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3-hydroxyoctanoyl-CoA + NAD+
3-ketooctanoyl-CoA + NADH
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3-ketohexadecanoyl-CoA + NADH
3-hydroxyhexadecanoyl-CoA + NAD+
3-ketohexanoyl-CoA + NADH
3-hydroxyhexanoyl-CoA + NAD+
3-oxodecanoyl-CoA + NADH
3-hydroxydecanoyl-CoA + NAD+
a long-chain (S)-3-hydroxyacyl-CoA + NAD+
a long-chain 3-oxoacyl-CoA + NADH + H+
acetoacetyl-CoA + NADH + H+
3-hydroxybutyryl-CoA + NAD+
additional information
?
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3-ketohexadecanoyl-CoA + NADH
3-hydroxyhexadecanoyl-CoA + NAD+
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3-ketohexadecanoyl-CoA + NADH
3-hydroxyhexadecanoyl-CoA + NAD+
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?
3-ketohexadecanoyl-CoA + NADH
3-hydroxyhexadecanoyl-CoA + NAD+
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-
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?
3-ketohexadecanoyl-CoA + NADH
3-hydroxyhexadecanoyl-CoA + NAD+
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?
3-ketohexanoyl-CoA + NADH
3-hydroxyhexanoyl-CoA + NAD+
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?
3-ketohexanoyl-CoA + NADH
3-hydroxyhexanoyl-CoA + NAD+
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-
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?
3-ketohexanoyl-CoA + NADH
3-hydroxyhexanoyl-CoA + NAD+
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-
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?
3-oxodecanoyl-CoA + NADH
3-hydroxydecanoyl-CoA + NAD+
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-
-
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?
3-oxodecanoyl-CoA + NADH
3-hydroxydecanoyl-CoA + NAD+
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-
-
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?
3-oxodecanoyl-CoA + NADH
3-hydroxydecanoyl-CoA + NAD+
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?
a long-chain (S)-3-hydroxyacyl-CoA + NAD+
a long-chain 3-oxoacyl-CoA + NADH + H+
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-
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?
a long-chain (S)-3-hydroxyacyl-CoA + NAD+
a long-chain 3-oxoacyl-CoA + NADH + H+
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-
-
?
a long-chain (S)-3-hydroxyacyl-CoA + NAD+
a long-chain 3-oxoacyl-CoA + NADH + H+
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-
-
?
a long-chain (S)-3-hydroxyacyl-CoA + NAD+
a long-chain 3-oxoacyl-CoA + NADH + H+
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-
-
?
acetoacetyl-CoA + NADH + H+
3-hydroxybutyryl-CoA + NAD+
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-
-
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?
acetoacetyl-CoA + NADH + H+
3-hydroxybutyryl-CoA + NAD+
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-
-
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?
additional information
?
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trifunctional, membrane bound, beta-oxidation enzyme
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?
additional information
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trifunctional, membrane bound, beta-oxidation enzyme
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additional information
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LCHAD and mitochondrial trifunctional protein, EC 4.2.1.17, deficiency can lead to retinopathy and peripheral neuropathy
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?
additional information
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mutational LCHAD deficiency leads to accumulation of long-chain 3-hydroxyacylcarnitines and the severe chorioretinopathy, retinal phenotypes in enzyme deficient children, the progression of the disease can be prevented by a dietary therapy including supplementation with docosahexaenoic acid, DHA, overview
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?
additional information
?
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mutational enzyme deficiency may lead to acute fatty liver in pregnancy, a serious, often lethal hepatic disorder, overview
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additional information
additional information
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has also enoyl-CoA-hydratase activity
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?
additional information
additional information
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has also enoyl-CoA-hydratase activity
has also 3-ketoacyl-CoA thiolase activity
?
additional information
additional information
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has also enoyl-CoA-hydratase activity
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?
additional information
additional information
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has also enoyl-CoA-hydratase activity
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?
