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- W2016454001 abstract "An effective method for the determination of the activity of signal peptidase I (SPase I) ofEscherichia colisis established using the hybrid protein pro-OmpA-nuclease A as substrate. Pro-OmpA-nuclease A, a hybrid secretory precursor was purified to homogeneity under denaturing conditions. When this protein was refolded, it could quantitatively processes by purified SPase I. TheKmof signal peptidase I was 0.0165 mM. Thekcatwas 8.73 s−1. TheKmis 50 to 100 times lower than that obtained with peptide substrates indicating that SPase I has a significantly greater affinity for the protein substrate. The turnover number,kcat, is two to four orders of magnitude greater as well. Thus, the specificity constant,kcat/Kmis six orders of magnitude greater with pro-OmpA-nuclease A than with peptide substrates. This is the first determination of kinetics of SPase I with a protein substrate." @default.
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- W2016454001 date "1995-01-01" @default.
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- W2016454001 title "Determination ofKm andkcat for Signal Peptidase I Using a Full Length Secretory Precursor, pro-OmpA-nuclease A<//INF><//INF>" @default.
- W2016454001 doi "https://doi.org/10.1006/jmbi.1994.0025" @default.
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