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Structure–function relationships of UMP kinases from pyrH mutants of Gram-negative bacteria
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| Zeitschriftentitel: | Microbiology |
|---|---|
| Personen und Körperschaften: | , , , , , |
| In: | Microbiology, 150, 2004, 7, S. 2153-2159 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Microbiology Society
|
| Schlagwörter: |
| author_facet |
Sakamoto, Hiroshi Landais, Stéphanie Evrin, Cécile Laurent-Winter, Christine Bârzu, Octavian Kelln, Rod A. Sakamoto, Hiroshi Landais, Stéphanie Evrin, Cécile Laurent-Winter, Christine Bârzu, Octavian Kelln, Rod A. |
|---|---|
| author |
Sakamoto, Hiroshi Landais, Stéphanie Evrin, Cécile Laurent-Winter, Christine Bârzu, Octavian Kelln, Rod A. |
| spellingShingle |
Sakamoto, Hiroshi Landais, Stéphanie Evrin, Cécile Laurent-Winter, Christine Bârzu, Octavian Kelln, Rod A. Microbiology Structure–function relationships of UMP kinases from pyrH mutants of Gram-negative bacteria Microbiology |
| author_sort |
sakamoto, hiroshi |
| spelling |
Sakamoto, Hiroshi Landais, Stéphanie Evrin, Cécile Laurent-Winter, Christine Bârzu, Octavian Kelln, Rod A. 1350-0872 1465-2080 Microbiology Society Microbiology http://dx.doi.org/10.1099/mic.0.26996-0 <jats:p>Bacterial uridine monophosphate (UMP) kinases are essential enzymes encoded by<jats:italic>pyrH</jats:italic>genes, and conditional-lethal or other<jats:italic>pyrH</jats:italic>mutants were analysed with respect to structure–function relationships. A set of thermosensitive<jats:italic>pyrH</jats:italic>mutants from<jats:italic>Escherichia coli</jats:italic>was generated and studied, along with already described<jats:italic>pyrH</jats:italic>mutants from<jats:italic>Salmonella enterica</jats:italic>serovar Typhimurium. It is shown that Arg-11 and Gly-232 are key residues for thermodynamic stability of the enzyme, and that Asp-201 is important for both catalysis and allosteric regulation. A comparison of the amino acid sequence of UMP kinases from several prokaryotes showed that these were conserved residues. Discussion on the enzyme activity level in relation to bacterial viability is also presented.</jats:p> Structure–function relationships of UMP kinases from pyrH mutants of Gram-negative bacteria Microbiology |
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10.1099/mic.0.26996-0 |
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Microbiology Society, 2004 |
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Microbiology Society, 2004 |
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Microbiology Society |
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Microbiology |
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| title |
Structure–function relationships of UMP kinases from pyrH mutants of Gram-negative bacteria |
| title_unstemmed |
Structure–function relationships of UMP kinases from pyrH mutants of Gram-negative bacteria |
| title_full |
Structure–function relationships of UMP kinases from pyrH mutants of Gram-negative bacteria |
| title_fullStr |
Structure–function relationships of UMP kinases from pyrH mutants of Gram-negative bacteria |
| title_full_unstemmed |
Structure–function relationships of UMP kinases from pyrH mutants of Gram-negative bacteria |
| title_short |
Structure–function relationships of UMP kinases from pyrH mutants of Gram-negative bacteria |
| title_sort |
structure–function relationships of ump kinases from pyrh mutants of gram-negative bacteria |
| topic |
Microbiology |
| url |
http://dx.doi.org/10.1099/mic.0.26996-0 |
| publishDate |
2004 |
| physical |
2153-2159 |
| description |
<jats:p>Bacterial uridine monophosphate (UMP) kinases are essential enzymes encoded by<jats:italic>pyrH</jats:italic>genes, and conditional-lethal or other<jats:italic>pyrH</jats:italic>mutants were analysed with respect to structure–function relationships. A set of thermosensitive<jats:italic>pyrH</jats:italic>mutants from<jats:italic>Escherichia coli</jats:italic>was generated and studied, along with already described<jats:italic>pyrH</jats:italic>mutants from<jats:italic>Salmonella enterica</jats:italic>serovar Typhimurium. It is shown that Arg-11 and Gly-232 are key residues for thermodynamic stability of the enzyme, and that Asp-201 is important for both catalysis and allosteric regulation. A comparison of the amino acid sequence of UMP kinases from several prokaryotes showed that these were conserved residues. Discussion on the enzyme activity level in relation to bacterial viability is also presented.</jats:p> |
