NDLI: Mutation of conserved residues in Escherichia coli thioredoxin: effects on stability and function.

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Mutation of conserved residues in Escherichia coli thioredoxin: effects on stability and function.

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Mutation of conserved residues in Escherichia coli thioredoxin: effects on stability and function.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Gleason, F. K.
Description	Author Affiliation: Gleason FK ( Department of Plant Biology, University of Minnesota, St. Paul 55108.)
Abstract	Mutations were made in three highly conserved residues in Escherichia coli thioredoxin. An internal charged residue, Asp-26, was changed to an alanine. The mutant protein was more stable than the wild type. It can function as a substrate for thioredoxin reductase with a 10-fold increase in the Km over the wild type. Although the redox potential was not substantially changed from that of the wild type, thioredoxin D26A was a poor reducing agent for ribonucleotide reductase. Asp-26 apparently serves to maintain an optimal charge distribution in the active site region for interaction with other proteins. Mutation of a surface Pro-34 in the active site disulfide ring to a serine had little effect on protein stability. A slight decrease in the redox potential (9 mV) made thioredoxin P34S a better reducing agent for ribonucleotide reductase. In contrast, mutation of the internal cis Pro-76 to an alanine destabilized the protein. The data indicate a change had also occurred in the charge distribution in the active site region. Thioredoxin P76A had a higher redox potential than the wild type protein and was not an effective reducing agent for ribonucleotide reductase. It was concluded that this residue is essential for maintaining the conformation of the active site and the redox potential of thioredoxin.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	5
Volume Number	1
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1992-05-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Escherichia Coli Enzymology Thioredoxins Genetics Metabolism Amino Acid Sequence Conserved Sequence Enzyme Stability Fluorescence Hydrogen-ion Concentration Models, Molecular Molecular Sequence Data Mutagenesis, Site-directed Oxidation-reduction Protein Denaturation Ribonucleoside Diphosphate Reductase Comparative Study Research Support, U.s. Gov't, Non-p.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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