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malfunction
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the placenta of an 8-month-old child diagnosed with long-chain 3-hydroxyacyl coenzyme A dehydrogenase (LCHAD) deficiency shows maternal floor infarction/massive perivillous fibrin, MFI/MPVFD, phenotype, overview
malfunction
a patient with hemophagocytic lymphohistiocytosis and LCHAD deficiency suffers pancytopenia, liver failure, and rhabdomyolysis. LCHAD deficiency, especially in 1 to 6 months old infants with laboratory findings of hypoglycemia, metabolic acidosis, and elevated creatine kinase, may also have hemophagocytic lymphohistiocytosis (HLH), a secondary HLH may develop in patients with LCHAD deficiency
malfunction
analysis of the effects of the major long-chain monocarboxylic 3-hydroxylated fatty acids (LCHFA) accumulating in the disorders mitochondrial trifunctional protein (MTP) and long-chain 3-hydroxy-acyl-CoA dehydrogenase (LCHAD) deficiencies, namely 3-hydroxytetradecanoic (3HTA) and 3-hydroxypalmitic (3HPA) acids, on important mitochondrial functions in rat skeletal muscle mitochondria 3HTA and 3HPA markedly increases resting and decrease ADP-stimulated and CCCP-stimulated (uncoupled) respiration. 3HPA provokes similar effects in permeabilized skeletal muscle fibers, validating the results obtained in purified mitochondria. 3HTA and 3HPA markedly diminish mitochondrial membrane potential, NAD(P)H content, and Ca2+ retention capacity in Ca2+-loaded mitochondria. Mitochondrial permeability transition (mPT) induction probably underlies these effects since they are totally prevented by cyclosporin A and ADP. In contrast, the dicarboxylic analogue of 3HTA does not alter the tested parameters. 3HTA and 3HPA behave as metabolic inhibitors, uncouplers of oxidative phosphorylation and mPT inducers in skeletal muscle. The pathomechanisms disrupting mitochondrial homeostasis may be involved in the muscle alterations characteristic ofMTP and LCHAD deficiencies
malfunction
children with long-chain 3-hydroxyacyl-CoA dehydrogenasedeficiency (LCHAD) have a defect in the degradation of long-chain fatty acids and are at risk of hypoketotic hypoglycemia and insufficient energy production as well as accumulation of toxic fatty acid intermediates. lipolysis and accumulation of long chain acylcarnitines occurs before hypoglycemia in fasting children with LCHAD, which may indicate more limited fasting tolerance than previously suggested, phenotypes, overview. Early and increased lipolysis and accumulation of long chain acylcarnitines after 4 h of fasting, albeit no patients developed hypoglycemia
malfunction
effects of long-chain 3-hydroxylated fatty acids (LCHFA) that accumulate in LCHAD deficiency on liver bioenergetics in mitochondrial preparations from young rats: 3-hydroxytetradecanoic (3HTA) and 3-hydroxypalmitic (3HPA) acids, the monocarboxylic acids that are found at the highest tissue concentrations in this disorder, act as metabolic inhibitors and uncouplers of oxidative phosphorylation. These fatty acids decrease ADP-stimulated and uncoupled respiration, mitochondrial membrane potential and NAD(P)H content, and, in contrast, increased resting respiration. 3HTA and 3HPA markedly reduce Ca2+ retention capacity and induce swelling in C2+-loaded mitochondria. The effects are mediated by mitochondrial permeability transition (MPT) induction since they are totally prevented by the classical MPT inhibitors cyclosporin A and ADP, as well as by ruthenium red, a Ca2+ uptake blocker. Long-chain monocarboxylic 3-hydroxylated fatty acids alter oxygen consumption in liver mitochondria. The major monocarboxylic LCHFA accumulating in LCHAD deficiency disrupt energy mitochondrial homeostasis in the liver leading to liver dysfunction
malfunction
