Kinsella B T, Doonan S
Biosci Rep. 1986 Oct;6(10):921-9. doi: 10.1007/BF01116247.
The nucleotide sequence of a 1.46 kb cDNA, selected from a human liver library by the expression of fumarase antigenic determinants, was determined using the dideoxy chain termination method. The cDNA contained an open reading frame extending from the extreme 5'-base and coding for a protein with 468 amino acids. This protein, with the exception of an N-terminal methionine, was identified as mitochondrial fumarase. The protein showed a high degree of identity of structure with the fumarase from Bacillus subtilis (56.6%) and a fumarase from Escherichia coli (product of the fumC gene, 59.3%), and a lower degree of identity with the aspartase of E. coli (37.2%).
通过富马酸酶抗原决定簇的表达从人肝脏文库中筛选出一个1.46 kb的cDNA,采用双脱氧链终止法测定其核苷酸序列。该cDNA包含一个从最末端5′碱基开始延伸的开放阅读框,编码一个含有468个氨基酸的蛋白质。除了N端的甲硫氨酸外,该蛋白质被鉴定为线粒体富马酸酶。该蛋白质与枯草芽孢杆菌的富马酸酶(56.6%)和大肠杆菌的富马酸酶(fumC基因产物,59.3%)在结构上具有高度同源性,与大肠杆菌的天冬氨酸酶的同源性较低(37.2%)。