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Literature summary for 7.1.1.2 extracted from

  • Matsushita, K.; Otofuji, A.; Iwahashi, M.; Toyama, H.; Adachi, O.
    NADH dehydrogenase of Corynebacterium glutamicum. Purification of an NADH dehydrogenase II homolog able to oxidize NADPH (2001), FEMS Microbiol. Lett., 204, 271-276.
    View publication on PubMed
Search for more literature for 7.1.1.2

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Corynebacterium glutamicum 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
55000
-
 x * 55000, SDS-PAGE Corynebacterium glutamicum

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Corynebacterium glutamicum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ubiquinone-1 + NADH + H+ the protein shows NADH-ubiquinone-1 oxidoreductase activity, NADPH oxidase (EC 1.6.3.1) and NADPH-ubiquinone-1 oxidoreductase (EC 1.6.5.2) activities Corynebacterium glutamicum ubiquinol-1 + NAD+
-
 ?

Subunits

Subunits Comment Organism
? x * 55000, SDS-PAGE Corynebacterium glutamicum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Corynebacterium glutamicum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
 Corynebacterium glutamicum

pH Range

pH Minimum pH Maximum Comment Organism
5.5 7.5 pH 5.5: about 80% of maximal activity, pH 7.5: about 85% of maximal activity Corynebacterium glutamicum

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Corynebacterium glutamicum