α-裂解蛋白酶

α-裂解蛋白酶（aLP）是蛋白质组学应用的一种替代型特异性蛋白酶。该蛋白酶可在T、A、S和V残基后进行切割。它可产生与胰蛋白酶具有相似平均长度的肽。aLP首先是从粘细菌杆菌产酶溶杆菌中分离得到的。aLP的前体形式含有397个氨基酸。在其成熟体形式中，aLP含有198个氨基酸。其三级结构核心类似于胰腺丝氨酸蛋白酶。aLP的晶体结构研究已被报道。也有关于aLP活性位点和催化机制的几项研究。前区在aLP的激活、分泌和折叠中的作用已被研究。在各种溶液组分存在下aLP的活性如下：0.1％脱氧胆酸钠：~1.75倍增强的活性 1.0%脱氧胆酸钠：~60%的活性0.1% SDS：~50%的活性1.0% SDS：~40%的活性1M盐酸胍：~20%的活性4M盐酸胍：~1%的活性（基本上已灭活） Alpha-lytic protease (aLP) is an alternative specificity protease for proteomics applications. This protease cleaves after T, A, S, and V residues. It generates peptides of similar average length as trypsin. aLP was first isolated from the myxobacterium Lysobacter enzymogenes . The pro-form of aLP is 397 amino acids long. In its mature form, aLP is 198 amino acids long. Its tertiary structural core resembles those of pancreatic serine proteases. Crystal structure studies of aLP have been reported. Several studies are available on the active site and catalytic mechanism of aLP. The role of the pro-region in the activation, secretion and folding of aLP has been studied. The activity of aLP in the presence of various solution components is as follows: 0.1% sodium deoxycholate: ~1.75-fold enhanced activity 1.0% sodium deoxycholate: ~60% activity 0.1% SDS: ~50% activity 1.0% SDS: ~40% activity 1 M guanidine HCl: ~20% activity 4 M guanidine HCl: ~1% activity (essentially inactivated)

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