Difference between revisions of "Part:BBa K3182004"

Revision as of 15:43, 14 September 2019

CHAP(K)

Staphylococcus phage endolysin, designed to target Staphylococcus aureus. This part was designed to be assembled with BBa_K3182010.

The LysK is an endolysin targeting gram positive bacteria. It has two catalytical domains known as CHAP (cysteine-and histidine depentent amidohydrolase/peptidase) and a central amidase-2 domain together with a cell binding domain. The CHAP domain which is the truncated part expressed in this year’s LiU iGEM (more specifically CHAP C1-C162) team still has lytic activity against staphylococcus. The C1 to C162 amino acids are required for full endopeptidase activity.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

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 Staphylococcus phage endolysin, designed to target Staphylococcus aureus. This part was designed to be assembled with BBa_K3182010.
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-Bacteriophage endolysins digest the peptidoglycan wall of bacteria. The LysK is an endolysin targeting gram + bacteria. It has two catalytical domains known as CHAP (cysteine-and histidine depentent amidohydrolase/peptidase) and a central amidase-2 domain together with a cell binding domain. The CHAP domain which is the truncated part expressed in this year’s LiU iGEM (more specifically CHAP C1-C162) team still has lytic activity against staphylococcus. The C1 to C162 amino acids are required for full endopeptidase activity.
+The LysK is an endolysin targeting gram positive bacteria. It has two catalytical domains known as CHAP (cysteine-and histidine depentent amidohydrolase/peptidase) and a central amidase-2 domain together with a cell binding domain. The CHAP domain which is the truncated part expressed in this year’s LiU iGEM (more specifically CHAP C1-C162) team still has lytic activity against staphylococcus. The C1 to C162 amino acids are required for full endopeptidase activity.