Purification and properties of crystalline 3-hydroxybutyrate dehydrogenase from <i>Rhodopseudomonas spheroides</i>

Bergmeyer, H.U.; Gawehn, Karlfried; Klotzsch, Helmut; Krebs, Harald; Williamson, D.

doi:10.1042/bj1020423

Cited by 97 publications

(52 citation statements)

References 14 publications

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“…From the amino acid composition a molecular mass of 106 kDa was calculated. A similar molecular mass was reported for Azotobacter beijerinckii BOHB-DH ) and a value of 85 kDa was reported for the Rhodopseudomonas spheroides enzyme (Bergmeyer et al, 1967). The amino acid composition (Table 2) shows that the protein is rich in acidic amino acids and has only 12 half-cysteines (six 0.2 0.4 0.6 NAD(P)H concn (mM) Fig.…”

Section: Amino Acidsupporting

confidence: 78%

“…1 .30) which catalyses the oxidation reduction reaction between 1-hydroxybutyrate and acetoacetate in the PHB cycle has a key role in the degradation of PHB and in regulation of PHB and in regulation of PHB synthesis and degradation. This enzyme has been studied from various sources (Delafield et al, 1965;Jurtshuk et al, 1968;Bergmeyer et al, 1967;Kovar et al, 1986). It has been found in mammals, where it is involved in degradation of pfl-hydroxybutyrate during starvation periods or diabetes.…”

Section: Introductionmentioning

confidence: 99%

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Purification and characterization of D(--)- -hydroxybutyrate dehydrogenase from Azospirillum brasilense Cd

Tal¹,

Smirnoff²,

Okon³

1990

Journal of General Microbiology

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D ( -)-0-hydroxybutyrate dehydrogenase (BOHB-DH) (EC 1.1.1.30) was puri6ed 991-fold from Azospidlum brasilense Cd. Its specific activity was 5650 units (mg protein)-l min-'. 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 S H groups. Under the assay conditions used, BOHB-DH activity was maximal at pH 8.0 and at 36 OC. The enzyme is an NAD+ oxidoreductase, and is inhibited by NADPH and NADH. It has high affinity for P-hydroxybutyrate: the K, value for the P-hydroxybutyrate substrate is 1 mM. Adenosine phosphates, pyruvate, acetyl-coenzyme A, oxaloacetate and 2-oxoglutarate inhibited purified BOHB-DH.

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Section: Amino Acidsupporting

confidence: 78%

Section: Introductionmentioning

confidence: 99%

Purification and characterization of D(--)- -hydroxybutyrate dehydrogenase from Azospirillum brasilense Cd

Tal¹,

Smirnoff²,

Okon³

1990

Journal of General Microbiology

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“…Similarly, 3-hydroxybutyrate dehydrogenase (3HBDH) was expressed at a higher level in testosterone-treated individuals in both sexes and both tissues. 3HBDH catalyzes the reversible reaction between beta-hydroxybutyric acid and acetoacetate, a key step in the breakdown of fatty acids for energy (Bergmeyer et al, 1967;Williamson et al, 1962). Both male and female rats respond to androgen treatment with changes in the expression of fatty acid metabolizing genes as well (van Nas et al, 2009).…”

Section: Effect Of Testosterone Treatment In Both Sexesmentioning

confidence: 99%

Potential for sexual conflict assessed via testosterone-mediated transcriptional changes in liver and muscle of a songbird

Peterson

Rosvall

Taylor

et al. 2013

Journal of Experimental Biology

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Males and females can be highly dimorphic in metabolism and physiology despite sharing nearly identical genomes, and both sexes respond phenotypically to elevated testosterone, a steroid hormone that alters gene expression. Only recently has it become possible to learn how a hormone such as testosterone affects global gene expression in non-model systems, and whether it affects the same genes in males and females. To investigate the transcriptional mechanisms by which testosterone exerts its metabolic and physiological effects on the periphery, we compared gene expression by sex and in response to experimentally elevated testosterone in a well-studied bird species, the dark-eyed junco (Junco hyemalis). We identified 291 genes in the liver and 658 in the pectoralis muscle that were differentially expressed between males and females. In addition, we identified 1727 genes that were differentially expressed between testosterone-treated and control individuals in at least one tissue and sex. Testosterone treatment altered the expression of only 128 genes in both males and females in the same tissue, and 847 genes were affected significantly differently by testosterone treatment in the two sexes. These substantial differences in transcriptional response to testosterone suggest that males and females may employ different pathways when responding to elevated testosterone, despite the fact that many phenotypic effects of experimentally elevated testosterone are similar in both sexes. In contrast, of the 121 genes that were affected by testosterone treatment in both sexes, 78% were regulated in the same direction (e.g. either higher or lower in testosteronetreated than control individuals) in both males and females. Thus, it appears that testosterone acts through both unique and shared transcriptional pathways in males and females, suggesting multiple mechanisms by which sexual conflict can be mediated.

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“…From the experimental data it was possible to estimate pK a1 = 4.0, pK a2 = 10.2. These constants can be attributed to the aspartic acid (pK a 3.9) or glutamic acid (pK a 4.0) and Tyrosine (10.46) respectively [43]. In fact, near the catalytic center there is one residue that has an important paper in the catalysis, Trp155.…”

Section: Catalysis Of 3-β-hydroxybutyrate By Hbh Using a Screen-printmentioning

confidence: 99%

Use of a Simple Fabrication Process to Produce a Biosensor: The 3-Hydroxybutyrate Dehydrogenase Case

Ribau¹,

Fortunato²

2018

JPP

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This study was aimed to construct a biodegradable but reliable 3-β-hydroxybutyrate biosensor. In this context a versatile paper based biosensor, quickly, easily and cheaply fabricated is reported. The procedure of fabrication is based on the assumption that the introduction of the enzyme in the carbon ink will allow enzyme stabilization and facilitate the study of the catalysis of enzymes and the detection of substrates. To prove this concept we use the enzyme 3-hydroxybutyrate dehydrogenase, in aqueous solution. This enzyme was chosen because it catalyzes the 3-β-hydroxybutyrate, which results from ketoacidosis. The quantification this substance in the diabetics' blood is very important as it can increase the reliability of the diagnosis of glycaemia. To prove the multi-use of this biosensor we not only study the redox process in steady state and during the catalytic process, but also detected and quantify the 3-β-hydroxybutyrate. Our results showed that it was possible to study the redox process that occurred during the catalysis and to confirm the amino acid residues that participate in it. It was also observed that glucose and ascorbic acid can interfere in the detection and quantification of the 3-β-hydroxybutyrate, what should be in mind when the quantification of the 3-β-hydroxybutyrate is made in blood samples.

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Purification and properties of crystalline 3-hydroxybutyrate dehydrogenase from Rhodopseudomonas spheroides

Cited by 97 publications

References 14 publications

Purification and characterization of D(--)- -hydroxybutyrate dehydrogenase from Azospirillum brasilense Cd

Purification and characterization of D(--)- -hydroxybutyrate dehydrogenase from Azospirillum brasilense Cd

Potential for sexual conflict assessed via testosterone-mediated transcriptional changes in liver and muscle of a songbird

Use of a Simple Fabrication Process to Produce a Biosensor: The 3-Hydroxybutyrate Dehydrogenase Case

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