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Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

A dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial that is encoded in the genome of human. [PRO:DNx, UniProtKB:P10515]

Synonyms

EC 2.3.1.12;
70 kDa mitochondrial autoantigen of primary biliary cirrhosis;
PBC;
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex;
M2 antigen complex 70 kDa subunit;
Pyruvate dehydrogenase complex compone

Research

Bioassay Publications (1)

TimeframeStudies on this Protein(%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's1 (100.00)2.80

Compounds (1)

Drugs with Activation Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
hyperforinHomo sapiens (human)Kd0.578011

Enables

This protein enables 3 target(s):

TargetCategoryDefinition
dihydrolipoyllysine-residue acetyltransferase activitymolecular functionCatalysis of the reaction: (R)-N6-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA = (R)-N6-(S8-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA. [RHEA:17017]
protein bindingmolecular functionBinding to a protein. [GOC:go_curators]
identical protein bindingmolecular functionBinding to an identical protein or proteins. [GOC:jl]

Located In

This protein is located in 3 target(s):

TargetCategoryDefinition
mitochondrioncellular componentA semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. [GOC:giardia, ISBN:0198506732]
mitochondrial matrixcellular componentThe gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. [GOC:as, ISBN:0198506732]
intracellular membrane-bounded organellecellular componentOrganized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. [GOC:go_curators]

Part Of

This protein is part of 1 target(s):

TargetCategoryDefinition
pyruvate dehydrogenase complexcellular componentA multi-enzyme complex that catalyzes the oxidative decarboxylation of pyruvate to form acetyl-CoA. The complex comprises multiple copies of three enzymes referred to as E1, E2 and E3: pyruvate dehydrogenase (E1, which may be a homodimer or a heterotetramer of two alpha and two beta subunits, depending on species), dihydrolipoamide S-acetyltransferase (E2), and dihydrolipoamide dehydrogenase (E3). Additional proteins may also be present. [PMID:36863425]

Involved In

This protein is involved in 3 target(s):

TargetCategoryDefinition
glucose metabolic processbiological processThe chemical reactions and pathways involving glucose, the aldohexose gluco-hexose. D-glucose is dextrorotatory and is sometimes known as dextrose; it is an important source of energy for living organisms and is found free as well as combined in homo- and hetero-oligosaccharides and polysaccharides. [ISBN:0198506732]
acetyl-CoA biosynthetic process from pyruvatebiological processThe chemical reactions and pathways resulting in the formation of acetyl-CoA from pyruvate. [GOC:dph, GOC:go_curators, GOC:tb]
tricarboxylic acid cyclebiological processA nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle. [ISBN:0198506732]