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Literature summary for 1.1.1.30 extracted from

  • Hoque, M.M.; Shimizu, S.; Juan, E.C.; Sato, Y.; Hossain, M.T.; Yamamoto, T.; Imamura, S.; Suzuki, K.; Amano, H.; Sekiguchi, T.; Tsunoda, M.; Takenaka, A.
    Structure of D-3-hydroxybutyrate dehydrogenase prepared in the presence of the substrate D-3-hydroxybutyrate and NAD+ (2009), Acta Crystallogr. Sect. F, 65, 331-335.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Alcaligenes faecalis

Crystallization (Commentary)

Crystallization (Comment) Organism
in the presence of the substrate D-3-hydroxybutyrate and the cofactor NAD+ at the optimum pH for the catalytic reaction. At 277 and 293 K using the hanging-drop vapour-diffusion method, to 2.3 A resolution. Structure is isomorphous to that of the complex with the substrate analogue acetate Alcaligenes faecalis

Organism

Organism UniProt Comment Textmining
Alcaligenes faecalis D0VWQ0
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-

Purification (Commentary)

Purification (Comment) Organism
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Alcaligenes faecalis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-3-hydroxybutyrate + NAD+ the reversible reactions occur by shuttle movements of a hydrogen negative ion from the C3 atom of the substrate to the C4 atom of NAD+ and from the C4 atom of NADH to the C3 atom of the product. The reaction may be further coupled to the withdrawal of a proton from the hydroxyl group of the substrate by the ionized Tyr155 residue Alcaligenes faecalis acetoacetate + NADH + H+
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r

Subunits

Subunits Comment Organism
tetramer
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Alcaligenes faecalis

Synonyms

Synonyms Comment Organism
HBDH
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Alcaligenes faecalis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Alcaligenes faecalis

Cofactor

Cofactor Comment Organism Structure
NAD+
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Alcaligenes faecalis
NADH
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Alcaligenes faecalis