c-terminal propeptide of bka has a protease sensitive structure without any inhibitory effect on bka

نویسندگان

hesam tavoli

ali salimi

khosro khajeh

چکیده

in our previous study, we compared the two α-amylase enzymes from bacillus sp.kr8104, bka∆(n44) and bka∆(n44c193) which is the secreted form of it. the results indicated that the presence of 193 amino acids propeptide in the c-terminal of bka∆(n44) changed its enzymatic parameters like an uncompetitive inhibitor in comparison to bka∆(n44c193). in the present study, we cloned the dna sequence of bka∆(n44) which codes the 193 amino acids propeptide in its c-terminal and the effect of this fragment as an inhibitor on bka∆(n44c193) was investigated. we also studied the possible foldase activity of the propeptide in bka∆(n44c193). protease sensitivity of c-terminal 193 amino acid propeptide, bka∆(n44) and bka∆(n44c193) was compared in order to explain why  bka∆(n44c193) is the only secreted form of α-amylase in the culture medium of bacillus sp.kr8104. circular dichroism indicated that the secondary structure of the c-terminal is mostly beta sheeted. at the end we proposed a possible regulatory role for the c-terminal propeptide of bka.

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C-Terminal Propeptide of BKA has a Protease Sensitive Structure Without any Inhibitory Effect on BKA

In our previous study, we compared the two α-amylase enzymes from Bacillus sp.KR8104, BKA∆(N44) and BKA∆(N44C193) which is the secreted form of it. The results indicated that the presence of 193 amino acids propeptide in the C-terminal of BKA∆(N44) changed its enzymatic parameters like an uncompetitive inhibitor in comparison to BKA∆(N44C193). In the present study, we cloned the DNA sequence of...

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عنوان ژورنال:
biomacromolecular journal

ناشر: iran society of biophysical chemistry (isobc)

ISSN

دوره 1

شماره 1 2015

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