A minimal peptide substrate in biotin holoenzyme synthetase‐catalyzed biotinylation
Open Access
- 1 January 1999
- journal article
- Published by Wiley in Protein Science
- Vol. 8 (4), 921-929
- https://doi.org/10.1110/ps.8.4.921
Abstract
Protein Science, the flagship journal of The Protein Society, serves an international forum for publishing original reports on all scientific aspects of protein molecules. The Journal publishes papers by leading scientists from all over the world that report on advances in the understanding of proteins in the broadest sense. Protein Science aims to unify this field by cutting across established disciplinary lines and focusing on “protein-centered” science.Keywords
This publication has 40 references indexed in Scilit:
- Structural characterization of the entire 1.3S subunit of transcarboxylase from Propionibacterium shermaniiProtein Science, 1998
- Structure of the Carboxy-Terminal Fragment of the Apo-Biotin Carboxyl Carrier Subunit ofEscherichia coliAcetyl-CoA CarboxylaseBiochemistry, 1997
- Phenotypic Analysis of Antigen-Specific T LymphocytesScience, 1996
- Purification and Characterization of Intact and Truncated Forms of the Escherichia coli Biotin Carboxyl Carrier Subunit of Acetyl-CoA CarboxylaseJournal of Biological Chemistry, 1996
- A versatile plasmid expression vector for the production of biotinylated proteins by site-specific, enzymatic modification in Escherichia coliGene, 1996
- Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasingStructure, 1995
- Catalytic specificity of protein-tyrosine kinases is critical for selective signallingNature, 1995
- Use of Peptide Libraries to Map the Substrate Specificity of a Peptide-Modifying Enzyme: A 13 Residue Consensus Peptide Specifies Biotinylation in Escherichia coliNature Biotechnology, 1993
- Cooperative binding of the Escherichia coli repressor of biotin biosynthesis to the biotin operator sequenceBiochemistry, 1993
- Prediction of the three‐dimensional structures of the biotinylated domain from yeast pyruvate carboxylase and of the lipoylated H‐protein from the pea leaf glycine cleavage system: A new automated method for the prediction of protein tertiary structureProtein Science, 1993