Discovery Of A Novel Protease With High Specificity Toward Serine Side Chains

Tech ID: 30087 / UC Case 2019-085-0

Patent Status

Patent Pending

Brief Description

Pyrroloquinoline quinone (PQQ), a prominent redox cofactor in a variety of prokaryotes, is produced from a ribosomally synthesized and post-translationally modified peptide PqqA via a pathway comprised of four conserved proteins PqqB-PqqE. These four proteins are now fairly well characterized and span Radical SAM activity (PqqE), aided by a peptide chaperone (PqqD), a dual hydroxylase (PqqB), and an eight electron, eight proton oxidase (PqqC). A full description of this pathway has been hampered by a lack of information regarding a protease/peptidase required for the excision of an early, cross-linked di-amino acid precursor to PQQ. 


UC Berkeley researchers have isolated and characterized a two component, heterodimer protein that is able to rapidly catalyze cleavage of PqqA into smaller peptides.  The UC researchers have developed: novel proteases that can cut peptide bonds both N- and C- terminal to the amino acid serine; compositions comprising such proteases; and methods of use, including to assay the extent, position, and time course of protein phosphorylation at serine side chains. 

Suggested uses

  • proteomic analyses of the large family of proteins that have undergone post-translational phosphorylation at serine



  • proteases that can cut peptide bonds both N- and C- terminal to the amino acid serine


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  • Klinman, Judith P.

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