Dihydrolipoyllysine-Residue Acetyltransferase
"Dihydrolipoyllysine-Residue Acetyltransferase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
An enzyme that catalyzes the acetyltransferase reaction using ACETYL CoA as an acetyl donor and dihydrolipoamide as acceptor to produce COENZYME A (CoA) and S-acetyldihydrolipoamide. It forms the (E2) subunit of the PYRUVATE DEHYDROGENASE COMPLEX.
| Descriptor ID |
D051047
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| MeSH Number(s) |
D05.500.562.625.750 D08.811.600.741.625 D08.811.913.050.134.310
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| Concept/Terms |
Dihydrolipoyllysine-Residue Acetyltransferase- Dihydrolipoyllysine-Residue Acetyltransferase
- Acetyltransferase, Dihydrolipoyllysine-Residue
- Dihydrolipoyllysine Residue Acetyltransferase
- Dihydrolipoamide Acetyltransferase
- Acetyltransferase, Dihydrolipoamide
- Pyruvate Dehydrogenase Complex E2
- Dihydrolipoyl Acetyltransferase
- Acetyltransferase, Dihydrolipoyl
- Dihydrolipoyl Transacetylase
- Transacetylase, Dihydrolipoyl
- Lipoate Acetyltransferase
- Acetyltransferase, Lipoate
- Acetyl-CoA-Dihydrolipoamide S-Acetyltransferase
- Acetyl CoA Dihydrolipoamide S Acetyltransferase
- S-Acetyltransferase, Acetyl-CoA-Dihydrolipoamide
- Dihydrolipoamide S-Acetyltransferase
- Dihydrolipoamide S Acetyltransferase
- S-Acetyltransferase, Dihydrolipoamide
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Below are MeSH descriptors whose meaning is more general than "Dihydrolipoyllysine-Residue Acetyltransferase".
Below are MeSH descriptors whose meaning is more specific than "Dihydrolipoyllysine-Residue Acetyltransferase".
This graph shows the total number of publications written about "Dihydrolipoyllysine-Residue Acetyltransferase" by people in this website by year, and whether "Dihydrolipoyllysine-Residue Acetyltransferase" was a major or minor topic of these publications.
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Below are the most recent publications written about "Dihydrolipoyllysine-Residue Acetyltransferase" by people in Profiles.
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Conformational flexibility of pyruvate dehydrogenase complexes: a computational analysis by quantized elastic deformational model. J Mol Biol. 2003 Jun 27; 330(1):129-35.
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Direct evidence for the size and conformational variability of the pyruvate dehydrogenase complex revealed by three-dimensional electron microscopy. The "breathing" core and its functional relationship to protein dynamics. J Biol Chem. 2001 Jun 15; 276(24):21704-13.
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Three-dimensional structure of the truncated core of the Saccharomyces cerevisiae pyruvate dehydrogenase complex determined from negative stain and cryoelectron microscopy images. J Biol Chem. 1992 Dec 05; 267(34):24769-75.
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Overexpression and mutagenesis of the catalytic domain of dihydrolipoamide acetyltransferase from Saccharomyces cerevisiae. Biochemistry. 1990 Sep 18; 29(37):8614-9.