猪胃蛋白酶以及与胃蛋白酶抑制剂复合的猪胃蛋白酶的¹H、¹³C和¹⁵N主链共振归属
¹H, ¹³C, and ¹⁵N backbone resonance assignments of the porcine pepsin and porcine pepsin complexed with pepstatin.
作者信息
Horimoto Yasumi, Wang Shenlin, Yada Rickey Y
机构信息
Department of Food Science, University of Guelph, Guelph, ON, N1G 2W1, Canada,
出版信息
Biomol NMR Assign. 2014 Apr;8(1):57-61. doi: 10.1007/s12104-012-9452-4. Epub 2012 Dec 21.
Pepsin is formed as the zymogen, pepsinogen, which includes an additional 44 residue prosegment (PS) on the N-terminus. Upon acidification (pH <3) the PS is removed, yielding active pepsin. The PS is critical to such processes as the initiation of correct folding and protein stability. In the present study, the NMR assignments of the 34.6 kDa native porcine pepsin and porcine pepsin complexed with pepstatin are reported in order to obtain structural information regarding PS-catalyzed protein folding. Such information would contribute to a better understanding of the nature of folding/unfolding energy barrier of pepsin and other aspartic proteases.
胃蛋白酶最初是以酶原胃蛋白酶原的形式形成的，胃蛋白酶原在N端包含一个额外的44个残基的前肽段（PS）。在酸化（pH <3）时，前肽段被去除，产生活性胃蛋白酶。前肽段对于正确折叠的起始和蛋白质稳定性等过程至关重要。在本研究中，报道了34.6 kDa天然猪胃蛋白酶以及与胃蛋白酶抑制剂复合的猪胃蛋白酶的核磁共振（NMR）归属，以便获得有关前肽段催化蛋白质折叠的结构信息。这些信息将有助于更好地理解胃蛋白酶和其他天冬氨酸蛋白酶折叠/去折叠能量屏障的本质。
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