Difference between revisions of "Part:BBa K2973000"

Revision as of 13:09, 19 October 2019

T7-RBS-β-Lactamase-No Signal peptide

This composite part consists of T7 Promoter(BBa_J64997) and T7 Terminator(BBa_K731721), Ribosomal Binding Site(BBa_B0034), CDS of β-lactamase without the signal peptide. β-lactamase (EC 3.5.2.6) is a small monomeric enzyme(29kDa) that is produced by bacteria and gives them resistance to antibiotics with β-lactam ring because of its ability to hydrolyze the amide bond in the β-lactam ring. This ability can be exploited in order to use β-lactamase as a protein reporter by providing the enzyme with its chromogenic substrate Nitrocefin. Nitrocefin is a chromogenic cephalosporin first reported in 1972 as a novel and straightforward substrate used to detect bacteria resistant to β-lactam antibiotics. Normally, a nitrocefin solution has a yellow color, but after its hydrolysis by β-lactamase, the color of the solution turns red, allowing that way the detection of the enzyme.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
INCOMPATIBLE WITH RFC[12]
Illegal NheI site found at 851
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

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 <partinfo>BBa_K2973000 short</partinfo>
-This composite part consists of T7 Promoter(BBa_J64997) and T7 Terminator(BBa_K731721), Ribosomal Binding Site(BBa_B0034), CDS of B-lactamase without the signal peptide. Beta lactamase (EC 3.5.2.6) is a small monomeric enzyme(29kDa) that is produced by bacteria and gives them resistance to antibiotics with &#946;-lactam ring because of its ability to hydrolyze the amid bond in the &#946;-lactam ring. This ability can be exploited in order to use b-lactamase as a protein reporter by providing the enzyme with its chromogenic substrate Nitrocefin. Nitrocefin is a chromogenic cephalosporin first reported in 1972 as a novel and straightforward substrate used to detect bacteria resistant to &#946;-lactam antibiotics. Normally, a nitrocefin solution has yellow color, but after its hydrolysis by b-lactamase , the color of the solution turns red, allowing that way the detection of the enzyme.
+This composite part consists of T7 Promoter(BBa_J64997) and T7 Terminator(BBa_K731721), Ribosomal Binding Site(BBa_B0034), CDS of β-lactamase without the signal peptide. β-lactamase (EC 3.5.2.6) is a small monomeric enzyme(29kDa) that is produced by bacteria and gives them resistance to antibiotics with &#946;-lactam ring because of its ability to hydrolyze the amide bond in the &#946;-lactam ring. This ability can be exploited in order to use β-lactamase as a protein reporter by providing the enzyme with its chromogenic substrate Nitrocefin. Nitrocefin is a chromogenic cephalosporin first reported in 1972 as a novel and straightforward substrate used to detect bacteria resistant to &#946;-lactam antibiotics. Normally, a nitrocefin solution has a yellow color, but after its hydrolysis by β-lactamase, the color of the solution turns red, allowing that way the detection of the enzyme.
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