Structure and posttranslational modification of lipoyl domain of 2-oxo-acid dehydrogenase multienzyme complexes.
Perham
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Cambridge Centre for Molecular Recognition, Department of Biochemistry, University of Cambridge, United Kingdom.
D042942:3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide); D000107:Acetylation; D000215:Acylation; D000595:Amino Acid Sequence; D002250:Carbon Radioisotopes; D002850:Chromatography, Gel / Q000379:methods; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D004926:Escherichia coli; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D007658:Ketone Oxidoreductases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D010446:Peptide Fragments / Q000737:chemistry* / Q000302:isolation & purification; D017510:Protein Folding; D011499:Protein Processing, Post-Translational; D017433:Protein Structure, Secondary; D011768:Pyruvate Dehydrogenase Complex / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D011773:Pyruvates / Q000378:metabolism; D019289:Pyruvic Acid; D011865:Radioisotope Dilution Technique; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism
D002250:Carbon Radioisotopes; D009097:Multienzyme Complexes; D010446:Peptide Fragments; D011768:Pyruvate Dehydrogenase Complex; D011773:Pyruvates; D011994:Recombinant Proteins; D019289:Pyruvic Acid; D007658:Ketone Oxidoreductases; D042942:3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)