Homicide followed by freezing and burning: Usefulness of measuring SCHAD (short-chain 3-hydroxyacyl-CoA dehydrogenase) activity

2006 ◽  
Vol 13 (6-8) ◽  
pp. 339-340 ◽  
Author(s):  
L. Fanton ◽  
H. Yappo-Ette ◽  
C. Vianey-Saban ◽  
D. Malicier
Keyword(s):  
Dehydrogenase Activity ◽  
Short Chain ◽  
Hydroxyacyl Coa Dehydrogenase

scholarly journals Acyl-CoA dehydrogenase activity in the riboflavin-deficient rat. Effects of starvation

1987 ◽  
Vol 244 (2) ◽  
pp. 387-391 ◽  
Author(s):  
N S Ross ◽  
C L Hoppel
Keyword(s):  
Fatty Acid ◽  
Dehydrogenase Activity ◽  
Fatty Acid Oxidation ◽  
Specific Activity ◽  
Short Chain ◽  
Acid Oxidation ◽  
Riboflavin Deficiency ◽  
Mitochondrial Fatty Acid ◽  
Chain Acyl ◽  
Riboflavin Deficient

Riboflavin deficiency in weanling rats causes a metabolic disorder characterized by failure to oxidize fatty acids. The disorder is similar to that seen in several human diseases, some of which are responsive to pharmacological doses of riboflavin. Previous analysis of the riboflavin-deficient rat has shown that the failure of fatty acid oxidation is due to a decrease in the activity of the acyl-CoA dehydrogenases of beta-oxidation. The activity of these flavoenzymes in liver rapidly decreases when a riboflavin-deficient diet is initiated. The objectives of these experiments were to analyse the effects of starvation on liver mitochondria isolated from the riboflavin-deficient rat. Our studies show that the decreased mitochondrial fatty acid oxidation induced by riboflavin deficiency is partially reversed by starvation. The extent of this reversal is proportional to the duration of starvation. The starvation-associated increase in fatty acid oxidation is mediated by an increase in the mitochondrial short-chain acyl-CoA dehydrogenase activity. The activity of this enzyme is increased such that the ratio of short-chain acyl-CoA dehydrogenase apoenzyme to holoenzyme does not change. We conclude that short-chain acyl-CoA dehydrogenase activity is limiting for fatty acid oxidation when its activity falls below a critical point. The increased mitochondrial specific activity of short-chain acyl-CoA dehydrogenase during starvation may result from an increased availability of flavin coenzyme or an increase in enzyme catalytic efficiency.

Structural organization of the human short-chain l -3-hydroxyacyl-CoA dehydrogenase gene HADHSC pseudogene sequence, AF026868.-->

1998 ◽  
Vol 9 (9) ◽  
pp. 763-768 ◽  
Author(s):  
Patrick J.C.M. Vredendaal ◽  
Inge E.T. van den Berg ◽  
An K. Stroobants ◽  
Daphne L. van der A ◽  
Helga E.M. Malingré ◽  
...  
Keyword(s):  
Structural Organization ◽  
Short Chain ◽  
Dehydrogenase Gene ◽  
Hydroxyacyl Coa Dehydrogenase

Diagnosis of a patient with a kinetic variant of medium and short-chain 3-hydroxyacyl-CoA dehydrogenase deficiency by newborn screening

2012 ◽  
Vol 106 (3) ◽  
pp. 277-280 ◽  
Author(s):  
Laura Vilarinho ◽  
Jorge Sales Marques ◽  
Hugo Rocha ◽  
Altina Ramos ◽  
Lurdes Lopes ◽  
...  
Keyword(s):  
Newborn Screening ◽  
Dehydrogenase Deficiency ◽  
Short Chain ◽  
Hydroxyacyl Coa Dehydrogenase

scholarly journals β-hydroxyacyl-CoA-dehydrogenase activity differentiates unfrozen from frozen-thawed Yellowfin tuna (Thunnus albacares)

2019 ◽  
Vol 8 (3) ◽  
Author(s):  
Cristian Bernardi ◽  
Erica Tirloni ◽  
Simone Stella ◽  
Aniello Anastasio ◽  
Patrizia Cattaneo ◽  
...  
Keyword(s):  
Dehydrogenase Activity ◽  
Statistical Approach ◽  
Threshold Value ◽  
Critical Value ◽  
Yellowfin Tuna ◽  
Thunnus Albacares ◽  
Probability Level ◽  
Statistical Algorithm ◽  
Hydroxyacyl Coa Dehydrogenase

Changes in the β-hydroxyacyl-CoAdehydrogenase (HADH) activity of fresh and frozen-thawed Yellowfin tuna were examined. A statistical approach to HADH activities determined in press juice allowed to set a critical value to differentiate fresh from frozen-thawed Yellowfin tuna: the threshold value was 3.7 U mL-1 at the probability level of 1%. The analysis of 37 tuna (not ready to eat) sampled on retail revealed the unconformity to labelling of 4 samples. A simple statistical algorithm was built to get probabilities from observed values on tuna of being or not frozen/thawed.

