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Literature summary for 1.6.5.9 extracted from

  • Mogi, T.; Matsushita, K.; Murase, Y.; Kawahara, K.; Miyoshi, H.; Ui, H.; Shiomi, K.; Omura, S.; Kita, K.
    Identification of new inhibitors for alternative NADH dehydrogenase (NDH-II): Research Letter (2009), FEMS Microbiol. Lett., 291, 157-161.
    View publication on PubMed
Search for more literature for 1.6.5.9

Inhibitors

Inhibitors Comment Organism Structure
1-hydroxy-2-dodecyl-4(1H)quinolone 28% residual activity at 0.01 mM Gluconobacter oxydans
aculeacin A 63% residual activity at 0.005 mg/ml Gluconobacter oxydans
aurachin C 1-10 12% residual activity at 0.01 mM, noncompetitive inhibitor Gluconobacter oxydans
funiculosin 68% residual activity at 0.005 mg/ml Gluconobacter oxydans
Gramicidin S 31% residual activity at 0.005 mg/ml Gluconobacter oxydans
polymixin B 51% residual activity at 0.005 mg/ml Gluconobacter oxydans
scopafungin 33% residual activity at 0.005 mg/ml, noncompetitive inhibitor Gluconobacter oxydans
staurosporine 70% residual activity at 0.005 mg/ml Gluconobacter oxydans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.157
-
 NADH at 25°C in 100mM Tris-HCl (pH 7.4) Gluconobacter oxydans

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasmic membrane NDH-II is bound peripherally to the inner surface of the cytoplasmic membrane Gluconobacter oxydans
-
-

Organism

Organism UniProt Comment Textmining
Gluconobacter oxydans
-
 formerly Gluconobacter suboxydans strain IFO12528
-
Gluconobacter oxydans NBRC3172
-
 formerly Gluconobacter suboxydans strain IFO12528
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information NDH-II does not pump protons Gluconobacter oxydans ?
-
 ?
additional information NDH-II does not pump protons Gluconobacter oxydans NBRC3172 ?
-
 ?
NADH + H+ + ubiquinone-1
-
 Gluconobacter oxydans NAD+ + ubiquinol-1
-
 ?
NADH + H+ + ubiquinone-1
-
 Gluconobacter oxydans NBRC3172 NAD+ + ubiquinol-1
-
 ?

Synonyms

Synonyms Comment Organism
alternative NADH:quinone reductase
-
 Gluconobacter oxydans
NDH-II
-
 Gluconobacter oxydans

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Gluconobacter oxydans

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.0014
-
 Gramicidin S at 25°C in 100mM Tris-HCl (pH 7.4) Gluconobacter oxydans
0.0055
-
 scopafungin at 25°C in 100mM Tris-HCl (pH 7.4) Gluconobacter oxydans

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.00034
-
 at 25°C in 100mM Tris-HCl (pH 7.4) Gluconobacter oxydans aurachin C 1-10
0.0012
-
 at 25°C in 100mM Tris-HCl (pH 7.4) Gluconobacter oxydans Gramicidin S
0.0017
-
 at 25°C in 100mM Tris-HCl (pH 7.4) Gluconobacter oxydans 1-hydroxy-2-dodecyl-4(1H)quinolone
0.0062
-
 at 25°C in 100mM Tris-HCl (pH 7.4) Gluconobacter oxydans scopafungin

General Information

General Information Comment Organism
physiological function NDH-II is a key enzyme for the regeneration of an oxidized form of NAD Gluconobacter oxydans