EVOLUTION IN THE STRUCTURE AND FUNCTION OF ASPARTIC PROTEASES
EVOLUTION IN THE STRUCTURE AND FUNCTION OF ASPARTIC PROTEASES
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DOI：
10.1002/jcb.240330106
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发表时间：
1987-01-01
影响因子：
4
通讯作者：
WONG, RNS
中科院分区：
文献类型：
--
作者：
TANG, J;WONG, RNS
天冬氨酸蛋白酶(EC3.4.23)是胃酶家族的一组蛋白水解酶，它们共享相同的催化装置，通常在酸性溶液中发挥作用。这一方面将天冬氨酸蛋白酶的功能限制在不同生物体中的某些特定位置；因此，天冬氨酸蛋白酶的出现没有丝氨酸蛋白酶等其他类型的酶那么丰富。天冬氨酸蛋白水解酶最著名的来源是胃(对于胃酶，胃蛋白酶。和凝乳酶)。溶酶体(用于组织蛋白酶D和E)、肾脏(用于肾素)、酵母颗粒和真菌(用于分泌的蛋白酶，如根胃酶、青霉蛋白酶和内皮肽酶)。这些天冬氨酸蛋白酶的结构和功能关系已被广泛研究，并已成为几篇综述或专著的主题(唐：酸性蛋白酶，结构，功能和生物学。纽约：全会出版社，1977；唐：《摩尔细胞生物化学》26：93-109,1979；Kostka：天冬氨酸蛋白酶及其抑制剂。柏林：沃尔特·德·格鲁伊特，1985)。所有哺乳动物的天冬氨酸蛋白酶都是以酶原的形式合成的，然后被激活为活性的蛋白酶。虽然还没有发现真菌天冬氨酸蛋白酶的酶原，但根霉胃蛋白酶的cdna结构表明存在一种“前”酶(Wong等人：FED Proc 44：2725,1985)。可能还合成了其他真菌天冬氨酸蛋白酶作为发酵原。
Aspartic proteases (EC3. 4.23) are a group of proteolytic enzymes of the pepsin family that share the same catalytic apparatus and usually function in acid solutions. This latter aspect limits the function of aspartic proteases to some specific locations in different organisms; thus the occurrence of aspartic proteases is less abundant than other groups of proteases, such as serine proteases. The best known sources of aspartic proteases are stomach (for pepsin, gastricsin. and chymosin). lysosomes (for cathepsins D and E), kidney (for renin), yeast granules, and fungi (for secreted proteases such as rhizopuspepsin, penicillopepsin, and endothiapepsin). These aspartic proteases have been extensively studied for their structure and function relationships and have been the topics of several reviews or monographs (Tang: Acid Proteases, Structure, Function and Biology. New York: Plenum Press, 1977; Tang: J Mol Cell Biochem 26: 93–109, 1979; Kostka: Aspartic Proteinases and Their Inhibitors. Berlin: Walter de Gruyter, 1985). All mammalian aspartic proteases are synthesized as zymogens and are subsequently activated to active proteases. Although a zymogen for a fungal aspartic protease has not been found, the cDNA structure of rhizopuspepsin suggests the presence of a “pro” enzyme (Wong et al: Fed Proc 44: 2725, 1985). It is probable that other fungal aspartic proteases are also synthesized as zymogens.