Difference between revisions of "Part:BBa K3187020"

Revision as of 12:50, 24 September 2019

Tobacco Vein Mottling Virus Protease Cleavage Site

The Sortase A7M is a mutated form of the enzyme Sortase from Staphylococcus aureus. Sortase is an enzyme that catalyzes the formation of a peptide bond between a protein containing a C-terminal LPETG amino acid sequence and a protein containing an N-terminal polyG sequence (two or more glycines on the N- terminus). Peptide bond formation is between the threonine (T) of the LPETG and the N- terminal glycine. Due to the mutations it is calcium-independent which is why it can be used in vivo without disturbing the calcium concentrations in cells. It has a molecular weight of 17,85 kDa.

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]

Revision as of 12:19, 24 September 2019 (view source) Registry (Talk \| contribs)		Revision as of 12:50, 24 September 2019 (view source) PeterGockel (Talk \| contribs) Newer edit →
Line 4:		Line 4:

	The Sortase A7M is a mutated form of the enzyme Sortase from Staphylococcus aureus. Sortase is an enzyme that catalyzes the formation of a peptide bond between a protein containing a C-terminal LPETG amino acid sequence and a protein containing an N-terminal polyG sequence (two or more glycines on the N- terminus). Peptide bond formation is between the threonine (T) of the LPETG and the N- terminal glycine. Due to the mutations it is calcium-independent which is why it can be used in vivo without disturbing the calcium concentrations in cells. It has a molecular weight of 17,85 kDa.		The Sortase A7M is a mutated form of the enzyme Sortase from Staphylococcus aureus. Sortase is an enzyme that catalyzes the formation of a peptide bond between a protein containing a C-terminal LPETG amino acid sequence and a protein containing an N-terminal polyG sequence (two or more glycines on the N- terminus). Peptide bond formation is between the threonine (T) of the LPETG and the N- terminal glycine. Due to the mutations it is calcium-independent which is why it can be used in vivo without disturbing the calcium concentrations in cells. It has a molecular weight of 17,85 kDa.
		+