Yamamoto K, Kojima Y, Kikuchi T, Shigyo T, Sugihara K, Takashio M, Emi S
Tsuruga Institute of Biotechnology, Toyobo Co., Ltd., Fukui.
J Biochem. 1996 Jan;119(1):80-4. doi: 10.1093/oxfordjournals.jbchem.a021219.
The nucleotide sequence of the uricase gene from the thermophilic bacterium Bacillus sp. TB-90 was determined. The primary structure of the uricase deduced from the nucleotide sequence comprised 332 amino acids, with a total molecular mass of 37,994 Da. The molecular mass of the subunit of the uricase produced by the transformant of Escherichia coli agreed well with this value. However, the molecular mass of a subunit of the uricase produced by Bacillus sp. TB-90 was found to be 34,000 Da by SDS-PAGE. The difference between these molecular masses was attributed to processing of the C-terminal 13 amino acid residue in Bacillus sp. TB-90. Comparison of the enzymatic properties of both uricases showed that the thermostability of the uricase produced by the transformant was enhanced by about 10 degrees C in comparison to that produced by Bacillus sp. TB-90.
测定了嗜热芽孢杆菌TB-90尿酸酶基因的核苷酸序列。从核苷酸序列推导的尿酸酶一级结构由332个氨基酸组成，总分子量为37994道尔顿。大肠杆菌转化体产生的尿酸酶亚基分子量与此值吻合良好。然而，通过SDS-PAGE发现芽孢杆菌TB-90产生的尿酸酶亚基分子量为34000道尔顿。这些分子量之间的差异归因于芽孢杆菌TB-90中C末端13个氨基酸残基的加工。两种尿酸酶酶学性质的比较表明，与芽孢杆菌TB-90产生的尿酸酶相比，转化体产生的尿酸酶热稳定性提高了约10℃。
