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CATH domain | Related DB codes (homologues) |
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2.40.50.100 : OB fold (Dihydrolipoamide Acetyltransferase, E2P) | M00163,M00222,M00145,M00188,M00189,T00223,M00190,M00208 | 3.30.559.10 : Chloramphenicol Acetyltransferase | M00188,M00189,T00223,M00190 | 4.10.320.10 : Dihydrolipoamide Transferase | M00188,M00189,T00223,M00190 |
Enzyme Name | UniProtKB | KEGG |
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| P06959 |
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Protein name | Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex | dihydrolipoyllysine-residue acetyltransferaseacetyl-CoA:dihydrolipoamide S-acetyltransferasedihydrolipoamide S-acetyltransferasedihydrolipoate acetyltransferasedihydrolipoic transacetylasedihydrolipoyl acetyltransferaselipoate acetyltransferaselipoate transacetylaselipoic acetyltransferaselipoic acid acetyltransferaselipoic transacetylaselipoylacetyltransferasethioltransacetylase Atransacetylase Xenzyme-dihydrolipoyllysine:acetyl-CoA S-acetyltransferaseacetyl-CoA:enzyme 6-N-(dihydrolipoyl)lysine S-acetyltransferase |
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Synonyms | EC 2.3.1.12Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complexE2 |
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RefSeq | NP_414657.1 (Protein) NC_000913.2 (DNA/RNA sequence) YP_488418.1 (Protein) NC_007779.1 (DNA/RNA sequence)
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Pfam | PF00198 (2-oxoacid_dh) PF00364 (Biotin_lipoyl) PF02817 (E3_binding) [Graphical view]
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KEGG pathways | MAP code | Pathways |
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MAP00010 | Glycolysis / Gluconeogenesis | MAP00020 | Citrate cycle (TCA cycle) | MAP00620 | Pyruvate metabolism |
UniProtKB:Accession Number | P06959 |
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Entry name | ODP2_ECOLI |
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Activity | Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine. |
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Subunit | Forms a 24-polypeptide structural core with octahedral symmetry. |
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Subcellular location |
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Cofactor | Binds 3 lipoyl cofactors covalently. |
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Compound table: links to PDB-related databases & PoSSuM |
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| Substrates | Products |
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KEGG-id | C00010 | L00017 | C00024 | C15973 |
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Compound | CoA | Enzyme N(6)-(S-acetyldihydrolipoyl)lysine | Acetyl-CoA | Enzyme N(6)-(dihydrolipoyl)lysine |
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Type | amine group,carbohydrate,nucleotide,peptide/protein,sulfhydryl group | amide group,carbohydrate,lipid,peptide/protein,sulfhydryl group,sulfide group | amine group,carbohydrate,nucleotide,peptide/protein,sulfide group | amide group,lipid,peptide/protein,sulfhydryl group |
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ChEBI | 15346
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| 15351
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PubChem | 6816 87642
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| 444493 6302
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| | | | | | | | | | | |
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1qjoA |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound |
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Active-site residues | pdb | Cofactor-binding residues |
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| | | | | | | | |
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1qjoA |  |  |  |  |  |  |  | LYS 41(Lipolyl binding)
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[13] | p.1547 |
| [14] | Scheme I, p.3899-3901 |
| [17] | p.1194-1195 |
| [20] | Fig.1, p.4292-4295 |
| [32] | Fig.6 |
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references | [1] |
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PubMed ID | 389239 |
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Journal | Biochem Biophys Res Commun |
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Year | 1979 |
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Volume | 90 |
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Pages | 431-8 |
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Authors | Fuller CC, Reed LJ, Oliver RM, Hackert ML |
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Title | Crystallization of a dihydrolipoyl transacetylase--dihydrolipoyl dehydrogenase subcomplex and its implications regarding the subunit structure of the pyruvate dehydrogenase complex from Escherichia coli. |
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[2] |
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PubMed ID | 6376124 |
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Journal | Eur J Biochem |
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Year | 1984 |
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Volume | 141 |
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Pages | 361-74 |
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Authors | Spencer ME, Darlison MG, Stephens PE, Duckenfield IK, Guest JR |
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Title | Nucleotide sequence of the sucB gene encoding the dihydrolipoamide succinyltransferase of Escherichia coli K12 and homology with the corresponding acetyltransferase. |
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[3] |
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PubMed ID | 3101735 |
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Journal | Biochemistry |
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Year | 1986 |
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Volume | 25 |
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Pages | 8173-8 |
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Authors | Yang YS, Frey PA |
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Title | Dihydrolipoyl transacetylase of Escherichia coli. Formation of 8-S-acetyldihydrolipoamide. |
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[4] |
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Comments | LIPOYL DOMAIN CONFORMATION. |
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Medline ID | 89052887 |
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PubMed ID | 3191993 |
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Journal | FEBS Lett |
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Year | 1988 |
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Volume | 240 |
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Pages | 205-10 |
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Authors | Hanemaaijer R, Vervoort J, Westphal AH, de Kok A, Veeger C |
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Title | Mobile sequences in the pyruvate dehydrogenase complex, the E2 component, the catalytic domain and the 2-oxoglutarate dehydrogenase complex of Azotobacter vinelandii, as detected by 600 MHz 1H-NMR spectroscopy. |
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Related UniProtKB | P10802 |
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[5] |
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PubMed ID | 2271545 |
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Journal | Biochemistry |
