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Engineering an enzyme by site-directed mutagenesis to be resistant to chemical oxidation.
Open accessAbstract
Site-directed mutagenesis can be employed to alter activity critical residues in proteins which are susceptible to chemical oxidation. Previous studies have implicated methionine 222 as a primary site for oxidative inactivation of subtilisin (Stauffer, C. E., and Etson, D. (1969) J. Biol. Chem. 244, 5333-5338). Because of uncertainties in predicting which amino acid would be the optimal substitute for methionine 222, we prepared all 19 amino acid substitutions at this site in the cloned subtilisin gene using a cassette mutagenesis method (Wells, J. A., Vasser, M., and Powers, D. P. (1985) Gene (Amst.), in press). Mutant enzymes were expressed in Bacillus subtilis and were found to vary widely in specific activity. Mutants containing nonoxidizable amino acids (i.e. Ser, Ala, and Leu) were resistant to inactivation by 1 M H2O2, whereas methionine and cysteine enzymes were rapidly inactivated. These studies demonstrate the feasibility of improving oxidative stability in proteins by site-directed mutagenesis.
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Cites
An Algorithm for Least-Squares Estimation of Nonlinear Parameters
Marquardt, D. W. (1963) · Journal of the Society for Industrial and Applied Mathematics · doi:10.1137/0111030 · Cited by 30,728
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Engineering the third wave of biocatalysis
Bornscheuer, U. T., Huisman, G. W., Kazlauskas, R. J., Lutz, S., Moore, J. C., & Robins, K. (2012) · Nature · doi:10.1038/nature11117 · Cited by 2,628
The oxidative environment and protein damage
Davies, M. J. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.08.007 · Cited by 1,392
The Crucial Role of Methodology Development in Directed Evolution of Selective Enzymes
Qu, G., Li, A., Acevedo‐Rocha, C. G., Sun, Z., & Reetz, M. T. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.201901491 · Cited by 473
Requirement of pro-sequence for the production of active subtilisin E in Escherichia coli.
Ikemura, H., Takagi, H., & Inouye, M. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47646-6 · Cited by 335
Maurer, K.-H. (2004) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2004.06.005 · Cited by 299
Metadata
- Authors
- Estell, D. A., Graycar, T. P., & Wells, J. A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1985-06
- Volume
- 260
- Issue
- 11
- Pages
- 6518-6521
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1590376353
- Cited by
- 337
- References
- 1
- FWCI
- 7.29
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Estell, D. A., Graycar, T. P., & Wells, J. A. (1985). Engineering an enzyme by site-directed mutagenesis to be resistant to chemical oxidation. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)88811-1
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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