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Literature summary for 1.8.1.4 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
Search for more literature for 1.8.1.4

Protein Variants

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

Localization

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens P09622
-
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
homodimer
-
 Homo sapiens

Synonyms

Synonyms Comment Organism
dihydrolipoamide dehydrogenase
-
 Homo sapiens
E3
-
 Homo sapiens
hLADH
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Homo sapiens
NAD+
-
 Homo sapiens
NADH
-
 Homo sapiens

General Information

General Information Comment Organism
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
physiological function human dihydrolipoamide dehydrogenase is a flavoenzyme component (E3) of the human 2-oxoglutarate dehydrogenase complex and few other dehydrogenase complexes Homo sapiens