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

doi:https://doi.org/10.1093/protein/10.9.1057

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

Rutgers, The State University

Research output: Contribution to journal › Article › peer-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 language	English (US)
Pages (from-to)	1057-1060
Number of pages	4
Journal	Protein Engineering
Volume	10
Issue number	9
DOIs	https://doi.org/10.1093/protein/10.9.1057
State	Published - 1997

ASJC Scopus subject areas

Biochemistry
Molecular Biology

Keywords

Activation energy
Nuclease
Secretion
Signal peptide

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https://doi.org/10.1093/protein/10.9.1057

Cite this

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

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.",

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TY - JOUR

T1 - Catalytic efficiency of signal peptidase I of Escherichia coli is comparable to that of members of the serine protease family

AU - Suciu, Dominic

AU - Chatterjee, Sukalyan

AU - Inouye, Masayori

PY - 1997

Y1 - 1997

N2 - 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.

AB - 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.

KW - Activation energy

KW - Nuclease

KW - Secretion

KW - Signal peptide

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DO - https://doi.org/10.1093/protein/10.9.1057

M3 - Article

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VL - 10

SP - 1057

EP - 1060

JO - Protein Engineering

JF - Protein Engineering

SN - 0269-2139

IS - 9

ER -

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

Abstract

ASJC Scopus subject areas

Keywords

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