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- W2162536024 abstract "d(−)-β-hydroxybutyrate dehydrogenase (BOHB-DH) (EC 1.1.1.30) was purified 991-fold from Azospirillum brasilense Cd. Its specific activity was 5650 units (mg protein)−1 min−1. The enzyme is a tetramer, with identical subunits and a total molecular mass of 100 kDa. BOHB-DH is not a glycoprotein. It is acidic and contains six disulphide bonds without free -SH groups. Under the assay conditions used, BOHB-DH activity was maximal at pH 8·0 and at 36 °C. The enzyme is an NAD+ oxidoreductase, and is inhibited by NADPH and NADH. It has high affinity for β-hydroxybutyrate: the K m value for the β-hydroxybutyrate substrate is 1 mm. Adenosine phosphates, pyruvate, acetyl-coenzyme A, oxaloacetate and 2-oxoglutarate inhibited purified BOHB-DH." @default.
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- W2162536024 date "1990-04-01" @default.
- W2162536024 modified "2023-10-12" @default.
- W2162536024 title "Purification and characterization of D(--)- -hydroxybutyrate dehydrogenase from Azospirillum brasilense Cd" @default.
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- W2162536024 doi "https://doi.org/10.1099/00221287-136-4-645" @default.
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