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Dihydrolipoyl transacetylase information


DLAT
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesDLAT, DLTA, PDC-E2, PDCE2, dihydrolipoamide S-acetyltransferase, Dihydrolipoyl transacetylase, E2
External IDsOMIM: 608770 MGI: 2385311 HomoloGene: 6814 GeneCards: DLAT
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001931

NM_145614

RefSeq (protein)

NP_663589

Location (UCSC)Chr 11: 112.02 – 112.06 MbChr 9: 50.55 – 50.57 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Dihydrolipoyl transacetylase (or dihydrolipoamide acetyltransferase) is an enzyme component of the multienzyme pyruvate dehydrogenase complex. The pyruvate dehydrogenase complex is responsible for the pyruvate decarboxylation step that links glycolysis to the citric acid cycle. This involves the transformation of pyruvate from glycolysis into acetyl-CoA which is then used in the citric acid cycle to carry out cellular respiration.

There are three different enzyme components in the pyruvate dehydrogenase complex. Pyruvate dehydrogenase (EC 1.2.4.1) is responsible for the oxidation of pyruvate, dihydrolipoyl transacetylase (this enzyme; EC 2.3.1.12) transfers the acetyl group to coenzyme A (CoA), and dihydrolipoyl dehydrogenase (EC 1.8.1.4) regenerates the lipoamide. Because dihydrolipoyl transacetylase is the second of the three enzyme components participating in the reaction mechanism for conversion of pyruvate into acetyl CoA, it is sometimes referred to as E2.

In humans, dihydrolipoyl transacetylase enzymatic activity resides in the pyruvate dehydrogenase complex component E2 (PDCE2) that is encoded by the DLAT (dihydrolipoamide S-acetyltransferase) gene.[5]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000150768 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000000168 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Leung PS, Watanabe Y, Munoz S, Teuber SS, Patel MS, Korenberg JR, Hara P, Coppel R, Gershwin ME (1993). "Chromosome localization and RFLP analysis of PDC-E2: the major autoantigen of primary biliary cirrhosis". Autoimmunity. 14 (4): 335–40. doi:10.3109/08916939309079237. PMID 8102256.

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Dihydrolipoyl transacetylase

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Dihydrolipoyl transacetylase (or dihydrolipoamide acetyltransferase) is an enzyme component of the multienzyme pyruvate dehydrogenase complex. The pyruvate...

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Pyruvate dehydrogenase complex

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24 molecules of dihydrolipoyl transacetylase (E2). Up to 16 homodimers of pyruvate dehydrogenase (E1) and 8 homodimers of dihydrolipoyl dehydrogenase (E3)...

Word Count : 3219

E2

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Iodine-deficiency (ICD-10 code: E02) Estradiol, an estrogen steroid hormone Dihydrolipoyl transacetylase, the second element of the multienzyme pyruvate dehydrogenase...

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Oxidative decarboxylation

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lipoamide to coenzyme A (CoA) by the activity of the E2, or dihydrolipoyl transacetylase, component of the complex. This is an isoenergetic conversion...

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Lipoic acid

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metabolism EC 2.3.1.12 dihydrolipoyl transacetylase (E2) DLAT pyruvate dehydrogenase complex (PDC) energy metabolism EC 2.3.1.61 dihydrolipoyl succinyltransferase...

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Pyruvate dehydrogenase deficiency

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mutation. More rarely, mutations occur in the E2 (dihydrolipoyl transacetylase) or the E3 (dihydrolipoyl dehydrogenase) subunits of the PDC enzymatic complex...

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Pyruvate dehydrogenase lipoamide kinase isozyme 1

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"Recombinant expression and evaluation of the lipoyl domains of the dihydrolipoyl acetyltransferase component of the human pyruvate dehydrogenase complex"...

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PDK2

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interaction between the pyruvate dehydrogenase kinase isoform 2 and the dihydrolipoyl acetyltransferase". The Journal of Biological Chemistry. 278 (36): 33681–93...

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E3 binding protein

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The E3 binding protein directly interacts with the dihydrolipoamide transacetylase (E2) core, anchoring it to the complex. E3BP binds the I domain of E2...

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