Oh T K, Park M J, Lee J K, Kim H K, Nam H S
Microbial Enzyme Research Unit, Korea Research Institute of Bioscience & Biotechnology, Yusung, Taejon, South Korea.
Biosci Biotechnol Biochem. 1997 Nov;61(11):1934-6. doi: 10.1271/bbb.61.1934.
An aminopeptidase A (EC 3.4.11.7) was purified to homogeneity from Bacillus licheniformis NS115 and its enzymatic properties were characterized. The enzyme had an apparent molecular mass of 64 kDa, consisting of heterodimeric 42 kDa and 22 kDa subunits, and is a new enzyme from N-terminal analysis of heavy and light subunits. The light subunit had no catalytic activity against the substrate and apparent K(m) values of heavy and whole enzyme were 0.26 and 0.087 mM of gamma-glutamyl-p-nitroanilide, respectively.
从地衣芽孢杆菌NS115中纯化出一种氨肽酶A(EC 3.4.11.7)并对其酶学性质进行了表征。该酶的表观分子量为64 kDa,由42 kDa和22 kDa的异源二聚体亚基组成,通过对重链和轻链亚基的N端分析可知它是一种新酶。轻链亚基对底物没有催化活性,重链亚基和全酶对γ-谷氨酰-对硝基苯胺的表观K(m)值分别为0.26 mM和0.087 mM。