2 edition of 3-ketoacid CoA transferase and D-3-hydroxybutyrate in ischemia. found in the catalog.
3-ketoacid CoA transferase and D-3-hydroxybutyrate in ischemia.
Reginald Sidney Harding
Written in English
|The Physical Object|
|Number of Pages||151|
Further analysis indicated that left ventricular carbonyl production correlated negatively with succinyl-CoAketoacid-coenzyme A transferase 1 activity (r 2 = , P = ) and ATP. Three classes of CoA-transferase – as distinguished by differences in their primary sequences, their substrate specificity, and the mechanism by which acyl transfer occurs – have been described. , The Class I CoA-transferases are mainly involved in fatty acid metabolism, and include enzymes that transfer 3-ketoacids, short-chain fatty acids, and (E)-glutaconate in which acetyl-CoA or.
The effects of diabetes and training on the activity of 3-ketoacid CoA-transferase in gastrocnemius muscle are shown in Figs. 2 and 3. When expressed per gram of gastrocnemius muscle, the activity of 3-ketoacid CoA-transferase transferase was decreased by 32% in sedentary diabetic rats compared with their sedentary counterparts (P. Activities of a number of metabolic enzymes such as glycerol phosphate dehydrogenase, pyruvate carboxylase, succinyl-CoAketoacid-CoA transferase and FAD-linked glycerol phosphate dehydrogenase were reduced in human β cells under diabetic conditions.
Decreased rate of ketone-body oxidation and decreased activity of Dhydroxybutyrate dehydrogenase and succinyl-CoAoxo-acid CoA-transferase in heart mitochondria of diabetic rats. Biochem J 49–56, Crossref PubMed ISI Google Scholar; Khullar M, . (e) Nrf2 nuclear accumulation levels. (f) Expression levels of the retinal ketolysis and fumarate synthesis‐related enzymes, D‐3‐hydroxybutyrate dehydrogenase (BDH1), succinyl‐CoA‐3‐oxaloacid CoA transferase (SCOT), acetyl‐CoA acetyltransferase 1 (ACAT1), succinate dehydrogenase subunit A (SDHA), and citrate synthase (CS).
Plantation journal of Evans Dunn of East Feliciana Parish, Louisiana
Cooking the books
History of the 20th Century
Celtic bards, chiefs, and kings
Off-highway vehicle guide
Report of the Committee of Inquiry into Collapse of Cooling Towers at Ferrybridge, Monday 1 November, 1965.
From Strength to Strength
Fair Isle survey
Expenditures of the Isthmian Canal Commission. Message from the President of the United States, transmitting a report from the Acting Secretary of State giving statement of the expenditures of the Isthmian Canal Commission, as the same are accounted for by said commission, etc., in response to the Senates resolution of June 30, 1902.
The rates of Dhydroxybutyrate utilization and of acetoacetate production are proportional to Dhydroxybutyrate concentration. Acetoacetate is then converted to its CoA ester, acetoacetyl-CoA, by the enzyme 3-ketoacyl-CoA transferase (succinyl-CoAketoacid CoA transferase). 3-ketoacyl-CoA transferase is the key enzyme of ketone body.
Abstract. We have examined the metabolism of ketone bodies in neuroblastoma C and glioma C6 cells, two established lines of neural origin. The three ketone body-metabolizing enzymes are present in cells of both lines in the relative proportions normally found in brain (Dhydroxybutyrate dehydrogenase less than acetoacetyl-CoA thiolase less than 3-ketoacid CoA-transferase), the Cited by: No measurable succinyl-CoA: 3-ketoacid CoA-transferase (CoA-transferase) activity could be detected in homogenates of the post mortem brain, muscle and kidney tissue, or in the cultured skin fibroblasts.
Since seven other enzyme activities involving both glycolysis and ketone body oxidation were present in these same tissues, it was reasonable Cited by: Succinyl-CoAketoacid coenzyme A transferase (SCOT), the mitochondrial enzyme involved in the breakdown of ketone bodies in the extrahepatic tissues, was identified in rat heart to undergo age-associated increase in a novel, nitro-hydroxy, addition to tryptophanlocated in close proximity (∼10 Å) of the enzyme active by: 3-ketoacid CoA-transferase.
3-ketoacid coenzyme A transferase. 3-ketoacid coenzyme A-transferase. 3-oxo-CoA transferase. 3-oxoacid CoA dehydrogenase. 3-ketoacid CoA transferase and D-3-hydroxybutyrate in ischemia. book coenzyme A-transferase. SCOT.
SCOT-t. acetoacetate succinyl-CoA transferase. acetoacetyl coenzyme A-succinic thiophorase. coenzyme A-transferase, 3-oxoacid. succinyl coenzyme A. The defects in ketolysis include succinyl-CoAketoacid CoA transferase (SCOT) deficiency and mitochondrial acetoacetyl-CoA thiolase (b-ketothiolase or T2) deficiency.
