Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
1 to 25 of 30  Show
  1. 1
    "The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component."
    Stephens P.E., Darlison M.G., Lewis H.M., Guest J.R.
    Eur. J. Biochem. 133:481-489(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], LIPOYLATION AT LYS-41; LYS-144 AND LYS-245.
    Category: Sequences.
    Strain: K12.
    Source: UniProtKB/Swiss-Prot (reviewed).
  2. 2
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 4451 other entries.

  3. 3
    "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 4275 other entries.

  4. 4
    "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Category: Sequences.
    Strain: K12 / EMG2.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 220 other entries.

  5. 5
    "Amino acid sequence around lipoic acid residues in the pyruvate dehydrogenase multienzyme complex of Escherichia coli."
    Hale G., Perham R.N.
    Biochem. J. 187:905-908(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 35-47, LIPOYLATION AT LYS-41.
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).
  6. 6
    "Overexpression of restructured pyruvate dehydrogenase complexes and site-directed mutagenesis of a potential active-site histidine residue."
    Russel G.C., Guest J.R.
    Biochem. J. 269:443-450(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-603.
    Category: Pathology & Biotech.
    Source: UniProtKB/Swiss-Prot (reviewed).
  7. 7
    "Isolation and characterization of lipoylated and unlipoylated domains of the E2p subunit of the pyruvate dehydrogenase complex of Escherichia coli."
    Ali S.T., Guest J.R.
    Biochem. J. 271:139-145(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: LIPOYLATED DOMAINS STUDIES, LIPOYLATION AT LYS-144.
    Category: Family & Domains.
    Source: UniProtKB/Swiss-Prot (reviewed).
  8. 8
    "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 299 other entries.

  9. 9
    "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-396, IDENTIFICATION BY MASS SPECTROMETRY.
    Category: PTM / Processing, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 89 other entries.

  10. 10
    "Protein-protein interaction revealed by NMR T(2) relaxation experiments: the lipoyl domain and E1 component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus."
    Howard M.J., Chauhan H.J., Domingo G.J., Fuller C., Perham R.N.
    J. Mol. Biol. 295:1023-1037(2000) [PubMed] [Europe PMC] [Abstract]
    Category: Structure.
    Source: PDB:1QJO.
  11. 11
    "Restricted motion of the lipoyl-lysine swinging arm in the pyruvate dehydrogenase complex of Escherichia coli."
    Jones D.D., Stott K.M., Howard M.J., Perham R.N.
    Biochemistry 39:8448-8459(2000) [PubMed] [Europe PMC] [Abstract]
    Category: Structure.
    Source: PDB:1QJO.
  12. 12
    "Histidine 407, a phantom residue in the E1 subunit of the Escherichia coli pyruvate dehydrogenase complex, activates reductive acetylation of lipoamide on the E2 subunit. An explanation for conservation of active sites between the E1 subunit and transketolase."
    Nemeria N., Arjunan P., Brunskill A., Sheibani F., Wei W., Yan Y., Zhang S., Jordan F., Furey W.
    Biochemistry 41:15459-15467(2002) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Source: BioCyc:MetaCyc:E2P-MONOMER, BioCyc:EcoCyc:E2P-MONOMER.
  13. 13
    "Expression and purification of the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase subunits of the Escherichia coli pyruvate dehydrogenase multienzyme complex: a mass spectrometric assay for reductive acetylation of dihydrolipoamide acetyltransferase."
    Wei W., Li H., Nemeria N., Jordan F.
    Protein Expr. Purif. 28:140-150(2003) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Source: BioCyc:MetaCyc:E2P-MONOMER, BioCyc:EcoCyc:E2P-MONOMER.
  14. 14
    "Interaction network containing conserved and essential protein complexes in Escherichia coli."
    Butland G., Peregrin-Alvarez J.M., Li J., Yang W., Yang X., Canadien V., Starostine A., Richards D., Beattie B., Krogan N., Davey M., Parkinson J., Greenblatt J., Emili A.
    Nature 433:531-537(2005) [PubMed] [Europe PMC] [Abstract]
    Category: Interaction.
    Source: IntAct:P06959.

    This publication is mapped to 1271 other entries.

  15. 15
    Category: Interaction.
    Source: IntAct:P06959.