Acyl-CoA dehydrogenase activity in pea cotyledon tissue during germination and initial growth

2000 ◽  
Vol 28 (6) ◽  
pp. 760-762 ◽  
Author(s):  
C. Masterson ◽  
A. Blackburn ◽  
C. Wood
Keyword(s):  
Dehydrogenase Activity ◽  
Chain Length ◽  
Root Formation ◽  
Short Chain ◽  
Initial Growth ◽  
Chain Acyl ◽  
Pea Seeds ◽  
Acyl Coa Dehydrogenases ◽  
Hydroponically Grown ◽  
Long Chain

Acyl-CoA dehydrogenase activity has been measured in homogenates of post-imbibition to 14-day-old hydroponically grown pea seeds at daily intervals, using C4, C12 and C16 acyl-CoA substrates. The activity peaks of the different chain-length acyl-CoA dehydrogenases did not transpose at all points and the ratios of the chain-length activities were not constant. It therefore has to be concluded that more than one dehydrogenase is present in pea mitochondria. There was a post-imbibition initial surge of activity with short- and mid-chain-length substrates. The C16- handling enzyme first peaked at 3–4 days, which coincided with the onset of plumule unfurling and greening. Further peaks were observed with all three substrates, coinciding with secondary root formation and leaf enlargement and later with cotyledon degeneration. Overall activity showed that the long-chain acyl-CoA dehydrogenase was much more active than the short-chain acyl-CoA dehydrogenase.

scholarly journals Intrinsic alcohol dehydrogenase and hydroxysteroid dehydrogenase activities of human mitochondrial short-chain L-3-hydroxyacyl-CoA dehydrogenase

1999 ◽  
Vol 345 (1) ◽  
pp. 139-143 ◽  
Author(s):  
Xue-Ying HE ◽  
Ying-Zi YANG ◽  
Horst SCHULZ ◽  
Song-Yu YANG
Keyword(s):  
Alcohol Dehydrogenase ◽  
Catalytic Properties ◽  
Amyloid Β ◽  
Hydroxysteroid Dehydrogenase ◽  
Amino Acid Sequences ◽  
Short Chain ◽  
Amyloid Β Peptide ◽  
Kinetic Measurements ◽  
Hydroxyacyl Coa Dehydrogenase ◽  
Adh Activity

The alcohol dehydrogenase (ADH) activity of human short-chain L-3-hydroxyacyl-CoA dehydrogenase (SCHAD) has been characterized kinetically. The kcat of the purified enzyme was estimated to be 2.2 min-1, with apparent Km values of 280 mM and 22μM for 2-propanol and NAD+, respectively. The kcat of the ADH activity was three orders of magnitude less than the L-3-hydroxyacyl-CoA dehydrogenase activity but was comparable with that of the enzyme's hydroxysteroid dehydrogenase (HSD) activity for oxidizing 17β-oestradiol [He, Merz, Mehta, Schulz and Yang (1999) J. Biol. Chem. 274, 15014-15019]. However, the kcat values of intrinsic ADH and HSD activities of human SCHAD were found to be two orders of magnitude less than those reported for endoplasmic-reticulum-associated amyloid β-peptide-binding protein (ERAB) [Yan, Shi, Zhu, Fu, Zhu, Zhu, Gibson, Stern, Collison, Al-Mohanna et al. (1999) J. Biol. Chem. 274, 2145-2156]. Since human SCHAD and ERAB apparently possess identical amino acid sequences, their catalytic properties should be identical. The recombinant SCHAD has been confirmed to be the right gene product and not a mutant variant. Steady-state kinetic measurements and quantitative analyses reveal that assay conditions such as pH and concentrations of coenzyme and substrate do not account for the kinetic differences reported for ERAB and SCHAD. Rather problematic experimental procedures appear to be responsible for the unrealistically high catalytic rate constants of ERAB. Eliminating the confusion surrounding the catalytic properties of this important multifunctional enzyme paves the way for exploring its role(s) in the pathogenesis of Alzheimer's disease.

scholarly journals Short-Chain Acyl-Coenzyme A Dehydrogenase Activity, Antigen, and Biosynthesis Are Absent in the BALB/cByJ Mouse

1992 ◽  
Vol 31 (6) ◽  
pp. 552-556 ◽  
Author(s):  
Brad A Amendt ◽  
Eric Freneaux ◽  
Cameron Reece ◽  
Philip A Wood ◽  
William J Rhead
Keyword(s):  
Dehydrogenase Activity ◽  
Coenzyme A ◽  
Short Chain ◽  
Chain Acyl ◽  
Acyl Coenzyme A
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