ArticleProtein science : a publication of the Protein Society2021
Analysis of electrostatic coupling throughout the laboratory evolution of a designed retroaldolase.
Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 5 citations in OpenAlex.
- MAHOMES II: A webserver for predicting if a metal binding site is enzymatic.Protein science : a publication of the Protein Society · 2023Article
- MAHOMES II: A webserver for predicting if a metal binding site is enzymatic.bioRxiv : the preprint server for biology · 2023Article
- Understanding Self-Assembly of Silica-Precipitating Peptides to Control Silica Particle Morphology.Advanced materials (Deerfield Beach, Fla.) · 2023Article
- Analysis of electrostatic coupling throughout the laboratory evolution of a designed retroaldolase.Protein science : a publication of the Protein Society · 2021Article
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Authors and funding
5 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The roles of local interactions in the laboratory evolution of a highly active, computationally designed retroaldolase (RA) are examined. Partial Order Optimum Likelihood (POOL) is used to identify catalytically important amino acid interactions in several RA95 enzyme variants. The series RA95.5, RA95.5-5, RA95.5-8, and RA95.5-8F, representing progress along an evolutionary trajectory with increasing activity, is examined. Computed measures of coupling between charged states of residues show that, as evolution proceeds and higher activities are achieved, electrostatic coupling between the biochemically active amino acids and other residues is increased. In silico residue scanning suggests multiple coupling partners for the catalytic lysine K83. The effects of two predicted partners, Y51 and E85, are tested using site-directed mutagenesis and kinetic analysis of the variants Y51F and E85Q. The Y51F variants show decreases in k
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