    This publication is mapped to 2444 other entries.

  16. 16
    "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis."
    Lasserre J.P., Beyne E., Pyndiah S., Lapaillerie D., Claverol S., Bonneu M.
    Electrophoresis 27:3306-3321(2006) [PubMed] [Europe PMC] [Abstract]
    Category: Interaction.
    Source: IntAct:P06959.

    This publication is mapped to 225 other entries.

  17. 17
    "Rotational diffusion studies of the lipoyl domain of 2-oxoacid dehydrogenase multienzyme complexes."
    Harrison J.P., Morrison I.E., Cherry R.J.
    Biochemistry 29:5596-5604(1990) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Source: BioCyc:MetaCyc:E2P-MONOMER, BioCyc:EcoCyc:E2P-MONOMER.
  18. 18
    "A surface loop directs conformational switching of a lipoyl domain between a folded and a novel misfolded structure."
    Stott K.M., Yusof A.M., Perham R.N., Jones D.D.
    Structure 17:1117-1127(2009) [PubMed] [Europe PMC] [Abstract]
    Category: Structure.
    Source: PDB:2K7V.
  19. 19
    "Differential effect of YidC depletion on the membrane proteome of Escherichia coli under aerobic and anaerobic growth conditions."
    Price C.E., Otto A., Fusetti F., Becher D., Hecker M., Driessen A.J.
    Proteomics 10:3235-3247(2010) [PubMed] [Europe PMC] [Abstract]
    Category: Interaction.
    Source: IntAct:P06959.

    This publication is mapped to 33 other entries.

  20. 20
    "The binary protein-protein interaction landscape of Escherichia coli."
    Rajagopala S.V., Sikorski P., Kumar A., Mosca R., Vlasblom J., Arnold R., Franca-Koh J., Pakala S.B., Phanse S., Ceol A., Hauser R., Siszler G., Wuchty S., Emili A., Babu M., Aloy P., Pieper R., Uetz P.
    Nat. Biotechnol. 32:285-290(2014) [PubMed] [Europe PMC] [Abstract]
    Category: Interaction.
    Source: IntAct:P06959.

    This publication is mapped to 1250 other entries.

  21. 21
    "Acetylatable lipoic acid residues interact directly with lipoamide dehydrogenase in the pyruvate dehydrogenase multienzyme complex of Escherichia coli."
    Adamson S.R., Holmes C.F., Stevenson K.J.
    Biochem. Cell Biol. 64:250-255(1986) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Source: BioCyc:MetaCyc:E2P-MONOMER, BioCyc:EcoCyc:E2P-MONOMER.
  22. 22
    "Dihydrolipoyl transacetylase of Escherichia coli. Formation of 8-S-acetyldihydrolipoamide."
    Yang Y.S., Frey P.A.
    Biochemistry 25:8173-8178(1986) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Source: BioCyc:MetaCyc:E2P-MONOMER, BioCyc:EcoCyc:E2P-MONOMER.
  23. 23
    "Biochemical genetics of the alpha-keto acid dehydrogenase complexes of Escherichia coli K12: isolation and biochemical properties of deletion mutants."
    Langley D., Guest J.R.
    J. Gen. Microbiol. 99:263-276(1977) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Source: BioCyc:MetaCyc:E2P-MONOMER, BioCyc:EcoCyc:E2P-MONOMER.
  24. 24
    "A mutant pyruvate dehydrogenase complex of Escherichia coli deleted in the (alanine + proline)-rich region of the acetyltransferase component."
    Miles J.S., Guest J.R., Radford S.E., Perham R.N.
    Biochim. Biophys. Acta 913:117-121(1987) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Source: BioCyc:MetaCyc:E2P-MONOMER, BioCyc:EcoCyc:E2P-MONOMER.
  25. 25
    "Pyruvate dehydrogenase complex of Escherichia coli. Thiamin pyrophosphate and NADH-dependent hydrolysis of acetyl-CoA."
    CaJacob C.A., Gavino G.R., Frey P.A.
    J. Biol. Chem. 260:14610-14615(1985) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Source: BioCyc:MetaCyc:E2P-MONOMER, BioCyc:EcoCyc:E2P-MONOMER.
1 to 25 of 30  Show
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again