.../PAGE. The active-site motif of aspartic proteinases, Asp-Ser-Gly, was present in the 23 kDa protein corresponding to the C-terminal half of the precursor protein. The coding region of this daughter protein (152 residues) in the copia gag gene was expressed in E. coli to produce the recombinant enzyme...

... at pH approx. 2.6 towards acid-denatured haemoglobin; the specificity of nepenthesin I towards oxidized insulin B chain appears to be similar, but slightly wider than those of other APs (aspartic proteinases). Among the enzymic properties, however, the most notable is their unusual stability: both...

...Kenneth G. PAYIE; Takuji TANAKA; Susannah GAL; Rickey Y. YADA Aspartic proteinases are a well-characterized class of proteinases. In plants, all nascent aspartic proteinases possess a 100-amino-acid, plant-specific sequence (PSS) within their C-terminal lobe, presumed to possess a targeting role...

..., hydrogen bonds in triosephosphate isomerase reorganized during catalysis [6]. Loop structures have been identified in many enzymes where they have been implicated in protein function, stability and possibly in protein folding. In aspartic proteinases, a loop, commonly known as a flap, is found to extend...