HUMAN INSULIN-DEGRADING ENZYME SHARES STRUCTURAL AND FUNCTIONAL HOMOLOGIES WITH ESCHERICHIA-COLI PROTEASE-III
HUMAN INSULIN-DEGRADING ENZYME SHARES STRUCTURAL AND FUNCTIONAL HOMOLOGIES WITH ESCHERICHIA-COLI PROTEASE-III
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DOI：
10.1126/science.3059494
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发表时间：
1988-12-09
期刊：
影响因子：
56.9
通讯作者：
ROTH, RA
中科院分区：
文献类型：
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作者：
AFFHOLTER, JA;FRIED, VA;ROTH, RA
一种对胰岛素具有高亲和力的蛋白酶被认为在这种激素的细胞加工中起作用。编码这种酶的互补DNA（cDNA）已被分离和测序。推导的氨基酸序列的酶含有13个肽的序列来自分离的蛋白质。cDNA可以在体外转录产生合成RNA，在无细胞翻译中产生与天然蛋白酶共沉淀的蛋白质，并且可以与针对该酶的单克隆抗体免疫沉淀。这种蛋白酶的推导序列不包含任何已知蛋白酶类别（即金属、胱氨酸、天冬氨酸或丝氨酸）的共有序列，但它确实显示出与大肠杆菌蛋白酶（称为蛋白酶III）的同源性，该蛋白酶也切割胰岛素并存在于周质空间中。因此，这两种蛋白质可能是参与细胞间肽信号传导的蛋白酶家族的成员。
A proteinase with high affinity for insulin has been proposed to play a role in the cellular processing of this hormone. A complementary DNA (cDNA) coding for this enzyme has been isolated and sequenced. The deduced amino acid sequence of the enzyme contained the sequences of 13 peptides derived from the isolated protein. The cDNA could be transcribed in vitro to yield a synthetic RNA that in cell-free translations produced a protein that coelectrophoresed with the native proteinase and could be immunoprecipitated with monoclonal antibodies to this enzyme. The deduced sequence of this proteinase did not contain the consensus sequences for any of the known classes of proteinases (that is, metallo, cystcine, aspartic, or serine), but it did show homology to an Escherichia coli proteinase (called protease III), which also cleaves insulin and is present in the periplasmic space. Thus, these two proteins may be members of a family of proteases that are involved in intercellular peptide signaling.