Difference between revisions of "Part:BBa K1189008"
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| − | Beta-lactamase (BLA) is an enzyme frequently present in plasmids for selection. Beta-lactamase is a 29-kDa monomeric enzyme. Its enzymatic activity provides resistance to beta-lactam antibiotics such as cephamysin, carbapenems and penicillium through hydrolysis of the β-lactam ring, a structure shared by these antibiotics (Qureshi, 2007). Kinetically, beta-lactamase is simple and shows high catalytic efficiency. Also, no orthologs of BLA are known to be encoded by eukaryotic cells and no toxicity was identified making this protein very useful in studies involved eukaryotes (Qureshi, 2007). BLA has also been used to track pathogens in infected murine models (Kong et. al, 2010). However, in addition to its application in eukaryotic cells, beta-lactamase efficiently cleaves a wide variety of substrates but its versatility goes beyond that; BLA preserves its activity even when fused to heterologous protein (Moore et. al, 1997). This feature, in particular, makes beta-lactamase a potential tool for assemble of synthetic constructs. | + | Beta-lactamase (BLA) is an enzyme frequently present in plasmids for selection. Beta-lactamase is a 29-kDa monomeric enzyme. Its enzymatic activity provides resistance to beta-lactam antibiotics such as cephamysin, carbapenems and penicillium through hydrolysis of the β-lactam ring, a structure shared by these antibiotics (Qureshi, 2007). Kinetically, beta-lactamase is simple and shows high catalytic efficiency. Also, no orthologs of BLA are known to be encoded by eukaryotic cells and no toxicity was identified making this protein very useful in studies involved eukaryotes (Qureshi, 2007). BLA has also been used to track pathogens in infected murine models (Kong et. al, 2010). However, in addition to its application in eukaryotic cells, beta-lactamase efficiently cleaves a wide variety of substrates but its versatility goes beyond that; BLA preserves its activity even when fused to heterologous protein (Moore et. al, 1997). This feature, in particular, makes beta-lactamase a potential tool for assemble of synthetic constructs. This is submitted in the Freiburg fusion backbone for easy fusion construction. Additionally, the BsaI cut site in the gene has been mutagenized. |
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Revision as of 04:49, 28 September 2013
Beta-Lactamase
Beta-lactamase (BLA) is an enzyme frequently present in plasmids for selection. Beta-lactamase is a 29-kDa monomeric enzyme. Its enzymatic activity provides resistance to beta-lactam antibiotics such as cephamysin, carbapenems and penicillium through hydrolysis of the β-lactam ring, a structure shared by these antibiotics (Qureshi, 2007). Kinetically, beta-lactamase is simple and shows high catalytic efficiency. Also, no orthologs of BLA are known to be encoded by eukaryotic cells and no toxicity was identified making this protein very useful in studies involved eukaryotes (Qureshi, 2007). BLA has also been used to track pathogens in infected murine models (Kong et. al, 2010). However, in addition to its application in eukaryotic cells, beta-lactamase efficiently cleaves a wide variety of substrates but its versatility goes beyond that; BLA preserves its activity even when fused to heterologous protein (Moore et. al, 1997). This feature, in particular, makes beta-lactamase a potential tool for assemble of synthetic constructs. This is submitted in the Freiburg fusion backbone for easy fusion construction. Additionally, the BsaI cut site in the gene has been mutagenized.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]