long-chain 3-hydroxy fatty acids accumulating in long-chain 3-hydroxyacyl-CoA dehydrogenase and mitochondrial trifunctional protein deficiencies uncouple oxidative phosphorylation in heart mitochondria. Cardiomyopathy is a common clinical feature of some inherited disorders of mitochondrial fatty acid beta-oxidation including mitochondrial trifunctional protein (MTP) and isolated long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD) deficiencies. 3-Hydroxytetradecanoic (3HTA) and 3-hydroxypalmitic (3HPA) acids increase resting respiration and diminish the respiratory control and ADP/O ratios using glutamate/malate or succinate as substrates. 3-hydroxydodecanoic (3HDDA), 3HTA and 3HPA decrease DELTAPsi, the matrix NAD(P)H pool, and hydrogen peroxide production. These fatty acids behave as uncouplers of oxidative phosphorylation. 3HTA-induced uncoupling-effect is not mediated by the adenine nucleotide translocator and that this fatty acid induced the mitochondrial permeability transition pore opening in calcium-loaded organelles since cyclosporin A prevents the reduction of mitochondrial DELTAPsi and swelling provoked by 3HTA
malfunction
long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency (LCHADD) and trifunctional protein (TFP) deficiency are accompanied by increased levels of 3-hydroxypalmitoleoyl-carnitine combined with other hydroxylated long chain acylcarnitines, analysis of acylcarnitine profile of two LCHADD patients, overview. Patients with propionic acidemia (PA) or methylmalonic acidemia (MMA) also show high levels of 3-hydroxypalmitoleoyl-carnitine and heptadecanoylcarnitine
malfunction
long-chain 3-hydroxyacyl-CoA dehydrogenase, LCHAD, deficiency is a defect of the TFP complex caused by a mutation in the HADHA gene on short arm of chromosome 2 (2p23). The most common mutation (1528G.C, G510Q) is responsible for at least one allele in 60100 percent of individuals with LCHAD deficiency. LCHAD and TFP deficiencies are caused by different genetic mutations in the same protein, mitochondrial trifunctional protein (MTFP). Long-chain fatty acids are broken down by the MTFP after initial metabolism by very long-chain acyl-CoA dehydrogenase. In individuals with LCHAD deficiency, there is one enzymatic defect (3-hydroxylacyl-CoA dehydrogenase) which results in accumulation of long-chain hydroxylacylcarnitines. In TFP deficiency, the process of the b-oxidation includes defects in three enzymes, enoyl-CoA hydratase, 3-hydroxyl-CoA dehydrogenase (LCHAD), and 3-ketothiolase, which results in accumulation of mixed, long-chain acylcarnitine species. Although disorders of trifunctional protein (TFP) complex including longchain 3-hydroxyacyl-CoA dehydrogenase (LCHAD) and mitochondrial TFP deficiencies are extremely rare, the combined incidence of mitochondrial fatty acid disorders is quite frequent. With the expansion of newborn screening, what were once considered uncommon disorders are being identified with increasing frequency in asymptomatic infants. Infants with inborn errors of metabolism can present with breathing difficulties, acidosis (or alkalosis), and hypoglycemia, phenotype, detailed overview
malfunction
Long-chain 3-hydroxylated fatty acids (LCHFA) accumulate in long-chain 3-hydroxy-acyl-CoA dehydrogenase (LCHAD) and mitochondrial trifunctional protein (MTP) deficiencies. 3-Hydroxytetradecanoic acid (3 HTA) reduces mitochondrial membrane potential, NAD(P)H levels, Ca2+ retention capacity and ATP content, besides inducing swelling, cytochrome c release and H2O2 production in Ca2+-loaded mitochondrial preparations. Cyclosporine A plus ADP, as well as ruthenium red, a Ca2+ uptake blocker, prevent these effects, suggesting the involvement of the mitochondrial permeability transition pore (mPTP) and an important role for Ca2+, respectively. 3-Hydroxydodecanoic and 3-hydroxypalmitic acids, that also accumulate in LCHAD and MTP deficiencies, similarly induce mitochondrial swelling and decrease ATP content, but to a variable degree pending on the size of their carbon chain. Pathological neurological phenotype, detailed overview
