ArticleScientific reports2015
Protein evolution analysis of S-hydroxynitrile lyase by complete sequence design utilizing the INTMSAlign software.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Rational Design of the Soluble Variant of l-Pipecolic Acid Hydroxylase using the α-Helix Rule and the Hydropathy Contradiction Rule.ACS omega · 2022Article
- Protein engineering of the aldoxime dehydratase from Bacillus sp. OxB-1 based on a rational sequence alignment approach.Scientific reports · 2021Article
- AirID, a novel proximity biotinylation enzyme, for analysis of protein-protein interactions.eLife · 2020Article
- Rational identification of aggregation hotspots based on secondary structure and amino acid hydrophobicity.Scientific reports · 2017Article
- Catalytic Promiscuity of Ancestral Esterases and Hydroxynitrile Lyases.Journal of the American Chemical Society · 2016Article
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Authors and funding
2 authors.
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Abstract
Development of software and methods for design of complete sequences of functional proteins could contribute to studies of protein engineering and protein evolution. To this end, we developed the INTMSAlign software, and used it to design functional proteins and evaluate their usefulness. The software could assign both consensus and correlation residues of target proteins. We generated three protein sequences with S-selective hydroxynitrile lyase (S-HNL) activity, which we call designed S-HNLs; these proteins folded as efficiently as the native S-HNL. Sequence and biochemical analysis of the designed S-HNLs suggested that accumulation of neutral mutations occurs during the process of S-HNLs evolution from a low-activity form to a high-activity (native) form. Taken together, our results demonstrate that our software and the associated methods could be applied not only to design of complete sequences, but also to predictions of protein evolution, especially within families such as esterases and S-HNLs.
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