...Amy L. Stiegler; Titus J. Boggon Pseudoenzymes generally lack detectable catalytic activity despite adopting the overall protein fold of their catalytically competent counterparts, indeed ‘pseudo’ family members seem to be incorporated in all enzyme classes. The small GTPase enzymes are important...

...-catalytic functions that can be exerted by conventional protein kinases. allosteric regulation protein–protein interactions pseudoenzyme pseudokinases signalling Counterparts of active enzymes that lack key catalytic residues and are therefore predicted to possess defective catalytic...

...James M. Murphy; Hesso Farhan; Patrick A. Eyers Pseudoenzymes are catalytically dead counterparts of enzymes. Despite their first description some 50 years ago, the importance and functional diversity of these ‘fit-for-purpose’ polypeptides is only now being appreciated. Pseudoenzymes have been...

...Veronika Reiterer; Krzysztof Pawłowski; Hesso Farhan The pseudophosphatase STYX (serine/threonine/tyrosine interacting protein) is a catalytically inactive member of the protein tyrosine phosphatase family. We perform a phylogenetic analysis of STYX and ask how far does the pseudoenzyme status...

... pseudoenzyme pseudokinase thermal shift assay Protein kinase complements, or ‘kinomes’, are found within, and regulate cell biology across, all annotated phyla, including archaea, bacteria, plants and animals. The human kinome comprises >500 proteins that are responsible for the transient...