Klimova O A, Borukhov S I, Solovyeva N I, Balaevskaya T O
Institute of Molecular Genetics, USSR Academy of Science, Moscow.
Biochem Biophys Res Commun. 1990 Feb 14;166(3):1411-20. doi: 10.1016/0006-291x(90)91024-m.
A mixture of collagenolytic proteases has been isolated from the Kamchatka crab hepatopancreas. The four individual enzymes were further separated with FPLC and partially characterized. Crab collagenolytic proteases possess a high activity against different types of collagen, especially against calf skin collagen Type III and bovine lens capsule collagen Type IV, which is resistant to the microbial Clostridium sp. collagenases. In contrast with microbial collagenases the crab enzymes are good general proteases, able to cleave standard synthetic and protein substrates and possess a chymotrypsin-, trypsin- and elastase-like specificity. N-Terminal sequence analysis revealed that crab collagenolytic proteases had evolved from a trypsin-like ancestor. Crab proteases, structurally belonging to the trypsin-like enzymes, nevertheless, possess the unique ability, among this class of enzymes, to cleave the native insoluble collagen. It seems that crab collagenolytic proteases and true metalloenzyme vertebrate and microbial collagenases have certain common structural features particularly in the regions of their substrate binding site.
已从堪察加蟹的肝胰腺中分离出一种胶原分解蛋白酶混合物。这四种单独的酶通过快速蛋白质液相色谱法（FPLC）进一步分离并进行了部分特性鉴定。蟹胶原分解蛋白酶对不同类型的胶原具有高活性，尤其是对III型小牛皮胶原和IV型牛晶状体囊胶原，后者对微生物梭菌属胶原酶具有抗性。与微生物胶原酶不同，蟹酶是良好的通用蛋白酶，能够切割标准合成底物和蛋白质底物，并具有类似胰凝乳蛋白酶、胰蛋白酶和弹性蛋白酶的特异性。N端序列分析表明，蟹胶原分解蛋白酶是从类似胰蛋白酶的祖先进化而来的。蟹蛋白酶在结构上属于类似胰蛋白酶的酶，但在这类酶中具有独特的能力，即能够切割天然不溶性胶原。蟹胶原分解蛋白酶与真正的金属酶脊椎动物和微生物胶原酶似乎具有某些共同的结构特征，特别是在它们的底物结合位点区域。
