Lee K L, Albee K L, Bernasconi R J, Edmunds T
Genzyme Corporation, 1 Mountain Road, Framingham, MA 01701-9322, USA.
Biochem J. 1997 Oct 1;327 ( Pt 1)(Pt 1):199-202. doi: 10.1042/bj3270199.
The amino acid sequences of ananain (EC3.4.22.31) and stem bromelain (3.4.22.32), two cysteine proteases from pineapple stem, are similar yet ananain and stem bromelain possess distinct specificities towards synthetic peptide substrates and different reactivities towards the cysteine protease inhibitors E-64 and chicken egg white cystatin. We present here the complete amino acid sequence of ananain and compare it with the reported sequences of pineapple stem bromelain, papain and chymopapain from papaya and actinidin from kiwifruit. Ananain is comprised of 216 residues with a theoretical mass of 23464 Da. This primary structure includes a sequence insert between residues 170 and 174 not present in stem bromelain or papain and a hydrophobic series of amino acids adjacent to His-157. It is possible that these sequence differences contribute to the different substrate and inhibitor specificities exhibited by ananain and stem bromelain.
菠萝蛋白酶(EC3.4.22.31)和茎菠萝蛋白酶(3.4.22.32)是来自菠萝茎的两种半胱氨酸蛋白酶,它们的氨基酸序列相似,但菠萝蛋白酶和茎菠萝蛋白酶对合成肽底物具有不同的特异性,并且对半胱氨酸蛋白酶抑制剂E - 64和鸡卵类粘蛋白具有不同的反应性。我们在此展示菠萝蛋白酶的完整氨基酸序列,并将其与已报道的菠萝茎菠萝蛋白酶、木瓜蛋白酶、番木瓜凝乳蛋白酶以及猕猴桃肌动蛋白的序列进行比较。菠萝蛋白酶由216个残基组成,理论质量为23464道尔顿。该一级结构包括茎菠萝蛋白酶或木瓜蛋白酶中不存在的170至174位残基之间的序列插入以及与His - 157相邻的一系列疏水氨基酸。这些序列差异可能导致菠萝蛋白酶和茎菠萝蛋白酶表现出不同的底物和抑制剂特异性。