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[烟曲霉碱性磷酸酶1蛋白酶的分离鉴定及其多头绒泡菌蛋白抑制剂]

[Isolation and characterization of the ALP1 protease from Aspergillus fumigatus and its protein inhibitor from Physarium polycephalum].

作者信息

Davies D A, Kalinina N A, Samokhvalova L V, Malakhova G V, Scott G, Volynskaia A M, Nesmeianov V A

出版信息

Bioorg Khim. 2005 May-Jun;31(3):259-68. doi: 10.1007/s11171-005-0032-6.

DOI:10.1007/s11171-005-0032-6
PMID:16004384
Abstract

It is known that Aspergillus fumigatus secretes a serine protease ALP1 of the subtilisin family in the presence of extracellular protein substrates. We found conditions of A. fumigatus culturing that provide a high ALP1 activity inside cells without induction by extracellular proteins. The identity of the properties of the secreted and intracellular enzymes was shown. A thermostable protein inhibitor of the ALP1 protease was isolated from the plasmodium of the myxomycete Physarum polycephalum. Its molecular mass is 32-33 kDa. The inhibitor inhibits the ALP1 protease activity with IC50 of 0.14 microM. This protein was also shown to be a less efficient inhibitor of the activity of HIV-1 protease (IC50 2.5 microM). The English version of the paper: Russian Journal of Bioorganic Chemistry, 2005, vol. 31, no. 3; see also http://www.maik.ru.

摘要

已知烟曲霉在存在细胞外蛋白质底物的情况下会分泌枯草杆菌蛋白酶家族的丝氨酸蛋白酶ALP1。我们发现了烟曲霉的培养条件,该条件可在细胞内提供高ALP1活性,而无需细胞外蛋白质诱导。已证明分泌型和细胞内酶的特性相同。从多头绒泡菌的原质团中分离出了ALP1蛋白酶的一种热稳定蛋白抑制剂。其分子量为32 - 33 kDa。该抑制剂以0.14 microM的IC50抑制ALP1蛋白酶活性。该蛋白还被证明是HIV - 1蛋白酶活性的低效抑制剂(IC50为2.5 microM)。论文的英文版本:《俄罗斯生物有机化学杂志》,2005年,第31卷,第3期;另见http://www.maik.ru。

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