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Literature summary for 1.18.1.2 extracted from

  • Ittarat, W.; Sato, T.; Kitashima, M.; Sakurai, H.; Inoue, K.; Seo, D.
    Rubredoxin from the green sulfur bacterium Chlorobaculum tepidum donates a redox equivalent to the flavodiiron protein in an NAD(P)H dependent manner via ferredoxin-NAD(P)+ oxidoreductase (2021), Arch. Microbiol., 203, 799-808 .
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
rubredoxin substrate inhibition is observed with electron donor NADPH Bacillus subtilis
rubredoxin substrate inhibition is observed with electron donor NADPH, but not with NADH Chlorobaculum tepidum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0195
-
oxidized [2Fe-2S]-[rubredoxin] cosubstrate NADH, pH 7, 25°C Chlorobaculum tepidum
0.021
-
oxidized [2Fe-2S]-[rubredoxin] cosubstrate NADPH, pH 7, 25°C Bacillus subtilis
0.032
-
oxidized [2Fe-2S]-[rubredoxin] cosubstrate NADPH, pH 7, 25°C Chlorobaculum tepidum
0.207
-
NADH pH 7, 25°C Chlorobaculum tepidum

Organism

Organism UniProt Comment Textmining
Bacillus subtilis O05268
-
-
Bacillus subtilis 168 O05268
-
-
Chlorobaculum tepidum Q8KCB2
-
-
Chlorobaculum tepidum DSM 12025 Q8KCB2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information enzyme catalyzes the reduction of rubredoxin at rates comparable to those reported for NADH-rubredoxin oxidoreductases. At high concentrations, substrate inhibition is observed with electron donor NADPH Bacillus subtilis ?
-
-
additional information enzyme catalyzes the reduction of rubredoxin at rates comparable to those reported for NADH-rubredoxin oxidoreductases. At high concentrations, substrate inhibition is observed with electron donor NADPH, but not with NADH Chlorobaculum tepidum ?
-
-
additional information enzyme catalyzes the reduction of rubredoxin at rates comparable to those reported for NADH-rubredoxin oxidoreductases. At high concentrations, substrate inhibition is observed with electron donor NADPH Bacillus subtilis 168 ?
-
-
additional information enzyme catalyzes the reduction of rubredoxin at rates comparable to those reported for NADH-rubredoxin oxidoreductases. At high concentrations, substrate inhibition is observed with electron donor NADPH, but not with NADH Chlorobaculum tepidum DSM 12025 ?
-
-
NADH + 2 oxidized [2Fe-2S]-[ferredoxin]
-
Bacillus subtilis H+ + NAD+ + 2 reduced [2Fe-2S]-[ferredoxin]
-
?
NADH + 2 oxidized [2Fe-2S]-[ferredoxin]
-
Bacillus subtilis 168 H+ + NAD+ + 2 reduced [2Fe-2S]-[ferredoxin]
-
?
NADH + 2 oxidized [2Fe-2S]-[rubredoxin]
-
Bacillus subtilis H+ + NAD+ + 2 reduced [2Fe-2S]-[rubredoxin]
-
?
NADH + 2 oxidized [2Fe-2S]-[rubredoxin]
-
Chlorobaculum tepidum H+ + NAD+ + 2 reduced [2Fe-2S]-[rubredoxin]
-
?
NADH + 2 oxidized [2Fe-2S]-[rubredoxin]
-
Bacillus subtilis 168 H+ + NAD+ + 2 reduced [2Fe-2S]-[rubredoxin]
-
?
NADH + 2 oxidized [2Fe-2S]-[rubredoxin]
-
Chlorobaculum tepidum DSM 12025 H+ + NAD+ + 2 reduced [2Fe-2S]-[rubredoxin]
-
?
NADPH + 2 oxidized [2Fe-2S]-[rubredoxin]
-
Bacillus subtilis H+ + NADP+ + 2 reduced [2Fe-2S]-[rubredoxin]
-
?
NADPH + 2 oxidized [2Fe-2S]-[rubredoxin]
-
Chlorobaculum tepidum H+ + NADP+ + 2 reduced [2Fe-2S]-[rubredoxin]
-
?
NADPH + 2 oxidized [2Fe-2S]-[rubredoxin]
-
Bacillus subtilis 168 H+ + NADP+ + 2 reduced [2Fe-2S]-[rubredoxin]
-
?
NADPH + 2 oxidized [2Fe-2S]-[rubredoxin]
-
Chlorobaculum tepidum DSM 12025 H+ + NADP+ + 2 reduced [2Fe-2S]-[rubredoxin]
-
?

Synonyms

Synonyms Comment Organism
CT1512
-
Chlorobaculum tepidum
FNR
-
Chlorobaculum tepidum
YumC
-
Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
16.5
-
oxidized [2Fe-2S]-[rubredoxin] cosubstrate NADH, pH 7, 25°C Chlorobaculum tepidum
24.8
-
oxidized [2Fe-2S]-[rubredoxin] cosubstrate NADPH, pH 7, 25°C Chlorobaculum tepidum
34.7
-
NADH pH 7, 25°C Chlorobaculum tepidum
255
-
oxidized [2Fe-2S]-[rubredoxin] cosubstrate NADPH, pH 7, 25°C Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
NADH
-
Bacillus subtilis
NADH
-
Chlorobaculum tepidum
NADPH
-
Bacillus subtilis
NADPH
-
Chlorobaculum tepidum