3.7.7 48671
-
2 * 48671 + 2 * 57191, subunit BchN and subunit BchB, calculated from amino acid sequence Rhodobacter capsulatus
1.3.7.7 52000
-
2 * 52000 + 2 * 60000, NB-protein complex, SDS-PAGE Rhodobacter capsulatus
1.3.7.7 57191
-
2 * 48671 + 2 * 57191, subunit BchN and subunit BchB, calculated from amino acid sequence Rhodobacter capsulatus
1.3.7.7 60000
-
2 * 52000 + 2 * 60000, NB-protein complex, SDS-PAGE Rhodobacter capsulatus
1.3.7.7 67000
-
S-tag subunit BchL, gel filtration Rhodobacter capsulatus
1.3.7.7 200000
-
NB-protein complex, gel filtration Rhodobacter capsulatus

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.33 Rhodobacter capsulatus
-
-
-
1.3.7.7 Rhodobacter capsulatus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.33 both activities of the components protein L and proteins NB are rapidly lost during purification procedures, such as affinity chromatography with S-protein agarose. Attempts to purify the active components have so far been unsuccessful Rhodobacter capsulatus
1.3.7.7 S-protein agarose column chromatography Rhodobacter capsulatus

Storage Stability

EC Number Storage Stability Organism
1.3.1.33 enzyme in crude extracts stable for more than 6 months when maintained anaerobically at 4°C, with no significant loss of activity Rhodobacter capsulatus
1.3.7.7 4°C, NB- and L-protein subunits of the crude extract when maintained anaerobically, more than 6 months, remain stable with no significant loss of activity Rhodobacter capsulatus
1.3.7.7 4°C, NB- and L-protein subunits of the purified extract when maintained anaerobically, both activities of the components are rapidly lost during purification procedures such as affinity chromatography with S-protein agarose Rhodobacter capsulatus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.33 protochlorophyllide + NADPH
-
Rhodobacter capsulatus chlorophyllide + NADP+
-
?
1.3.7.7 protochlorophyllide + oxidized ferredoxin + ADP + phosphate
-
Rhodobacter capsulatus chlorophyllide a + reduced ferredoxin + ATP
-
?

Subunits

EC Number Subunits Comment Organism
1.3.1.33 ? 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 Rhodobacter capsulatus
1.3.1.33 More recombinant enzyme component L-protein forms a dimer, recombinant components NB-protein form a heterotetramer, gel filtration Rhodobacter capsulatus
1.3.7.7 heterotetramer 2 * 48671 + 2 * 57191, subunit BchN and subunit BchB, calculated from amino acid sequence Rhodobacter capsulatus
1.3.7.7 heterotetramer 2 * 52000 + 2 * 60000, NB-protein complex, SDS-PAGE Rhodobacter capsulatus
1.3.7.7 homodimer 2 * 36000, S-tag subunit BchL, SDS-PAGE Rhodobacter capsulatus
1.3.7.7 homodimer 2 * 36046, subunit BchL calculated from amino acid sequence Rhodobacter capsulatus

Synonyms

EC Number Synonyms Comment Organism
1.3.1.33 DPOR
-
Rhodobacter capsulatus
1.3.7.7 dark-operative protochlorophyllide reductase
-
Rhodobacter capsulatus
1.3.7.7 DPOR
-
Rhodobacter capsulatus
1.3.7.7 light-independent Pchlide oxidoreductase
-
Rhodobacter capsulatus

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.33 Ferredoxin
-
Rhodobacter capsulatus
1.3.7.7 ADP
-
Rhodobacter capsulatus