HMGCL deficiency and T2 deficiency also affect leucine and isoleucine catabolism, respectively. There are two enzymes involved in ketolysis: succinyl-CoAketoacid-CoA transferase, also known as acetoacetate succinyl-CoA transferase (SCOT, encoded by OXCT1 on chromosome 5p), which catalyzes the formation of acetoacetyl-CoA from acetoacetate, and β- ketothiolase, also known as mitochondrial acetoacetyl-CoA thiolase (MAT) and acetyl.
Mechanism and Specificity of Succinyl-CoAKetoacid Coenzyme A Transferase* (Received for publication, J ) HOWARD WHITE AND WILLIAM P. JENCKS From the Graduate Department of Biochemistry, Brandeis University, Waltham, Massachusetts ti4 (a) The reactivity of substituted acetates as substrates for CoA transferase increases sharply.
Succinyl-CoAketoacid coenzyme A transferase 1, mitochondrial (EC: Search proteins in UniProtKB for this EC number. See the description of this EC number in ENZYME.
Sakazaki H, Hirayama K, Murakami S, Yonezawa S, Shintaku H, Sawada Y, Fukao T, Watanabe H, Orii T, Isshiki G. A new Japanese case of succinyl-CoA: 3-ketoacid CoA-transferase deficiency.
J Inherit Metab Dis. ; – doi: /BF Sass JO. Inborn errors of ketogenesis and ketone body utilization. Succinyl-CoA: 3-ketoacid CoA transferase (SCOT) deficiency (EC ) is a mitochondrial matrix enzyme responsible for the formation of acetoacetyl-CoA by transfer of a CoA moiety from succinyl-CoA to acetoacetate.
This step is the rate-limiting step in the utilization of. We describe the distribution in human tissues of three enzymes of ketone body utilization: succinyl-CoAketoacid CoA transferase (SCOT), mitochondrial acetoacetyl-CoA thiolase (T2), and cytosolic acetoacetyl-CoA thiolase (CT).
Hereditary deficiency of each of. Succinyl-CoAketoacid CoA transferase (SCOT) deficiency is an inherited disorder that impairs the body's ability to break down ketones, which are molecules produced in the liver during the breakdown of fats.
The signs and symptoms of SCOT deficiency typically appear within the first few years of life. Tildon JT, Cornblath M () Succinyl-CoA: 3-ketoacid CoA-transferase deficiency. A cause for ketoacidosis in infancy. J Clin Invest – Google Scholar. Succinyl-CoA: 3-ketoacid CoA transferase (3-OAT; EC ) is the first enzyme involved in acetoacetate utilization, and it acts by transferring a CoA molecule from succinyl-CoA to acetoacetate.
In mitochondria of extrahepatic cells, AcAc is activated to AcAcCoA by succinyl-CoA: 3-ketoacid (oxoacid) CoA transferase (SCOT).
The ketolytic capacity of tissues varies directly with SCOT activity. In rat, if heart is assigned as %, other tissues are as follows: kidney (∼70%)⪢brain (∼10%)>skeletal muscle (∼5%)⪢liver (undetectable. in succinyl-CoA: 3-ketoacid CoA-transferase (CoA-transferase) in the post mortem tissues and the cultured fibroblasts of this infant, and to suggest a relationship which correlates this deficiency with the observed clini-cal manifestations and the biochemical studies of his tissue culture fibroblasts.
METHODS Case summary, C. (UM Succinyl-CoA: 3-ketoacid-CoA transferase (SCOT; locus symbol OXCT, EC ) deficiency is a rare genetic disorder affecting ketone body utilization in extra-hepatic tissues. The levels of Dhydroxybutyrate dehydrogenase (BDH1), the first enzyme in the 3HB ketolysis pathway, and citrate synthase (CS), an enzyme synthesizing citric acid from acetyl-CoA.
Acetoacetate, or bHB converted to acetoacetate by BDH, is converted next to acetoacetyl-CoA by a succinyl-CoA-dependent transferase (succinyl-CoAketoacid-CoA transferase, SCOT), which is the key reaction that enables ketone body utilization as energy substrates.
In the next step, acetoacetyl-CoA is cleaved into two molecules of acetyl-CoA. Two enzymes of ketone body metabolism, 3-oxoacid CoA-transferase and 3-hydroxybutyrate dehydrogenase were measured with ultramicromethods to map their activities along single, dissected segments of mouse nephron.
3-Oxoacid CoA-transferase activity was assayed with a radiochemical procedure by separating [14C]succinyl-CoA, formed in the presence.Figure 1 The chemical structures of the three ketone bodies: acetone, acetoacetate, and β-OHB.
There are three enzymatic steps involved in processing β-OHB to TCA cycle entry as acetyl-CoA. DHydroxybutyrate dehydrogenase (HBDH) converts β-OHB into acetoacetate, which can spontaneously be converted into acetone.
3-Ketoacyl-CoA transferase converts acetoacetate into acetoacetyl-CoA.In addition, levels of ATP in the fasting + DLHB group were significantly higher compared with other groups after 30 min of ischemia and min of reperfusion (P.