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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
1998-4-14
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0269-2139
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
10
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1057-60
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9464569-Bacterial Outer Membrane Proteins,
pubmed-meshheading:9464569-Bacterial Proteins,
pubmed-meshheading:9464569-Binding Sites,
pubmed-meshheading:9464569-Catalysis,
pubmed-meshheading:9464569-Escherichia coli,
pubmed-meshheading:9464569-Kinetics,
pubmed-meshheading:9464569-Membrane Proteins,
pubmed-meshheading:9464569-Micrococcal Nuclease,
pubmed-meshheading:9464569-Protein Conformation,
pubmed-meshheading:9464569-Protein Precursors,
pubmed-meshheading:9464569-Protein Sorting Signals,
pubmed-meshheading:9464569-Serine Endopeptidases,
pubmed-meshheading:9464569-Structure-Activity Relationship,
pubmed-meshheading:9464569-Temperature
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pubmed:year |
1997
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pubmed:articleTitle |
Catalytic efficiency of signal peptidase I of Escherichia coli is comparable to that of members of the serine protease family.
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pubmed:affiliation |
Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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