malfunction
mitochondrial trifunctional protein and long-chain 3-hydroxyacyl-CoA dehydrogenase deficiencies are fatty acid oxidation disorders biochemically characterized by tissue accumulation of long-chain fatty acids and derivatives, including the monocarboxylic long-chain 3-hydroxy fatty acids (LCHFAs) 3-hydroxytetradecanoic acid (3HTA) and 3-hydroxypalmitic acid (3HPA). Deregulation of mitochondrial functions can be provoked by long-chain fatty acid accumulating in long-chain 3-hydroxyacyl-CoA dehydrogenase and mitochondrial permeability transition deficiencies in rat heart. 3HTA and 3HPA significantly decrease mitochondrial membrane potential, the matrix NAD(P)H pool and Ca2+ retention capacity, and also induced mitochondrial swelling. These fatty acids also provoke a marked decrease of ATP production reflecting severe energy dysfunction. 3HTA-induced mitochondrial alterations are completely prevented by the classical mitochondrial permeability transition (mPT) inhibitors cyclosporin A and ADP, as well as by ruthenium red, a Ca2+ uptake blocker, indicating that LCHFAs induce Ca2+-dependent mPT pore opening. Comparison of the susceptibility of heart and brain to the toxic effects of these hydroxylated fatty acids, phenotypes, overview
malfunction
the common homozygous mutation in the trifunctional protein alpha-subunit gene HADHA (hydroxyacyl-CoA dehydrogenase), c.1528G>C, affects the long chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD) activity of trifunctional protein and causes blindness in infancy. LCHAD deficiency patient retinal pigment epithelia have intense cytoplasmic neutral lipid accumulation, and lipidomic analysis reveals an increased triglyceride accumulation. Patient retinal pigment epithelia are small and irregular in shape, and their tight junctions are disorganized. Their ultratructure shows decreased pigmentation, few melanosomes, and more melanolysosomes. Early pathogenic changes in LCHADD retinopathy occur with robust lipid accumulation, inefficient pigmentation that is evident soon after differentiation, and a defect in forming tight junctions inducing apoptosis. LCHADD-retinal pigment epithelia are an important model for mitochondrial trifunctional protein (TFP) retinopathy
malfunction
defects in long-chain 3-hydroxy acyl-CoA dehydrogenase lead to hepatocellular carcinoma
malfunction
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enzyme exon 15 deletion is embryonic lethal to the homozygous mice whereas heterozygous mice develop significant hepatic steatosis starting at young age (3 months old) and hepatocellular carcinoma at older age (more than13 months old) without any evidence of fibrosis or cirrhosis
malfunction
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long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency is characterized by lethargy, hypoglycemia, hypotonia, cardiomyopathy, and acute metabolic crisis
malfunction
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Long-chain 3-hydroxylated fatty acids (LCHFA) accumulate in long-chain 3-hydroxy-acyl-CoA dehydrogenase (LCHAD) and mitochondrial trifunctional protein (MTP) deficiencies. 3-Hydroxytetradecanoic acid (3 HTA) reduces mitochondrial membrane potential, NAD(P)H levels, Ca2+ retention capacity and ATP content, besides inducing swelling, cytochrome c release and H2O2 production in Ca2+-loaded mitochondrial preparations. Cyclosporine A plus ADP, as well as ruthenium red, a Ca2+ uptake blocker, prevent these effects, suggesting the involvement of the mitochondrial permeability transition pore (mPTP) and an important role for Ca2+, respectively. 3-Hydroxydodecanoic and 3-hydroxypalmitic acids, that also accumulate in LCHAD and MTP deficiencies, similarly induce mitochondrial swelling and decrease ATP content, but to a variable degree pending on the size of their carbon chain. Pathological neurological phenotype, detailed overview
