Conversion of cysteinyl residues to unnatural amino acid analogs. Examination in a model system
- 1 November 1996
- journal article
- Published by Springer Nature in Protein Journal
- Vol. 15 (8) , 737-742
- https://doi.org/10.1007/bf01887147
Abstract
Improved and efficient techniques have led to an explosive growth in the application of site-directed mutagenesis to the study of enzymes. However, the limited availability of only those 20 amino acids that are translated by the genetic code has prevented the systematic variation of an amino acid's properties in order to define more precisely its role in the catalytic mechanism of an enzyme. An approach is being examined that combines the high specificity of site-directed mutagenesis with the flexibility of chemical modification to overcome these limitations. A set of reagents has been synthesized and reacted with a cysteine model to produce a series of amino acid structural analogs at appreciable rates and in good overall yields. The selective incorporation of these analogs in place of important functional amino acids in a protein will allow a more detailed examination of the role of that amino acid.Keywords
This publication has 19 references indexed in Scilit:
- Regeneration of catalytic activity of glutamine synthetase mutants by chemical activation: Exploration of the role of arginines 339 and 359 in activityProtein Science, 1994
- Sequential site-directed mutagenesis and chemical modification to convert the active site arginine 292 of aspartate aminotransferase to homoarginineJournal of the American Chemical Society, 1992
- Reengineering the catalytic lysine of aspartate aminotransferase by chemical elaboration of a genetically introduced cysteineBiochemistry, 1991
- Mischarging Escherichia coli tRNAPhe with L-4'-[3-(trifluoromethyl)-3H-diazirin-3-yl]phenylalanine, a photoactivatable analog of phenylalanineBiochemistry, 1988
- Subtle alteration of the active site of ribulose bisphosphate carboxylase/oxygenase by concerted site-directed mutagenesis and chemical modificationBiochemical and Biophysical Research Communications, 1988
- N,iε-Acetyllysine transfer ribonucleic acid: a biologically active analogue of aminoacyl transfer ribonucleic acidsBiochemistry, 1976
- Structural invariants in protein foldingNature, 1975
- Reaction of papain with α-bromo-β-(5-imidazolyl)propionic acidBiochemistry, 1972
- Enzymic replacement of the arginyl by a lysyl residue in the reactive site of soybean trypsin inhibitorBiochemistry, 1969
- The Synthesis of Some Amines and Amino Acids Containing the Pyrazole NucleusJournal of the American Chemical Society, 1949