Lewis W G, Basford J M, Walton P L
Biochim Biophys Acta. 1978 Feb 10;522(2):551-60. doi: 10.1016/0005-2744(78)90087-6.
The action of Armillaria mellea protease has been evaluated on a number of polypeptide substrates. It has been shown to split the Pro7-Lys8 bonds in both native and oxidised lysine-vasopressin and the Ser11-Lys12 bond in glucagon. No other splits were detected in these substrates. The enzyme also caused extensive degradation of S-carboxymethyl lysozyme, S-carcoxymethyl pepsinogen and oxidised ribonuclease. A. In each case the only new amino-terminal residue to appear was lysine. A. mellea protease was inhibited by the chelating agents 1,10-phenanthroline, alpha, alpha'-bipyridine and imidazole. The pK1 values (negative log10 of concentration required for 50% inhibition) for these three inhibitors were 3.9, 3.4 and 1.1, respectively. Lysine, S-2-aminoethylcysteine and short chain aliphatic amines also proved to be relatively good inhibitors of A. mellea protease while arginine was a poor inhibitor.
已在多种多肽底物上评估了蜜环菌蛋白酶的作用。结果表明，它能裂解天然和氧化型赖氨酸加压素中的Pro7-Lys8键以及胰高血糖素中的Ser11-Lys12键。在这些底物中未检测到其他裂解情况。该酶还会导致S-羧甲基溶菌酶、S-羧甲基胃蛋白酶原和氧化型核糖核酸酶发生广泛降解。A. 在每种情况下，唯一出现的新氨基末端残基都是赖氨酸。蜜环菌蛋白酶受到螯合剂1,10-菲咯啉、α,α'-联吡啶和咪唑的抑制。这三种抑制剂的pK1值（50%抑制所需浓度的负对数）分别为3.9、3.4和1.1。赖氨酸、S-2-氨基乙基半胱氨酸和短链脂肪胺也被证明是蜜环菌蛋白酶相对较好的抑制剂，而精氨酸是一种较差的抑制剂。
