![]() Stennicke, unpublished results), human α 1-proteinase inhibitor (α1-PI) and an inhibitor from the seeds of bitter gourd ( K i 70 nM). Ī number of protein inhibitors of GluSGP have been described, e.g., wild-type and mutant turkey ovomucoid third domain, with the Leu18Glu mutant being the most potent ( K i 0.02 nM), the GluSGP propeptide ( K i 0.5 nM) (H.S. This is in agreement with the ability of GluSGP to distinguish between Glu and Gln in the P1 position. ![]() Furthermore, the pH dependence of K m for the hydrolysis of Suc-Ala-Ala-Pro- Glu↓NHPhNO 2 showed that the protonated form of Glu was not accepted as a substrate. This indicates that His213, which is involved in the substrate binding, remains capable of donating a hydrogen bond to the substrate even at high pH. The pH dependence of k cat/ K m for glutamyl endopeptidase II (GluSGP) has also been thoroughly investigated and it has been found to differ from that of glutamyl endopeptidase I in that activity does not approach zero even at high pH. Chloromethane derivatives of glutamic and aspartic acid-containing peptides have also been found to inhibit GluSGP. However, they are not efficiently inhibited by PMSF. Both GluSGP and GluSF have been found to be irreversibly inhibited by DFP and Boc-Phe-Leu-Glu-CH 2Cl.
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