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BDH1 3-hydroxybutyrate dehydrogenase, type 1

3-hydroxybutyrate dehydrogenase, D-beta-hydroxybutyrate dehydrogenase
Top mentioned proteins: CAN, ACID, HAD, OUT, Insulin
Papers on 3-hydroxybutyrate dehydrogenase
3-Hydroxybutyrate dehydrogenase-2 and ferritin-H synergistically regulate intracellular iron.
Devireddy et al., Cleveland, United States. In Febs J, 2014
A member of the short-chain dehydrogenase family of reductases, 3-hydroxybutyrate dehydrogenase-2, catalyzes a rate-limiting step in the biogenesis of the mammalian siderophore.
Closed complex of the D-3-hydroxybutyrate dehydrogenase induced by an enantiomeric competitive inhibitor.
Yoshimoto et al., Nagasaki, Japan. In J Biochem, 2009
D-3-Hydroxybutyrate dehydrogenase (HBDH) from Pseudomonas fragi showed a strict stereospecificity to the d-enantiomer of 3-hydroxybutyrate (d-3-HB) as a substrate.
The structures of Alcaligenes faecalis D-3-hydroxybutyrate dehydrogenase before and after NAD+ and acetate binding suggest a dynamical reaction mechanism as a member of the SDR family.
Takénaka et al., Yokohama, Japan. In Acta Crystallogr D Biol Crystallogr, 2008
D-3-Hydroxybutyrate dehydrogenase, which catalyzes the reversible reaction between D-3-hydroxybutyrate and acetoacetate, has been classified into the short-chain dehydrogenase/reductase family and is a useful marker in the assay of diabetes mellitus and/or ketoacidosis.
Cosubstrate-induced dynamics of D-3-hydroxybutyrate dehydrogenase from Pseudomonas putida.
Sträter et al., Leipzig, Germany. In Febs J, 2007
D-3-Hydroxybutyrate dehydrogenase from Pseudomonas putida belongs to the family of short-chain dehydrogenases/reductases. We have determined X-ray structures of the D-3-hydroxybutyrate dehydrogenase from Pseudomonas putida, which was recombinantly expressed in Escherichia coli, in three different crystal forms to resolutions between 1.9 and 2.1 A. The so-called substrate-binding loop (residues 187-210) was partially disordered in several subunits, in both the presence and absence of NAD(+).
Molecular basis of substrate recognition in D-3-hydroxybutyrate dehydrogenase from Pseudomonas putida.
Grunow et al., Leipzig, Germany. In Chembiochem, 2006
D-3-Hydroxybutyrate dehydrogenase from Pseudomonas putida (EC
Metabolic organization of the spotted ratfish, Hydrolagus colliei (Holocephali: Chimaeriformes): insight into the evolution of energy metabolism in the chondrichthyan fishes.
Ballantyne et al., Guelph, Canada. In J Exp Zool A Comp Exp Biol, 2006
High activities in oxidative tissues of enzymes of ketone body metabolism, including D-beta-hydroxybutyrate dehydrogenase, indicate that, like elasmobranchs, ketone bodies are of central importance in spotted ratfish.
Metabolic organization of freshwater, euryhaline, and marine elasmobranchs: implications for the evolution of energy metabolism in sharks and rays.
Ballantyne et al., Guelph, Canada. In J Exp Biol, 2006
D-beta-hydroxybutyrate dehydrogenase (d-beta-HBDH) was high in most tissues confirming the importance of ketone bodies in elasmobranchs.
Characterization of two D-beta-hydroxybutyrate dehydrogenase populations in heavy and light mitochondria from jerboa (Jaculus orientalis) liver.
El Kebbaj et al., Casablanca, Morocco. In Comp Biochem Physiol B Biochem Mol Biol, 2006
Mitochondrial membrane-bound and phospholipid-dependent D-beta-hydroxybutyrate dehydrogenase (BDH) (EC,
Trigonella foenum graecum seed powder protects against histopathological abnormalities in tissues of diabetic rats.
Baquer et al., New Delhi, India. In Mol Cell Biochem, 2004
The activity of the enzyme, glutamate dehydrogenase was significantly higher whereas the activity of D-beta-hydroxybutyrate dehydrogenase enzyme was significantly lower in liver and kidney of alloxan-induced diabetic rats.
Purification and characterization of the D-beta-hydroxybutyrate dehydrogenase from dromedary liver mitochondria.
Latruffe et al., Settat, Morocco. In Comp Biochem Physiol B Biochem Mol Biol, 2002
D-beta-hydroxybutyrate dehydrogenase (BDH) (EC,
(R)-3-hydroxybutyrate dehydrogenase: selective phosphatidylcholine binding by the C-terminal domain.
McIntyre et al., Nashville, United States. In Biochemistry, 2000
(R)-3-Hydroxybutyrate dehydrogenase (BDH) is a lipid-requiring mitochondrial enzyme that has a specific requirement of phosphatidylcholine (PC) for function.
The short-chain alcohol dehydrogenase superfamily: variations on a common theme.
Krozowski, Australia. In J Steroid Biochem Mol Biol, 1994
It can be shown that the 17 beta-hydroxysteroid dehydrogenase type 2 enzyme is more closely related to D-beta-hydroxybutyrate dehydrogenase than it is to 17 beta-hydroxysteroid dehydrogenase type 1. Carbonyl reductase, previously considered to be a member of the aldo-keto reductase superfamily, displayed high homology in the conserved domains and is clearly part of the SCAD superfamily despite the insertion of a large peptide between conserved domains.
Flow-injection determination of 3-hydroxybutyrate in serum with an immobilized 3-hydroxybutyrate dehydrogenase reactor and fluorescence detection.
Furusawa et al., Kōfu, Japan. In Talanta, 1994
3-Hydroxybutyrate dehydrogenase is immobilized on aminated poly(vinyl alcohol) beads and packed into a stainless-steel column (4 cm x 4 mm I.D.).
Lipid-protein interactions in biomembranes studied through the phospholipid specificity of D-beta-hydroxybutyrate dehydrogenase.
el Kebbaj et al., In Biochimie, 1986
This paper reports essential results obtained these last few years with D-beta-hydroxybutyrate dehydrogenase (BDH) from inner mitochondrial membrane, one of the most interesting and best documented examples of a lipid-requiring enzyme.
The effects of osmotic lysis on the oxidative phosphorylation and compartmentation of rat liver mitochondria.
Greenawalt et al., Baltimore, United States. In J Cell Biol, 1968
Assays for protein, malate dehydrogenase, D-beta-hydroxybutyrate dehydrogenase, and succinate dehydrogenase indicated that the inner compartment could be clearly separated from the outer membrane vesicles.
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