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Literature summary extracted from

  • Ambrus, A.; Mizsei, R.; Adam-Vizi, V.
    Structural alterations by five disease-causing mutations in the low-pH conformation of human dihydrolipoamide dehydrogenase (hLADH) analyzed by molecular dynamics - implications in functional loss and modulation of reactive oxygen species generation by pa (2015), Biochem. Biophys. Rep., 2, 50-56 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.8.1.4 I445M naturally occuring mutation, mutant enzyme structure analysis Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.8.1.4 mitochondrion
-
 Homo sapiens 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.8.1.4 dihydrolipoamide + NAD+ Homo sapiens
-
 lipoamide + NADH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.4 Homo sapiens P09622
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.4 dihydrolipoamide + NAD+
-
 Homo sapiens lipoamide + NADH + H+
-
 r

Subunits

EC Number Subunits Comment Organism
1.8.1.4 homodimer
-
 Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.8.1.4 dihydrolipoamide dehydrogenase
-
 Homo sapiens
1.8.1.4 E3
-
 Homo sapiens
1.8.1.4 hLADH
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.4 FAD
-
 Homo sapiens
1.8.1.4 NAD+
-
 Homo sapiens
1.8.1.4 NADH
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
1.8.1.4 malfunction pathogenic mutations of hLADH cause severe metabolic diseases (atypical forms of E3 deficiency) that often escalate to cardiological or neurological presentations and even premature death. The pathologies are generally accompanied by lactic acidosis. hLADH presents a distinct conformation under acidosis (pH 5.5-6.8) with lower physiological activity and the capacity of generating reactive oxygen species (ROS). Molecular dynamics simulation of the structural changes induced in the low-pH conformation of hLADH by five pathogenic mutations of hLADH. Determination of structures of these disease-causing mutants of hLADH, overview Homo sapiens
1.8.1.4 physiological function human dihydrolipoamide dehydrogenase is a flavoenzyme component (E3) of the human 2-oxoglutarate dehydrogenase complex and few other dehydrogenase complexes Homo sapiens