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• W2155920303 endingPage "4103" @default.
• W2155920303 startingPage "4091" @default.
• W2155920303 abstract "ABSTRACT Herpesviruses encode an essential, maturational serine protease whose catalytic domain, assemblin (28 kDa), is released by self-cleavage from a 74-kDa precursor (pPR, pUL80a). Although there is considerable information about the structure and enzymatic characteristics of assemblin, a potential pharmacologic target, comparatively little is known about these features of the precursor. To begin studying pPR, we introduced five point mutations that stabilize it against self-cleavage at its internal (I), cryptic (C), release (R), and maturational (M) sites and at a newly discovered “tail” (T) site. The resulting mutants, called ICRM-pPR and ICRMT-pPR, were expressed in bacteria, denatured in urea, purified by immobilized metal affinity chromatography, and renatured by a two-step dialysis procedure and by a new method of sedimentation into glycerol gradients. The enzymatic activities of the pPR mutants were indistinguishable from that of IC-assemblin prepared in parallel for comparison, as determined by using a fluorogenic peptide cleavage assay, and approximated rates previously reported for purified assemblin. The percentage of active enzyme in the preparations was also comparable, as determined by using a covalent-binding suicide substrate. An unexpected finding was that, in the absence of the kosmotrope Na 2 SO 4 , optimal activity of pPR requires interaction through its scaffolding domain. We conclude that although the enzymatic activities of assemblin and its precursor are comparable, there may be differences in how their catalytic sites become fully activated." @default.
• W2155920303 created "2016-06-24" @default.
• W2155920303 creator A5066860229 @default.
• W2155920303 creator A5074625066 @default.
• W2155920303 date "2007-04-15" @default.
• W2155920303 modified "2023-10-16" @default.
• W2155920303 title "Enzymatic Activities of Human Cytomegalovirus Maturational Protease Assemblin and Its Precursor (pPR, pUL80a): Maximal Activity of pPR Requires Self-Interaction through Its Scaffolding Domain" @default.
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• W2155920303 doi "https://doi.org/10.1128/jvi.02821-06" @default.
• W2155920303 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1900282" @default.
• W2155920303 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17287260" @default.
• W2155920303 hasPublicationYear "2007" @default.
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