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Year | 1990 |
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Volume | 29 |
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Pages | 8614-9 |
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Authors | Niu XD, Stoops JK, Reed LJ |
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Title | Overexpression and mutagenesis of the catalytic domain of dihydrolipoamide acetyltransferase from Saccharomyces cerevisiae. |
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[6] |
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PubMed ID | 2192914 |
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Journal | FEBS Lett |
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Year | 1990 |
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Volume | 264 |
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Pages | 206-10 |
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Authors | Dardel F, Packman LC, Perham RN |
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Title | Expression in Escherichia coli of a sub-gene encoding the lipoyl domain of the pyruvate dehydrogenase complex of Bacillus stearothermophilus. |
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[7] |
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PubMed ID | 1908777 |
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Journal | Eur J Biochem |
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Year | 1991 |
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Volume | 200 |
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Pages | 29-34 |
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Authors | Schulze E, Benen JA, Westphal AH, de Kok A |
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Title | Interaction of lipoamide dehydrogenase with the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. |
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[8] |
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PubMed ID | 1935951 |
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Journal | Eur J Biochem |
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Year | 1991 |
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Volume | 201 |
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Pages | 561-8 |
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Authors | Schulze E, Westphal AH, Obmolova G, Mattevi A, Hol WG, de Kok A |
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Title | The catalytic domain of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii and Escherichia coli. Expression, purification, properties and preliminary X-ray analysis. |
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[9] |
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PubMed ID | 1590756 |
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Journal | Biochem J |
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Year | 1992 |
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Volume | 283 |
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Pages | 665-71 |
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Authors | Hipps DS, Perham RN |
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Title | Expression in Escherichia coli of a sub-gene encoding the lipoyl and peripheral subunit-binding domains of the dihydrolipoamide acetyltransferase component of the pyruvate dehydrogenase complex of Bacillus stearothermophilus. |
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[10] |
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PubMed ID | 1730230 |
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Journal | Eur J Biochem |
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Year | 1992 |
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Volume | 203 |
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Pages | 245-50 |
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Authors | Snoep JL, Westphal AH, Benen JA, Teixeira de Mattos MJ, Neijssel OM, de Kok A |
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Title | Isolation and characterisation of the pyruvate dehydrogenase complex of anaerobically grown Enterococcus faecalis NCTC 775. |
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[11] |
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PubMed ID | 1429691 |
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Journal | J Biol Chem |
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Year | 1992 |
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Volume | 267 |
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Pages | 23484-8 |
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Authors | Green JD, Perham RN, Ullrich SJ, Appella E |
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Title | Conformational studies of the interdomain linker peptides in the dihydrolipoyl acetyltransferase component of the pyruvate dehydrogenase multienzyme complex of Escherichia coli. |
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[12] |
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PubMed ID | 1589018 |
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Journal | Nature |
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Year | 1992 |
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Volume | 357 |
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Pages | 196-7 |
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Authors | DeRosier DJ |
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Title | Enzyme complexes. A farewell to arms. |
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[13] |
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Comments | X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 381-637. |
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Medline ID | 92196586 |
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PubMed ID | 1549782 |
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Journal | Science |
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Year | 1992 |
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Volume | 255 |
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Pages | 1544-50 |
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Authors | Mattevi A, Obmolova G, Schulze E, Kalk KH, Westphal AH, de Kok A, Hol WG |
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Title | Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex. |
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Related PDB | 1eaa,1eab,1eac,1ead,1eae,1eaf |
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Related UniProtKB | P10802 |
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[14] |
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PubMed ID | 8471601 |
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Journal | Biochemistry |
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Year | 1993 |
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Volume | 32 |
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Pages | 3887-901 |
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Authors | Mattevi A, Obmolova G, Kalk KH, Teplyakov A, Hol WG |
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Title | Crystallographic analysis of substrate binding and catalysis in dihydrolipoyl transacetylase (E2p). |
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[15] |
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PubMed ID | 8436118 |
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Journal | Eur J Biochem |
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Year | 1993 |
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Volume | 211 |
