Healy V, O'Connell J, McCarthy T V, Doonan S
Department of Biochemistry, University College Cork, Lee Maltings, Prospect Row, Cork, Ireland.
Biochem Biophys Res Commun. 1999 Aug 19;262(1):60-3. doi: 10.1006/bbrc.1999.1151.
The fruiting body of the basidiomycete fungus Armillaria mellea produces a lysine-specific proteinase which exhibits both potent fibrinolytic activity and a remarkable resistance to denaturing agents. An improved purification protocol has been developed for this enzyme and the sequence of the 26 N-terminal amino acid residues of the pure protein has been determined by gas-phase sequencing. Searches of the SwissProt database showed that the N-terminal sequence of A. mellea proteinase is highly similar to those of lysine-specific metalloendopeptidases from the basidiomycetes Grifola frondosa and Pleurotus ostreatus. These results support the view that the A. mellea proteinase is a member of a novel class of lysine-specific metalloendopeptidases which may be exclusive to basidiomycete fungi.
担子菌蜜环菌的子实体产生一种赖氨酸特异性蛋白酶，该酶既具有强大的纤溶活性，又对变性剂具有显著抗性。已为这种酶开发了一种改进的纯化方案，并通过气相测序确定了纯蛋白26个N端氨基酸残基的序列。对瑞士蛋白质数据库的搜索表明，蜜环菌蛋白酶的N端序列与担子菌灰树花和平菇的赖氨酸特异性金属内肽酶的序列高度相似。这些结果支持了这样一种观点，即蜜环菌蛋白酶是一类新型赖氨酸特异性金属内肽酶的成员，这类酶可能是担子菌所特有的。
