ArticleProceedings of the National Academy of Sciences of the United States of America1999
Selection for improved subtiligases by phage display.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Nature-inspired protein ligation and its applications.Nature reviews. Chemistry · 2023Review
- Challenges in the use of sortase and other peptide ligases for site-specific protein modification.Chemical Society reviews · 2022Review
- From thiol-subtilisin to omniligase: Design and structure of a broadly applicable peptide ligase.Computational and structural biotechnology journal · 2021Article
- Engineered peptide ligases for cell signaling and bioconjugation.Biochemical Society transactions · 2020Review
- Enzyme-Based Labeling Strategies for Antibody-Drug Conjugates and Antibody Mimetics.Antibodies (Basel, Switzerland) · 2018Review
- Phage-Enabled Nanomedicine: From Probes to Therapeutics in Precision Medicine.Angewandte Chemie (International ed. in English) · 2017Review
- Reprogramming Caspase-7 Specificity by Regio-Specific Mutations and Selection Provides Alternate Solutions for Substrate Recognition.ACS chemical biology · 2016Article
- N-terminal protein modification using simple aminoacyl transferase substrates.Journal of the American Chemical Society · 2011Article
- Characterisation of a DNA polymerase highly mutated along the template binding interface.Molecular biotechnology · 2010Article
- Parallel in vivo and in vitro selection using phage display identifies protease-dependent tumor-targeting peptides.The Journal of biological chemistry · 2010Article
- Phage display in molecular imaging and diagnosis of cancer.Chemical reviews · 2010Review
- Inflammatory stimuli regulate caspase substrate profiles.Molecular & cellular proteomics : MCP · 2010Article
- Sampling the N-terminal proteome of human blood.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Ab initio folding of terminal segments with secondary structures reveals the fine difference between two closely related all-atom statistical energy functions.Protein science : a publication of the Protein Society · 2008Article
- De novo designed cyclic-peptide heme complexes.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Efficient display of two enzymes on filamentous phage using an improved signal sequence.Molecular biotechnology · 2003Article
- Directed evolution of an extremely fast phosphotriesterase by in vitro compartmentalization.The EMBO journal · 2003Article
- Chemical complementation: a reaction-independent genetic assay for enzyme catalysis.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- A novel strategy for the functional cloning of enzymes using filamentous phage display: the case of nucleotidyl transferases.Nucleic acids research · 2002Article
- Molecular markers of serine protease evolution.The EMBO journal · 2001Article
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2 authors.
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Abstract
Engineering enzyme activity has been challenging because of uncertainties in structure-function relationships and difficulties in screening a large number of mutant enzymes. A product capture strategy using phage display is presented here for the selection of improved enzymes from a large library of variants (>10(9) independently derived mutants). Subtiligase, a double mutant of subtilisin BPN' that catalyzes the ligation of peptides, was displayed on phage. Twenty-five active site residues were randomly mutated in groups of four or five to yield six different libraries that were independently sorted. Variants that ligated a biotin peptide onto their own extended N termini were selectively captured. Mutant subtiligases were identified that had increased ligase activity. The selection also yielded unexpected subtiligase mutants having residues known to improve the stability and oxidative resistance of wild-type subtilisin. These studies are exemplary for the use of phage to improve enzyme function when it is closely linked to a selectable catalytic event.
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