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Pages | 591-9 |
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Authors | Schulze E, Westphal AH, Hanemaaijer R, de Kok A |
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Title | Structure/function relationships in the pyruvate dehydrogenase complex from Azotobacter vinelandii. Role of the linker region between the binding and catalytic domain of the dihydrolipoyl transacetylase component. |
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[16] |
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PubMed ID | 8500617 |
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Journal | FEBS Lett |
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Year | 1993 |
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Volume | 323 |
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Pages | 243-6 |
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Authors | Machado RS, Guest JR, Williamson MP |
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Title | Mobility in pyruvate dehydrogenase complexes with multiple lipoyl domains. |
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[17] |
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Comments | X-ray crystallography |
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PubMed ID | 8487300 |
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Journal | J Mol Biol |
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Year | 1993 |
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Volume | 230 |
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Pages | 1183-99 |
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Authors | Mattevi A, Obmolova G, Kalk KH, Westphal AH, de Kok A, Hol WG |
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Title | Refined crystal structure of the catalytic domain of dihydrolipoyl transacetylase (E2p) from Azotobacter vinelandii at 2.6 A resolution. |
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Related PDB | 1dpb,1dpc,1dpd |
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[18] |
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PubMed ID | 8433963 |
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Journal | Protein Eng |
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Year | 1993 |
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Volume | 6 |
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Pages | 101-8 |
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Authors | Turner SL, Russell GC, Williamson MP, Guest JR |
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Title | Restructuring an interdomain linker in the dihydrolipoamide acetyltransferase component of the pyruvate dehydrogenase complex of Escherichia coli. |
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[19] |
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Comments | STRUCTURE BY NMR OF 1-78. |
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Medline ID | 94222112 |
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PubMed ID | 8068086 |
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Journal | Eur J Biochem |
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Year | 1994 |
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Volume | 221 |
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Pages | 87-100 |
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Authors | Berg A, de Kok A, Vervoort J |
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Title | Sequential 1H and 15N nuclear magnetic resonance assignments and secondary structure of the N-terminal lipoyl domain of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. |
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Related UniProtKB | P10802 |
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[20] |
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PubMed ID | 7703242 |
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Journal | Biochemistry |
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Year | 1995 |
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Volume | 34 |
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Pages | 4287-98 |
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Authors | Hendle J, Mattevi A, Westphal AH, Spee J, de Kok A, Teplyakov A, Hol WG |
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Title | Crystallographic and enzymatic investigations on the role of Ser558, His610, and Asn614 in the catalytic mechanism of Azotobacter vinelandii dihydrolipoamide acetyltransferase (E2p). |
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[21] |
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PubMed ID | 8918601 |
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Journal | J Mol Biol |
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Year | 1996 |
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Volume | 263 |
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Pages | 463-74 |
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Authors | Wallis NG, Allen MD, Broadhurst RW, Lessard IA, Perham RN |
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Title | Recognition of a surface loop of the lipoyl domain underlies substrate channelling in the pyruvate dehydrogenase multienzyme complex. |
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[22] |
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Comments | STRUCTURE BY NMR OF 1-78. |
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Medline ID | 97234563 |
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PubMed ID | 9119000 |
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Journal | Eur J Biochem |
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Year | 1997 |
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Volume | 244 |
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Pages | 352-60 |
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Authors | Berg A, Vervoort J, de Kok A |
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Title | Three-dimensional structure in solution of the N-terminal lipoyl domain of the pyruvate dehydrogenase complex from Azotobacter vinelandii. |
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Related PDB | 1iyu,1iyv |
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Related UniProtKB | P10802 |
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[23] |
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PubMed ID | 9280309 |
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Journal | FEBS Lett |
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Year | 1997 |
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Volume | 413 |
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Pages | 339-43 |
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Authors | Allen MD, Perham RN |
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Title | The catalytic domain of dihydrolipoyl acetyltransferase from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Expression, purification and reversible denaturation. |
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[24] |
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PubMed ID | 9729480 |
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Journal | Biochem J |
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Year | 1998 |
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Volume | 334 |
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Pages | 703-11 |
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Authors | Jackson JC, Vinluan CC, Dragland CJ, Sundararajan V, Yan B, Gounarides JS, Nirmala NR, Topiol S, Ramage P, Blume JE, Aicher TD, Bell PA, Mann WR |