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| author | Sakamoto, Hiroshi, Landais, Stéphanie, Evrin, Cécile, Laurent-Winter, Christine, Bârzu, Octavian, Kelln, Rod A. |
| author_facet | Sakamoto, Hiroshi, Landais, Stéphanie, Evrin, Cécile, Laurent-Winter, Christine, Bârzu, Octavian, Kelln, Rod A., Sakamoto, Hiroshi, Landais, Stéphanie, Evrin, Cécile, Laurent-Winter, Christine, Bârzu, Octavian, Kelln, Rod A. |
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| description | <jats:p>Bacterial uridine monophosphate (UMP) kinases are essential enzymes encoded by<jats:italic>pyrH</jats:italic>genes, and conditional-lethal or other<jats:italic>pyrH</jats:italic>mutants were analysed with respect to structure–function relationships. A set of thermosensitive<jats:italic>pyrH</jats:italic>mutants from<jats:italic>Escherichia coli</jats:italic>was generated and studied, along with already described<jats:italic>pyrH</jats:italic>mutants from<jats:italic>Salmonella enterica</jats:italic>serovar Typhimurium. It is shown that Arg-11 and Gly-232 are key residues for thermodynamic stability of the enzyme, and that Asp-201 is important for both catalysis and allosteric regulation. A comparison of the amino acid sequence of UMP kinases from several prokaryotes showed that these were conserved residues. Discussion on the enzyme activity level in relation to bacterial viability is also presented.</jats:p> |
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| spelling | Sakamoto, Hiroshi Landais, Stéphanie Evrin, Cécile Laurent-Winter, Christine Bârzu, Octavian Kelln, Rod A. 1350-0872 1465-2080 Microbiology Society Microbiology http://dx.doi.org/10.1099/mic.0.26996-0 <jats:p>Bacterial uridine monophosphate (UMP) kinases are essential enzymes encoded by<jats:italic>pyrH</jats:italic>genes, and conditional-lethal or other<jats:italic>pyrH</jats:italic>mutants were analysed with respect to structure–function relationships. A set of thermosensitive<jats:italic>pyrH</jats:italic>mutants from<jats:italic>Escherichia coli</jats:italic>was generated and studied, along with already described<jats:italic>pyrH</jats:italic>mutants from<jats:italic>Salmonella enterica</jats:italic>serovar Typhimurium. It is shown that Arg-11 and Gly-232 are key residues for thermodynamic stability of the enzyme, and that Asp-201 is important for both catalysis and allosteric regulation. A comparison of the amino acid sequence of UMP kinases from several prokaryotes showed that these were conserved residues. Discussion on the enzyme activity level in relation to bacterial viability is also presented.</jats:p> Structure–function relationships of UMP kinases from pyrH mutants of Gram-negative bacteria Microbiology |
| spellingShingle | Sakamoto, Hiroshi, Landais, Stéphanie, Evrin, Cécile, Laurent-Winter, Christine, Bârzu, Octavian, Kelln, Rod A., Microbiology, Structure–function relationships of UMP kinases from pyrH mutants of Gram-negative bacteria, Microbiology |
| title | Structure–function relationships of UMP kinases from pyrH mutants of Gram-negative bacteria |
| title_full | Structure–function relationships of UMP kinases from pyrH mutants of Gram-negative bacteria |
| title_fullStr | Structure–function relationships of UMP kinases from pyrH mutants of Gram-negative bacteria |
| title_full_unstemmed | Structure–function relationships of UMP kinases from pyrH mutants of Gram-negative bacteria |
| title_short | Structure–function relationships of UMP kinases from pyrH mutants of Gram-negative bacteria |
| title_sort | structure–function relationships of ump kinases from pyrh mutants of gram-negative bacteria |
| title_unstemmed | Structure–function relationships of UMP kinases from pyrH mutants of Gram-negative bacteria |
| topic | Microbiology |
| url | http://dx.doi.org/10.1099/mic.0.26996-0 |