Hirsch HE, Parks ME, Blanco CE, Simpson DR (1982) The ratio of 3-hydroxyacyl-CoA de- hydrogenase to lipoamide dehydrogenase activity in individual muscle fibers: mitochon- drial specialization for source of energy. J Neurosci Res 8:7-12...
This protein, called YP10, showed a high degree (>90%) of sequence homology with l-3-hydroxyacyl-CoA dehydrogenase (HAD) and had a dehydrogenase activity similar to pig heart HAD, which was inhibited by GLUT4 C-terminus synthetic peptide. An antiserum raised against pig heart HAD also ...
Summary Peroxisomal β-oxidation proceeds from enoyl-CoA through d-3-hydroxyacyl-CoA to 3-ketoacyl-CoA by the d-3-hydroxyacyl-CoA dehydratase/d-3-hydroxy-acyl-CoA dehydrogenase bifunctional protein (d-bifunctional protein), and the oxidation of bile-acid precursors also has been suggested as bein...
Table 2. Fatty acid oxidation, acyl-CoA dehydrogenase, 3-ketoacyl-CoA thiolase, and 3-hydroxyacyl-CoA dehydrogenase activity measurements in cultured skin fibroblasts o fuatient and control subjects Activity measured Substrate Patient Controls (n = 5)* Fatty acid oxidation? [ 1-14C]-succ~nic [...
l-3-Hydroxyacyl-CoA dehydrogenase (HAD), the penultimate enzyme in the beta-oxidation spiral, reversibly catalyzes the conversion of l-3-hydroxyacyl-CoA to the corresponding 3-ketoacyl-CoA. Similar to other dehydrogenases, HAD contains a general acid/base, His(158), which is within hydrogen bon...
Background Loss of function mutations in 3-Hydroxyacyl-CoA Dehydrogenase (HADH) cause protein sensitive hyperinsulinaemic hypoglycaemia (HH). HADH encodes short chain 3-hydroxacyl-CoA dehydrogenase, an enzyme that catalyses the penultimate reaction in mitochondrial ??-oxidation of fatty acids. Mutati...
This novel finding allows accurate determination of long-chain 3-hydroxyacyl-CoA dehydrogenase activity, which is of great importance for correct pre- and postnatal diagnosis in leukocytes and chorionic villi (fibroblasts), respectively. 展开 关键词: Soil quality Mediterranean soils Forest soils ...
Long chain 3-hydroxyacyl-CoA dehydrogenase deficiency (LCHADD) is a fatty acid oxidation disorder (FAOD) caused by a pathogenic variant, c.1528 G > C, in HADHA encoding the alpha subunit of trifunctional protein (TFPα). Individuals with LCHA
Also, the NH2-terminal fragments of MFE-2, including Met1–Thr312 and Met1–Ala316 (Figure 1), were isolated from rat liver with (3R)-hydroxyacyl-CoA dehydrogenase activity 2, 39. The dhΔSCP-2LΔ was expressed in Escherichia coli and purified chromatographically to apparent homogeneity. ...
Pette D: .4ctivities of malate dehydrogrnase, 3- hydroxyacyl-CoA dehydrogenase and fructose- I ,6- diphosphatase with regard to metabolic subpopulations o f fast- and slowtwitch fibres in rabbit muscles. Hi.rfochemixtq 60:9-19. 1979....