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Title | Heterologously expressed inner lipoyl domain of dihydrolipoyl acetyltransferase inhibits ATP-dependent inactivation of pyruvate dehydrogenase complex. Identification of important amino acid residues. |
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[25] |
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PubMed ID | 10419491 |
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Journal | J Biol Chem |
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Year | 1999 |
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Volume | 274 |
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Pages | 21769-75 |
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Authors | Thelen JJ, Muszynski MG, David NR, Luethy MH, Elthon TE, Miernyk JA, Randall DD |
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Title | The dihydrolipoamide S-acetyltransferase subunit of the mitochondrial pyruvate dehydrogenase complex from maize contains a single lipoyl domain. |
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[26] |
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PubMed ID | 10653630 |
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Journal | Biochemistry |
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Year | 2000 |
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Volume | 39 |
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Pages | 872-9 |
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Authors | Spector S, Wang M, Carp SA, Robblee J, Hendsch ZS, Fairman R, Tidor B, Raleigh DP |
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Title | Rational modification of protein stability by the mutation of charged surface residues. |
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[27] |
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PubMed ID | 10735853 |
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Journal | J Bacteriol |
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Year | 2000 |
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Volume | 182 |
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Pages | 2119-24 |
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Authors | Stein A, Firshein W |
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Title | Probable identification of a membrane-associated repressor of Bacillus subtilis DNA replication as the E2 subunit of the pyruvate dehydrogenase complex. |
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[28] |
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PubMed ID | 10913250 |
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Journal | Biochemistry |
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Year | 2000 |
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Volume | 39 |
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Pages | 8448-59 |
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Authors | Jones DD, Stott KM, Howard MJ, Perham RN |
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Title | Restricted motion of the lipoyl-lysine swinging arm in the pyruvate dehydrogenase complex of Escherichia coli. |
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Related PDB | 1qjo |
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[29] |
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PubMed ID | 11368334 |
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Journal | Arch Biochem Biophys |
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Year | 2001 |
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Volume | 386 |
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Pages | 123-35 |
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Authors | Liu S, Gong X, Yan X, Peng T, Baker JC, Li L, Robben PM, Ravindran S, Andersson LA, Cole AB, Roche TE |
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Title | Reaction mechanism for mammalian pyruvate dehydrogenase using natural lipoyl domain substrates. |
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[30] |
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PubMed ID | 11114246 |
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Journal | J Mol Biol |
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Year | 2001 |
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Volume | 305 |
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Pages | 49-60 |
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Authors | Jones DD, Stott KM, Reche PA, Perham RN |
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Title | Recognition of the lipoyl domain is the ultimate determinant of substrate channelling in the pyruvate dehydrogenase multienzyme complex. |
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[31] |
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PubMed ID | 12173931 |
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Journal | Biochemistry |
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Year | 2002 |
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Volume | 41 |
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Pages | 10446-53 |
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Authors | Jung HI, Cooper A, Perham RN |
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Title | Identification of key amino acid residues in the assembly of enzymes into the pyruvate dehydrogenase complex of Bacillus stearothermophilus: a kinetic and thermodynamic analysis. |
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[32] |
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PubMed ID | 12526798 |
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Journal | Cell |
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Year | 2003 |
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Volume | 112 |
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Pages | 113-22 |
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Authors | Jogl G, Tong L |
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Title | Crystal structure of carnitine acetyltransferase and implications for the catalytic mechanism and fatty acid transport. |
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comments | This enzyme is Dihydrolipoyllysine-residue acetyltransferase, E2 component of pyruvate dehydrogenase complex. The pyruvate dehydrogenase complex is composed of pyruvate dehydrogenaes (E1 component; E.C. 1.2.4.1), dihydrolipoyllysine S-acetyltransferase (E2 component; E.C. 2.3.1.12), and lipoamide dehydrogenase (E3 component; E.C. 1.8.1.4). (The E3 component corresponds to the entry T00017 in EzCatDB.) This enzyme is composed of three N-terminal lipoyl-binding domains, E1/E3-binding domain, and the C-terminal catalytic domain. Although this enzyme has the same domain composition as that of its homologue (M00189 in EzCatDB), the catalytic residues are slightly different from those of the homologue. (The structure of the catalytic domain of this enzyme has not been solved yet.) This enzyme catalyzes transfer of acetyl group from lypoyllysine of the lipoyl-binding domain to thiol group of CoA. Although the structure of the catalytic domain has not been solved yet, it seems to be homologous to that of its counterpart enzymes from Bacillus stearothermophilus (M00188 in EzCatDB) and human (M00190 in EzCatDB). Moreover, the catalytic residues are nearly conserved, except for Arginine residue (Arg202 of M00188 in EzCatDB).
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created | updated |
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2002-12-01 | 2009-02-26 |
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