Dihydrolipoyllysine-residue acetyltransferase

From Wikipedia, the free encyclopedia

In enzymology, a dihydrolipoyllysine-residue acetyltransferase (EC 2.3.1.12) is an enzyme that catalyzes the chemical reaction

acetyl-CoA + enzyme N₆-(dihydrolipoyl)lysine $\rightleftharpoons$ CoA + enzyme N₆-(S-acetyldihydrolipoyl)lysine

Thus, the two substrates of this enzyme are acetyl-CoA and enzyme N6-(dihydrolipoyl)lysine, whereas its two products are CoA and enzyme N6-(S-acetyldihydrolipoyl)lysine.

This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. The systematic name of this enzyme class is acetyl-CoA:enzyme N6-(dihydrolipoyl)lysine S-acetyltransferase. Other names in common use include acetyl-CoA:dihydrolipoamide S-acetyltransferase, dihydrolipoamide S-acetyltransferase, dihydrolipoate acetyltransferase, dihydrolipoic transacetylase, dihydrolipoyl acetyltransferase, lipoate acetyltransferase, lipoate transacetylase, lipoic acetyltransferase, lipoic acid acetyltransferase, lipoic transacetylase, lipoylacetyltransferase, thioltransacetylase A, transacetylase X, enzyme-dihydrolipoyllysine:acetyl-CoA S-acetyltransferase, and acetyl-CoA:enzyme 6-N-(dihydrolipoyl)lysine S-acetyltransferase. This enzyme participates in 3 metabolic pathways: glycolysis / gluconeogenesis, alanine and aspartate metabolism, and pyruvate metabolism.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 31 structures have been solved for this class of enzymes, with PDB accession codes 1B5S, 1DPB, 1DPC, 1DPD, 1EAA, 1EAB, 1EAC, 1EAD, 1EAE, 1EAF, 1FYC, 1IYU, 1IYV, 1LAB, 1LAC, 1W3D, 1W4E, 1W4F, 1W4G, 1W4H, 1W4I, 1W4J, 1W4K, 1W85, 1W88, 1Y8N, 1Y8O, 1Y8P, 2DNE, 2PNR, and 2Q8I.

[edit] References

IUBMB entry for 2.3.1.12
BRENDA references for 2.3.1.12 (Recommended.)
PubMed references for 2.3.1.12
PubMed Central references for 2.3.1.12
Google Scholar references for 2.3.1.12
BRADY RO, STADTMAN ER (1954). "Enzymatic thioltransacetylation". J. Biol. Chem. 211: 621–9. PMID 13221570.
McElroy, W.D. and Glass, B. (Eds.), A Symposium on the Mechanism of Enzyme Action, Johns Hopkins Press, Baltimore, 1954, p. 545-580.
Gunsalus IC, Barton LS and Gruber W (1956). "Biosynthesis and structure of lipoic acid derivatives". J. Am. Chem. Soc. 78: 1763–1766. doi:10.1021/ja01589a079.
Perham RN (2000). "Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions". Annu. Rev. Biochem. 69: 961–1004. doi:10.1146/annurev.biochem.69.1.961. PMID 10966480.