串珠镰刀菌酸性蛋白酶的特异性
Specificity of acid protease from Fusarium moniliforme.
作者信息
Kuczek M, Nowak K, Kołaczkowska M
出版信息
Acta Biochim Pol. 1983;30(1):3-10.
PMID:6346763
Abstract
Specificity of acid protease from Fusarium moniliforme was investigated using beta chain of oxidized insulin. The enzyme is highly specific for the bonds involving aromatic and hydrophobic amino acid residues. It shows high affinity for the following bonds: Leu(15)-Tyr(16), Tyr(16)-Leu(17), Phe(24)-Phe(25), Phe(25)-Tyr(26), and somewhat lower for other three bonds: His(10)-Leu(11), Leu(11)-Val(12) and Tyr(26)-Thr(27) in oxidized beta chain of insulin.
摘要
利用氧化胰岛素的β链研究了串珠镰刀菌酸性蛋白酶的特异性。该酶对涉及芳香族和疏水氨基酸残基的键具有高度特异性。它对以下键表现出高亲和力：Leu(15)-Tyr(16)、Tyr(16)-Leu(17)、Phe(24)-Phe(25)、Phe(25)-Tyr(26)，而对胰岛素氧化β链中的其他三个键His(10)-Leu(11)、Leu(11)-Val(12)和Tyr(26)-Thr(27)的亲和力稍低。
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