TY - JOUR ID - 13370 TI - C-Terminal Propeptide of BKA has a Protease Sensitive Structure Without any Inhibitory Effect on BKA JO - Biomacromolecular Journal JA - BMMJ LA - en SN - 7280-2423 AU - Tavoli, Hesam AU - Salimi, Ali AU - Khajeh, Khosro AD - Department of Biochemistry, Faculty of Biological Science, Tarbiat Modares University, Tehran, Iran AD - Nanobiotechnology Research Center, Baqiyatallah University of Medical Science, Tehran, Iran Y1 - 2015 PY - 2015 VL - 1 IS - 1 SP - 140 EP - 147 KW - α-Amylase KW - Bacillus KW - C-Terminal propeptide KW - Foldase activity KW - Uncompetitive inhibitor DO - N2 - 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. UR - https://www.bmmj.org/article_13370.html L1 - https://www.bmmj.org/article_13370_5c453cbf3e6f02e1455c3129e893cf32.pdf ER -