Catalytic efficiency of signal peptidase I of Escherichia coli is comparable to that of members of the serine protease family

Dominic Suciu, Sukalyan Chatterjee, Masayori Inouye

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

Abstract

A method for estimating the activity of bacterial signal peptidase I (SPase I) was used to determine its activation energy (E(act)). Pro-OmpA-nuclease A, a hybrid secretory precursor, was purified to homogeneity under denaturing conditions and used as a substrate. This substrate was used to determine the activity of SPase I at different temperatures. The results show that the conformation of the mature domain of the substrate pro-OmpA-nuclease A has no discernible effect on the activity of SPase I. The activity data at a range of temperatures were then used to determine the activation energy using the Arrhenius equation. We have estimated E(act) to be 10.4 ± 0.6 kcal/mol. This work indicates that SPase I is as catalytically efficient as the His-Ser-Asp family of proteases.

Original languageEnglish (US)
Pages (from-to)1057-1060
Number of pages4
JournalProtein Engineering
Volume10
Issue number9
DOIs
StatePublished - 1997

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Keywords

  • Activation energy
  • Nuclease
  • Secretion
  • Signal peptide

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