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Literature summary for 1.1.1.211 extracted from

  • 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 (2013), J. Bioenerg. Biomembr., 45, 47-57.
    View publication on PubMed
Search for more literature for 1.1.1.211

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Rattus norvegicus 5739
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
a long-chain (S)-3-hydroxyacyl-CoA + NAD+ Rattus norvegicus
-
 a long-chain 3-oxoacyl-CoA + NADH + H+
-
 ?
a long-chain (S)-3-hydroxyacyl-CoA + NAD+ Rattus norvegicus Wistar
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 a long-chain 3-oxoacyl-CoA + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus Q64428
-
-
Rattus norvegicus Wistar Q64428
-
-

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
a long-chain (S)-3-hydroxyacyl-CoA + NAD+
-
 Rattus norvegicus a long-chain 3-oxoacyl-CoA + NADH + H+
-
 ?
a long-chain (S)-3-hydroxyacyl-CoA + NAD+
-
 Rattus norvegicus Wistar a long-chain 3-oxoacyl-CoA + NADH + H+
-
 ?

Synonyms

Synonyms Comment Organism
LCHAD
-
 Rattus norvegicus
long-chain 3-hydroxyacyl-CoA dehydrogenase
-
 Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Rattus norvegicus

General Information

General Information Comment Organism
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 Rattus norvegicus
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) Rattus norvegicus