malT:Quickview: Difference between revisions
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Activated by maltotriose and ATP to form active oligomers. Signal transduction ATPases with numerous domains (STAND) protein. ATP hydrolysis is not required for transcription activation (Richet, 1989), but is required to recycle back to the inactive form, which has ADP, not ATP bound (Marquenet, 2007). MalY (Clausen, 2000; Schreiber, 2000), MalK (Reyes, 1988; Panagiotidis, 1998; Bohm, 2002) and Aes (Joly, 2002) negatively regulate MalT activity by binding and blocking maltotriose activation. MalT is required for phage lambda sensitivity.<ref name='LIB:EcoGene'/> | |||
Revision as of 00:08, 3 March 2009
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| Quickview | Gene | Gene Product(s) | Expression | Evolution | On One Page |
| References | Suggestions |
| Gene Name | |
|---|---|
| Product(s) |
MalT product, MalT product[1][2]: B3418 product, MalA product |
| Description | |
| Knock-Out Phenotype | |
| Regulation/Expression | |
| Regulation/Activity |
|
| edit table |
See Help:Quickview for help with entering information in the Quickview table.
Notes
Activated by maltotriose and ATP to form active oligomers. Signal transduction ATPases with numerous domains (STAND) protein. ATP hydrolysis is not required for transcription activation (Richet, 1989), but is required to recycle back to the inactive form, which has ADP, not ATP bound (Marquenet, 2007). MalY (Clausen, 2000; Schreiber, 2000), MalK (Reyes, 1988; Panagiotidis, 1998; Bohm, 2002) and Aes (Joly, 2002) negatively regulate MalT activity by binding and blocking maltotriose activation. MalT is required for phage lambda sensitivity.[4]
References
- ↑ 1.0 1.1 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
- ↑ 2.0 2.1 2.2 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.