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Literature summary extracted from

  • Wagener, N.; Pierik, A.J.; Ibdah, A.; Hille, R.; Dobbek, H.
    The Mo-Se active site of nicotinate dehydrogenase (2009), Proc. Natl. Acad. Sci. USA, 106, 11055-11060.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.17.1.5
-
Eubacterium barkeri

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.17.1.5 23000
-
dimer of heterotetramers, subunits of the heterotetramer: 1 * 50000 + 1 * 37000 + 1* 33000 + 1 * 23000, X-ray diffraction Eubacterium barkeri
1.17.1.5 37000
-
dimer of heterotetramers, subunits of the heterotetramer: 1 * 50000 + 1 * 37000 + 1* 33000 + 1 * 23000, X-ray diffraction Eubacterium barkeri
1.17.1.5 50000
-
dimer of heterotetramers, subunits of the heterotetramer: 1 * 50000 + 1 * 37000 + 1* 33000 + 1 * 23000, X-ray diffraction Eubacterium barkeri

Organism

EC Number Organism UniProt Comment Textmining
1.17.1.5 Eubacterium barkeri Q0QLF2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.17.1.5
-
Eubacterium barkeri

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.1.5 nicotinate + H2O + NADP+
-
Eubacterium barkeri 6-hydroxynicotinate + NADPH
-
?

Subunits

EC Number Subunits Comment Organism
1.17.1.5 octamer dimer of heterotetramers, subunits of the heterotetramer: 1 * 50000 + 1 * 37000 + 1* 33000 + 1 * 23000, X-ray diffraction Eubacterium barkeri

Synonyms

EC Number Synonyms Comment Organism
1.17.1.5 NDH
-
Eubacterium barkeri
1.17.1.5 nicotinate dehydrogenase
-
Eubacterium barkeri