glnD:Quickview: Difference between revisions
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!align=left {{table_heading_style}} | | !align=left {{table_heading_style}} |Standard Name | ||
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!align=left {{table_heading_style}} | | !align=left {{table_heading_style}} |Gene Synonym(s) | ||
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!align=left {{table_heading_style}} | | !align=left {{table_heading_style}} |Product Desc. | ||
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!align=left {{table_heading_style}} |Knock-Out Phenotype | !align=left {{table_heading_style}} |Knock-Out Phenotype | ||
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!align=left {{table_heading_style}} |Regulation/Expression | !align=left {{table_heading_style}} |Regulation/Expression | ||
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!align=left {{table_heading_style}} |Regulation/Activity | !align=left {{table_heading_style}} |Regulation/Activity | ||
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Revision as of 20:40, 4 March 2009
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| Quickview | Gene | Gene Product(s) | Expression | Evolution | On One Page |
| References | Suggestions |
See Help:Quickview for help with entering information in the Quickview table.
| Standard Name |
|---|
| Gene Synonym(s) |
| Product Desc. |
| Product Synonyms(s) |
| Knock-Out Phenotype |
| Regulation/Expression |
| Regulation/Activity |
| edit table |
See Help:Quickview for help with entering information in the Quickview table.
Notes
GlnD has both a uridylyltransferase and a uridylyl-removing activity. The only known substrates for GlnD are the two PII proteins GlnB and GlnK. In both cases GlnD covalently modifies residue Tyr51 in the T-loop of the substrate thereby controlling the ability of GlnB and GlnK to interact with their specific targets. The activity of GlnD is controlled by the intracellular glutamine availability. Glutamine inhibits the transferase action of GlnD and as a consequence GlnB and GlnK are deuridylylated in N-sufficient conditions. [Comment provided by EcoTeam member Mike Merrick, 11.16.06][1]
References