The PepSY domain: a regulator of peptidase activity in the microbial environment?

The PepSY domain: a regulator of peptidase activity in the microbial environment?
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DOI:
10.1016/j.tibs.2004.02.004
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发表时间:
2004-04-01
影响因子:
13.8
通讯作者:
Bateman, A
Bateman, A
中科院分区:
生物学1区
文献类型:
--
作者:
Yeats, C;Rawlings, ND;Bateman, A

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M4家族蛋白是常见的真菌性金属肽酶,参与从营养物生产到致病性的一系列功能。通常,它们由具有抑制和伴侣功能的前肽和肽酶单位组成。前肽被切割,但保持附着,直到肽酶被分泌,可以安全地激活。在这里,我们描述了前肽中的一个域,它可能包含抑制活性,但不包含伴侣活性。它也存在于许多非肽酶蛋白中,包括枯草芽孢杆菌(Bacillus subtilis)的YpeB蛋白——SleB孢子皮质裂解酶的一种调节剂——以及大量真细菌和古细菌细胞壁相关蛋白和分泌蛋白。我们认为它在局部环境中作为肽酶活性的调节剂,并保护细胞免受裂解。
The M4 family proteins are common eubacterial metallo-peptidases that are involved in a range of functions from nutrient production to pathogenicity. Typically, they consist of a propeptide with inhibitory and chaperone functions and a peptidase unit. The propeptide is cleaved but remains attached until the peptidase is secreted and can be safely activated. Here, we describe a domain in the propeptide that is likely to contain the inhibitory activity, but not the chaperone activity. It is also in many non-peptidase proteins, including Bacillus subtilis YpeB protein - a regulator of SleB spore cortex lytic enzyme - and a large number of eubacterial and archaeal cell-wall-associated and secreted proteins. We propose that it acts as a regulator of peptidase activity in the local environment and also protects the cell from lysis.