-
malfunction
-
effects of long-chain 3-hydroxylated fatty acids (LCHFA) that accumulate in LCHAD deficiency on liver bioenergetics in mitochondrial preparations from young rats: 3-hydroxytetradecanoic (3HTA) and 3-hydroxypalmitic (3HPA) acids, the monocarboxylic acids that are found at the highest tissue concentrations in this disorder, act as metabolic inhibitors and uncouplers of oxidative phosphorylation. These fatty acids decrease ADP-stimulated and uncoupled respiration, mitochondrial membrane potential and NAD(P)H content, and, in contrast, increased resting respiration. 3HTA and 3HPA markedly reduce Ca2+ retention capacity and induce swelling in C2+-loaded mitochondria. The effects are mediated by mitochondrial permeability transition (MPT) induction since they are totally prevented by the classical MPT inhibitors cyclosporin A and ADP, as well as by ruthenium red, a Ca2+ uptake blocker. Long-chain monocarboxylic 3-hydroxylated fatty acids alter oxygen consumption in liver mitochondria. The major monocarboxylic LCHFA accumulating in LCHAD deficiency disrupt energy mitochondrial homeostasis in the liver leading to liver dysfunction
-
malfunction
-
long-chain 3-hydroxy fatty acids accumulating in long-chain 3-hydroxyacyl-CoA dehydrogenase and mitochondrial trifunctional protein deficiencies uncouple oxidative phosphorylation in heart mitochondria. Cardiomyopathy is a common clinical feature of some inherited disorders of mitochondrial fatty acid beta-oxidation including mitochondrial trifunctional protein (MTP) and isolated long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD) deficiencies. 3-Hydroxytetradecanoic (3HTA) and 3-hydroxypalmitic (3HPA) acids increase resting respiration and diminish the respiratory control and ADP/O ratios using glutamate/malate or succinate as substrates. 3-hydroxydodecanoic (3HDDA), 3HTA and 3HPA decrease DELTAPsi, the matrix NAD(P)H pool, and hydrogen peroxide production. These fatty acids behave as uncouplers of oxidative phosphorylation. 3HTA-induced uncoupling-effect is not mediated by the adenine nucleotide translocator and that this fatty acid induced the mitochondrial permeability transition pore opening in calcium-loaded organelles since cyclosporin A prevents the reduction of mitochondrial DELTAPsi and swelling provoked by 3HTA
-
malfunction
-
analysis of the effects of the major long-chain monocarboxylic 3-hydroxylated fatty acids (LCHFA) accumulating in the disorders mitochondrial trifunctional protein (MTP) and long-chain 3-hydroxy-acyl-CoA dehydrogenase (LCHAD) deficiencies, namely 3-hydroxytetradecanoic (3HTA) and 3-hydroxypalmitic (3HPA) acids, on important mitochondrial functions in rat skeletal muscle mitochondria 3HTA and 3HPA markedly increases resting and decrease ADP-stimulated and CCCP-stimulated (uncoupled) respiration. 3HPA provokes similar effects in permeabilized skeletal muscle fibers, validating the results obtained in purified mitochondria. 3HTA and 3HPA markedly diminish mitochondrial membrane potential, NAD(P)H content, and Ca2+ retention capacity in Ca2+-loaded mitochondria. Mitochondrial permeability transition (mPT) induction probably underlies these effects since they are totally prevented by cyclosporin A and ADP. In contrast, the dicarboxylic analogue of 3HTA does not alter the tested parameters. 3HTA and 3HPA behave as metabolic inhibitors, uncouplers of oxidative phosphorylation and mPT inducers in skeletal muscle. The pathomechanisms disrupting mitochondrial homeostasis may be involved in the muscle alterations characteristic ofMTP and LCHAD deficiencies
-
metabolism
