ArticleMethods in enzymology2022
Methods for discovering catalytic activities for pseudokinases.
Article in Methods in enzymology, 2022. 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.
- TIR-like NADases act in bacterial immunity and the RNA vault.bioRxiv : the preprint server for biology · 2026Article
- Biochemical and structural insights into a 5' to 3' RNA ligase reveal a potential role in tRNA ligation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Biochemical and structural insights into a 5' to 3' RNA ligase reveal a potential role in tRNA ligation.bioRxiv : the preprint server for biology · 2024Article
- KINtaro: protein kinase-like database.BMC research notes · 2024Article
- Pan-kinome of Legionella expanded by a bioinformatics survey.Scientific reports · 2022Article
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4 authors.
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Abstract
Pseudoenzymes resemble active enzymes, but lack key catalytic residues believed to be required for activity. Many pseudoenzymes appear to be inactive in conventional enzyme assays. However, an alternative explanation for their apparent lack of activity is that pseudoenzymes are being assayed for the wrong reaction. We have discovered several new protein kinase-like families which have revealed how different binding orientations of adenosine triphosphate (ATP) and active site residue migration can generate a novel reaction from a common kinase scaffold. These results have exposed the catalytic versatility of the protein kinase fold and suggest that atypical kinases and pseudokinases should be analyzed for alternative transferase activities. In this chapter, we discuss a general approach for bioinformatically identifying divergent or atypical members of an enzyme superfamily, then present an experimental approach to characterize their catalytic activity.
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