The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity

This publication has 31 references indexed in Scilit:

• Solution Structures of Apo and Holo Biotinyl Domains from Acetyl Coenzyme A Carboxylase of Escherichia coli Determined by Triple-Resonance Nuclear Magnetic Resonance Spectroscopy
  Biochemistry, 1999
• A minimal peptide substrate in biotin holoenzyme synthetase‐catalyzed biotinylation
  Protein Science, 1999
• Structural characterization of the entire 1.3S subunit of transcarboxylase from Propionibacterium shermanii
  Protein Science, 1998
• Coupling of Site-Specific DNA Binding to Protein Dimerization in Assembly of the Biotin Repressor−Biotin Operator Complex
  Biochemistry, 1998
• Structure of the Carboxy-Terminal Fragment of the Apo-Biotin Carboxyl Carrier Subunit ofEscherichia coliAcetyl-CoA Carboxylase
  Biochemistry, 1997
• Evidence for Interdomain Interaction in the Escherichia coli Repressor of Biotin Biosynthesis from Studies of an N-Terminal Domain Deletion Mutant
  Biochemistry, 1996
• Evidence for Distinct Ligand-Bound Conformational States of the Multifunctional Escherichia coli Repressor of Biotin Biosynthesis
  Biochemistry, 1995
• A tale of two synthetases
  Nature Structural & Molecular Biology, 1994
• Kinetics of Biotinyl-5'-adenylate Synthesis Catalyzed by the Escherichia coli Repressor of Biotin Biosynthesis and the Stability of the Enzyme-Product Complex
  Biochemistry, 1994
• Use of Peptide Libraries to Map the Substrate Specificity of a Peptide-Modifying Enzyme: A 13 Residue Consensus Peptide Specifies Biotinylation in Escherichia coli
  Nature Biotechnology, 1993