ArticleJournal of molecular biology2013
Janus: prediction and ranking of mutations required for functional interconversion of enzymes.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 27 citations in OpenAlex.
- Computational remodeling of an enzyme conformational landscape for altered substrate selectivity.Nature communications · 2023Article
- Odd one out? Functional tuning of Zymomonas mobilis pyruvate kinase is narrower than its allosteric, human counterpart.Protein science : a publication of the Protein Society · 2022Article
- RNA binding candidates for human ADAR3 from substrates of a gain of function mutant expressed in neuronal cells.Nucleic acids research · 2019Article
- Computational tools for the evaluation of laboratory-engineered biocatalysts.Chemical communications (Cambridge, England) · 2016Review
- Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.Chemical Society reviews · 2015Review
- Directed evolution of the substrate specificity of dialkylglycine decarboxylase.Biochimica et biophysica acta · 2015Article
- Aspartate aminotransferase: an old dog teaches new tricks.Archives of biochemistry and biophysics · 2014Review
- Prediction of detailed enzyme functions and identification of specificity determining residues by random forests.PloS one · 2014Article
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Identification of residues responsible for functional specificity in enzymes is a challenging and important problem in protein chemistry. Active-site residues are generally easy to identify, but residues outside the active site are also important to catalysis and their identities and roles are more difficult to determine. We report a method based on analysis of multiple sequence alignments, embodied in our program Janus, for predicting mutations required to interconvert structurally related but functionally distinct enzymes. Conversion of aspartate aminotransferase into tyrosine aminotransferase is demonstrated and compared to previous efforts. Incorporation of 35 predicted mutations resulted in an enzyme with the desired substrate specificity but low catalytic activity. A single round of DNA back-shuffling with wild-type aspartate aminotransferase on this variant generated mutants with tyrosine aminotransferase activities better than those previously realized from rational design or directed evolution. Methods such as this, coupled with computational modeling, may prove invaluable in furthering our understanding of enzyme catalysis and engineering.
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Registered trials
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