the mitochondrial trifunctional protein (MTP) is an enzymatic complex associated with the inner mitochondrial membrane and participates in the beta-oxidation of long-chain fatty acids. MTP comprises the activities of 3-hydroxyacyl-CoA dehydrogenase (LCHAD), 2-enoyl-CoA hydratase and 3-oxoacyl-CoA thiolase (LKAT)
metabolism
-
the mitochondrial trifunctional protein (MTP) is an enzymatic complex associated with the inner mitochondrial membrane and participates in the beta-oxidation of long-chain fatty acids. MTP comprises the activities of 3-hydroxyacyl-CoA dehydrogenase (LCHAD), 2-enoyl-CoA hydratase and 3-oxoacyl-CoA thiolase (LKAT)
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physiological function
long-chain 3-hydroxy-acyl-CoA dehydrogenase (LCHAD) is part of the mitochondrial trifunctional protein (MTP) complex that also comprises other two enzyme activities, long-chain enoyl-CoA hydratase and long-chain ketoacyl-CoA thiolase (LCKT). This complex is responsible for mitochondrial oxidation of long-chain fatty acids (LCFA)
physiological function
-
long-chain 3-hydroxy-acyl-CoA dehydrogenase (LCHAD) is part of the mitochondrial trifunctional protein (MTP) complex that also comprises other two enzyme activities, long-chain enoyl-CoA hydratase and long-chain ketoacyl-CoA thiolase (LCKT). This complex is responsible for mitochondrial oxidation of long-chain fatty acids (LCFA)
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El-Fakhri, M.; Middleton, B.
The existence of an inner-membrane-bound, long acyl-chain-specific 3-hydroxyacyl-CoA dehydrogenase in mammalian mitochondria
Biochim. Biophys. Acta
713
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1982
Oryctolagus cuniculus, Rattus norvegicus
brenda
Carpenter, K.; Pollitt, R.J.; Middleton, B.
Human liver long-chain 3-hydroxyacyl-coenzyme A dehydrogenase is a multifunctional membrane-bound beta-oxidation enzyme of mitochondria
Biochem. Biophys. Res. Commun.
183
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1992
Homo sapiens
brenda
Middleton, B.
The mitochondrial long-chain trifunctional enzyme: 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase and 3-oxoacyl-CoA thiolase
Biochem. Soc. Trans.
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Homo sapiens
brenda
Uchida, Y.; Izai, K.; Orii, T.; Hashimoto, T.
Novel fatty acid beta-oxidation enzymes in rat liver mitochondria. II. Purification and properties of enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein
J. Biol. Chem.
267
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1992
Rattus norvegicus (Q64428)
brenda
Carpenter, K.; Pollitt, R.J.; Middleton, B.
A unique, membrane-bound, multifunctional enzyme from human liver mitochondria catalysing three steps of fatty acid beta-oxidation
Biochem. Soc. Trans.
21
35S
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Homo sapiens
brenda
Jones, P.M.; Butt, Y.M.; Bennett, M.J.
Effects of odd-numbered medium-chain fatty acids on the accumulation of long-chain 3-hydroxy-fatty acids in long-chain L-3-hydroxyacyl CoA dehydrogenase and mitochondrial trifunctional protein deficient skin fibroblasts
Mol. Genet. Metab.
81
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2004
Homo sapiens
brenda
Rakheja, D.; Bennett, M.J.; Foster, B.M.; Domiati-Saad, R.; Rogers, B.B.
Evidence for fatty acid oxidation in human placenta, and the relationship of fatty acid oxidation enzyme activities with gestational age
Placenta
23
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2002
Homo sapiens
brenda
Gillingham, M.B.; Weleber, R.G.; Neuringer, M.; Connor, W.E.; Mills, M.; van Calcar, S.; Ver Hoeve, J.; Wolff, J.; Harding, C.O.
Effect of optimal dietary therapy upon visual function in children with long-chain 3-hydroxyacyl CoA dehydrogenase and trifunctional protein deficiency
Mol. Genet. Metab.
86
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2005
Homo sapiens
brenda
Oey, N.A.; den Boer, M.E.; Wijburg, F.A.; Vekemans, M.; Auge, J.; Steiner, C.; Wanders, R.J.; Waterham, H.R.; Ruiter, J.P.; Attie-Bitach, T.
