Difference between revisions of "Part:BBa K1498000"

Latest revision as of 18:33, 17 October 2014

kerUS keratinase from Brevibacillus brevis

BBa_K1498000 comprises of the (codon optimised for E. coli) coding region of kerUS keratinase from Brevibacillus brevis. kerUS harbours a signal peptide for extracellular secretion, which is cleaved following secretion -to yield an active keratinase (Jaouadi et al., 2013).

Keratins are a class of fibrous, insoluble and abundant structural proteins which are found in structures such as hair, feathers, nails, hooves and wool. these proteins are highly stable, showing resistance to many proteolytic enzymes.

Keratinases are a group of proteases that can degrade keratin substrates.

BBa_K1498000 is a 383aa, 39.4 kDa protein. There is a predicted a signal peptide of 29 aa, which directs the protein for secretion. Secretion was shown to be effective in E. coli in addition to the endogenous organism. This along with other residues from a pro-sequence consisting of 79 aa which are cleaved by autoproteolytic processing in the periplasm. The active mature keratinase consists of 275 aa, with a molecular weight of 29 kDa.

References.

Jaouadi, N. Z., Rekik, H., Badis, A., Trabelsi, S., Belhoul, M., Yahiaoui, A. B., … Jaouadi, B. (2013). Biochemical and molecular characterization of a serine keratinase from Brevibacillus brevis US575 with promising keratin-biodegradation and hide-dehairing activities. PloS one, 8(10), e76722.

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
INCOMPATIBLE WITH RFC[25]
Illegal AgeI site found at 866
1000
COMPATIBLE WITH RFC[1000]

@@ Line 2: / Line 2: @@
 <partinfo>BBa_K1498000 short</partinfo>
-BBa_K1498000 comprises of the (codon optimised for ''E. coli'') coding region of kerUS keratinase from ''Brevibacillus brevis''. kerUS harbours a signal peptide for extracellular secretion, which is cleaved following secretion -to yield an active keratinase.
+BBa_K1498000 comprises of the (codon optimised for ''E. coli'') coding region of kerUS keratinase from ''Brevibacillus brevis''. kerUS harbours a signal peptide for extracellular secretion, which is cleaved following secretion -to yield an active keratinase (Jaouadi et al., 2013).
 Keratins are a class of fibrous, insoluble and abundant structural proteins which are found in structures such as hair, feathers, nails, hooves and wool. these proteins are highly stable, showing resistance to many proteolytic enzymes.
@@ Line 9: / Line 9: @@
 BBa_K1498000 is a 383aa, 39.4 kDa protein. There is a predicted a signal peptide of 29 aa, which directs the protein for secretion. Secretion was shown to be effective in ''E. coli'' in addition to the endogenous organism. This along with other residues from a pro-sequence consisting of 79 aa which are cleaved by autoproteolytic processing in the periplasm. The active mature keratinase consists of 275 aa, with a molecular weight of 29 kDa.
+'''References.'''
+Jaouadi, N. Z., Rekik, H., Badis, A., Trabelsi, S., Belhoul, M., Yahiaoui, A. B., … Jaouadi, B. (2013). Biochemical and molecular characterization of a serine keratinase from Brevibacillus brevis US575 with promising keratin-biodegradation and hide-dehairing activities. PloS one, 8(10), e76722.