Structure and posttranslational modification of lipoyl domain of 2-oxo-acid dehydrogenase multienzyme complexes

Methods Enzymol. 1995;251:436-48. doi: 10.1016/0076-6879(95)51147-4.
No abstract available

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)
  • Acetylation
  • Acylation
  • Amino Acid Sequence
  • Carbon Radioisotopes
  • Chromatography, Gel / methods
  • Cloning, Molecular
  • Electrophoresis, Polyacrylamide Gel / methods
  • Escherichia coli
  • Geobacillus stearothermophilus / enzymology*
  • Ketone Oxidoreductases / chemistry*
  • Ketone Oxidoreductases / isolation & purification
  • Ketone Oxidoreductases / metabolism*
  • Kinetics
  • Magnetic Resonance Spectroscopy / methods
  • Models, Molecular
  • Molecular Sequence Data
  • Multienzyme Complexes / chemistry*
  • Multienzyme Complexes / isolation & purification
  • Multienzyme Complexes / metabolism*
  • Peptide Fragments / chemistry*
  • Peptide Fragments / isolation & purification
  • Protein Folding
  • Protein Processing, Post-Translational*
  • Protein Structure, Secondary*
  • Pyruvate Dehydrogenase Complex / chemistry*
  • Pyruvate Dehydrogenase Complex / isolation & purification
  • Pyruvate Dehydrogenase Complex / metabolism*
  • Pyruvates / metabolism
  • Pyruvic Acid
  • Radioisotope Dilution Technique
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism

Substances

  • Carbon Radioisotopes
  • Multienzyme Complexes
  • Peptide Fragments
  • Pyruvate Dehydrogenase Complex
  • Pyruvates
  • Recombinant Proteins
  • Pyruvic Acid
  • Ketone Oxidoreductases
  • 3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)