Long-chain fatty acid oxidation during early human development
Pediatr. Res.
57
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Homo sapiens
brenda
Law, L.K.; Tang, N.L.; Hui, J.; Ho, C.S.; Ruiter, J.; Fok, T.F.; Wanders, R.J.; Lam, C.W.
A novel functional assay for simultaneous determination of total fatty acid beta-oxidation flux and acylcarnitine profiling in human skin fibroblasts using (2)H(31)-palmitate by isotope ratio mass spectrometry and electrospray tandem mass spectrometry
Clin. Chim. Acta
382
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2007
Homo sapiens
brenda
Kong, X.F.; Zhang, X.X.; Yu, Y.Y.; Shi, Q.; La, D.D.; Zhu-Ge, C.D.; Deng, L.; Gong, Q.M.; Shen, B.Y.; Peng, C.H.; Li, H.W.
No mutation was found in the alpha-subunit of the mitochondrial tri-functional protein in one patient with severe acute fatty liver of pregnancy and her relatives
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22
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Homo sapiens
brenda
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Production of two monomer structures containing medium-chain-length polyhydroxyalkanoates by beta-oxidation-impaired mutant of Pseudomonas putida KT2442
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100
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Pseudomonas putida (Q88L88), Pseudomonas putida KT 2240 (Q88L88)
brenda
Park, H.D.; Kim, S.R.; Ki, C.S.; Lee, S.Y.; Chang, Y.S.; Jin, D.K.; Park, W.S.
Two novel HADHB gene mutations in a Korean patient with mitochondrial trifunctional protein deficiency
Ann. Clin. Lab. Sci.
39
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2009
Homo sapiens
brenda
Griffin, A.C.; Strauss, A.W.; Bennett, M.J.; Ernst, L.M.
Mutations in long-chain 3-hydroxyacyl coenzyme A dehydrogenase are associated with placental maternal floor infarction/massive perivillous fibrin deposition
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15
368-374
2012
Homo sapiens
brenda
Tonin, A.M.; Amaral, A.U.; Busanello, E.N.; Gasparotto, J.; Gelain, D.P.; Gregersen, N.; Wajner, M.
Mitochondrial bioenergetics deregulation caused by long-chain 3-hydroxy fatty acids accumulating in LCHAD and MTP deficiencies in rat brain: a possible role of mPTP opening as a pathomechanism in these disorders?
Biochim. Biophys. Acta
1842
1658-1667
2014
Rattus norvegicus (Q64428), Rattus norvegicus Wistar (Q64428)
brenda
Hickmann, F.H.; Cecatto, C.; Kleemann, D.; Monteiro, W.O.; Castilho, R.F.; Amaral, A.U.; Wajner, M.
Uncoupling, metabolic inhibition and induction of mitochondrial permeability transition in rat liver mitochondria caused by the major long-chain hydroxyl monocarboxylic fatty acids accumulating in LCHAD deficiency
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1847
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2015
Rattus norvegicus (Q64428), Rattus norvegicus Wistar (Q64428)
brenda
Malvagia, S.; Haynes, C.A.; Grisotto, L.; Ombrone, D.; Funghini, S.; Moretti, E.; McGreevy, K.S.; Biggeri, A.; Guerrini, R.; Yahyaoui, R.; Garg, U.; Seeterlin, M.; Chace, D.; De Jesus, V.R.; la Marca, G.
Heptadecanoylcarnitine (C17) a novel candidate biomarker for newborn screening of propionic and methylmalonic acidemias
Clin. Chim. Acta
450
342-348
2015
Homo sapiens (P40939), Homo sapiens
brenda
Cecatto, C.; Hickmann, F.H.; Rodrigues, M.D.; Amaral, A.U.; Wajner, M.
