Protejezelike

Protejezelike refers to proteins or protein domains that adopt a protease-like fold or substrate-binding mode but do not display proteolytic catalytic activity. The term appears in speculative and design-focused literature and is not part of a formal, universally accepted classification. In many proposals, protejezelike molecules retain the structural features common to serine or metalloproteases—such as a paired catalytic-cleft geometry or a solvent-accessible binding pocket—yet lack one or more catalytic residues, rendering them catalytically inactive.

Structural and functional properties: Protejezelike candidates often remain structurally stable and can bind peptide substrates or inhibitors with affinities similar to active proteases, even though they do not hydrolyze substrates. Some may exhibit conformational flexibility that modulates binding or acts as a decoy for proteases, influencing proteolytic networks.

Potential roles and applications: In biology, they are hypothesized to act as regulators of proteolysis, scaffolds for protease complexes, or decoys that temper protease activity. In synthetic biology and drug design, protejezelike scaffolds are used to study substrate recognition, to engineer specificity, or to create protease-inhibitor interfaces without triggering substrate turnover.

Discovery and status: The concept has been explored mainly through computational modeling, directed evolution, and structural studies of inactive homologs. There is no established clinical or industrial application, and practical assessment requires careful evaluation of stability, binding, and regulation in relevant systems.