Difference between revisions of "Part:BBa K523001"
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===Usage and Biology=== | ===Usage and Biology=== | ||
| − | While an amylase ought to be capable of degrading starch, the product protein is believed to be periplasmic and thus ought to only degrade starch if it leaks from the periplasm in significant quantities. Its natural function in ''E. coli'' presumably involves degrading shorter glucose chains. | + | While an amylase ought to be capable of degrading starch, the product protein is believed to be periplasmic and thus ought to only degrade starch if it leaks from the periplasm in significant quantities. Its natural function in ''E. coli'' presumably involves degrading shorter glucose chains: [http://dx.doi.org/10.1128/JB.00767-08 Lengsfeld ''et al'' (2008)] state that "MalS produces preferentially maltohexaose from longer maltodextrins in the periplasm". |
The SignalP program predicts that a 17 amino acid localisation signal (at the N terminal) is cleaved off before the protein reaches its mature form. | The SignalP program predicts that a 17 amino acid localisation signal (at the N terminal) is cleaved off before the protein reaches its mature form. | ||
<font color="red">Edinburgh 2011 carried out some experiments on this part under the control of the lac promoter - see details at part <partinfo>BBa_K523006</partinfo>.</font> | <font color="red">Edinburgh 2011 carried out some experiments on this part under the control of the lac promoter - see details at part <partinfo>BBa_K523006</partinfo>.</font> | ||
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<span class='h3bb'>'''Sequence and Features'''</span> | <span class='h3bb'>'''Sequence and Features'''</span> | ||
Revision as of 19:23, 18 September 2011
RBS + malS (E. coli periplasmic α-amylase)
This is the E. coli amylase gene malS. The part contains the native Ribosome Binding Site.
The part was made using the strategy outlined in BBa_K523000, and therefore contains 4 extra bases at the 5' end which generate a BglII restriction site.
Usage and Biology
While an amylase ought to be capable of degrading starch, the product protein is believed to be periplasmic and thus ought to only degrade starch if it leaks from the periplasm in significant quantities. Its natural function in E. coli presumably involves degrading shorter glucose chains: [http://dx.doi.org/10.1128/JB.00767-08 Lengsfeld et al (2008)] state that "MalS produces preferentially maltohexaose from longer maltodextrins in the periplasm".
The SignalP program predicts that a 17 amino acid localisation signal (at the N terminal) is cleaved off before the protein reaches its mature form.
Edinburgh 2011 carried out some experiments on this part under the control of the lac promoter - see details at part BBa_K523006.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 1233
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 369
Illegal AgeI site found at 1534 - 1000COMPATIBLE WITH RFC[1000]