Deregulation of mitochondrial functions provoked by long-chain fatty acid accumulating in long-chain 3-hydroxyacyl-CoA dehydrogenase and mitochondrial permeability transition deficiencies in rat heart - mitochondrial permeability transition pore opening as a potential contributing pathomechanism of cardiac alterations in these disorders
FEBS J.
282
4714-4726
2015
Rattus norvegicus (Q64428)
brenda
Polinati, P.P.; Ilmarinen, T.; Trokovic, R.; Hyotylainen, T.; Otonkoski, T.; Suomalainen, A.; Skottman, H.; Tyni, T.
Patient-specific induced pluripotent stem cell-derived RPE cells: understanding the pathogenesis of retinopathy in long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency
Invest. Ophthalmol. Vis. Sci.
56
3371-3382
2015
Homo sapiens (P40939), Homo sapiens
brenda
Tonin, A.; Amaral, A.; Busanello, E.; Grings, M.; Castilho, R.; Wajner, M.
Long-chain 3-hydroxy fatty acids accumulating in long-chain 3-hydroxyacyl-CoA dehydrogenase and mitochondrial trifunctional protein deficiencies uncouple oxidative phosphorylation in heart mitochondria
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45
47-57
2013
Rattus norvegicus (Q64428), Rattus norvegicus Wistar (Q64428)
brenda
Haglind, C.; Nordenstroem, A.; Ask, S.; von Doebeln, U.; Gustafsson, J.; Stenlid, M.
Increased and early lipolysis in children with long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD) deficiency during fast
J. Inherit. Metab. Dis.
38
315-322
2015
Homo sapiens (P40939), Homo sapiens
brenda
Erdol, S.; Ture, M.; Baytan, B.; Yakut, T.; Saglam, H.
An unusual case of LCHAD deficiency presenting with a clinical picture of hemophagocytic lymphohistiocytosis: secondary HLH or coincidence?
J. Pediatr. Hematol. Oncol.
38
661-662
2016
Homo sapiens (P40939), Homo sapiens
brenda
Anderson, S.; Brooks, S.S.
When the usual symptoms become an unusual diagnosis: a case report of trifunctional protein complex
Neonatal Netw.
32
262-273
2013
Homo sapiens (P40939), Homo sapiens
brenda
Cecatto, C.; Godoy, K.d.o.s..S.; da Silva, J.C.; Amaral, A.U.; Wajner, M.
Disturbance of mitochondrial functions provoked by the major long-chain 3-hydroxylated fatty acids accumulating in MTP and LCHAD deficiencies in skeletal muscle
Toxicol. In Vitro
36
1-9
2016
Rattus norvegicus (Q64428), Rattus norvegicus Wistar (Q64428)
brenda
Han, Y.; Yang, Z.; Ding, X.; Yu, H.; Yi, Y.
Expression of long chain fatty acid oxidase in maternal and fetal tissues in preeclampsia-like mouse model in mid-gestation
Zhonghua Yi Xue Za Zhi
95
26-29
2015
Mus musculus
brenda
Stinton, C.; Fraser, H.; Geppert, J.; Johnson, R.; Connock, M.; Johnson, S.; Clarke, A.; Taylor-Phillips, S.
Newborn screening for long-chain 3-hydroxyacyl-CoA dehydrogenase and mitochondrial trifunctional protein deficiencies using acylcarnitines measurement in dried blood spots - a systematic review of test accuracy
Front. Pediatr.
9
606194
2021
Homo sapiens
brenda
Khare, T.; Khare, S.; Angdisen, J.J.; Zhang, Q.; Stuckel, A.; Mooney, B.P.; Ridenhour, S.E.; Gitan, R.S.; Hammoud, G.M.; Ibdah, J.A.
Defects in long-chain 3-hydroxy acyl-CoA dehydrogenase lead to hepatocellular carcinoma A novel etiology of hepatocellular carcinoma
Int. J. Cancer
147
1461-1473
2020
Mus musculus, Homo sapiens (P40939), Homo sapiens
brenda