Cloning and characterization of a sulfonate/α-ketoglutarate dioxygenase from Saccharomyces cerevisiae
Cloning and characterization of a sulfonate/α-ketoglutarate dioxygenase from Saccharomyces cerevisiae
复制标题
DOI：
10.1128/jb.181.18.5876-5879.1999
复制
发表时间：
1999-09-01
影响因子：
3.2
通讯作者：
Hausinger, RP
中科院分区：
文献类型：
--
作者：
Hogan, DA;Auchtung, TA;Hausinger, RP
该基因序列与大肠杆菌牛磺酸/ α -酮戊二酸双加氧酶有31.5%的同源性，与富营养Ralstonia eutropha TfdA（一种除草剂降解酶）有27%的同源性。纯化后的重组酵母蛋白是一种Fe（II）依赖性磺酸/ α -酮戊二酸双加氧酶，虽然牛磺酸是一种较差的底物，但可以利用多种其他磺酸盐，其中最好的天然底物是异硫酸盐和牛磺胆酸盐，编码该酶的基因被破坏会对酿酒酵母利用异硫酸盐和牛磺酸作为硫源产生负面影响，这有力地证明了YLL057c在磺酸分解代谢中发挥作用。
The Saccharomyces cerevisiae open reading frame YLL057c is predicted to encode a gene product with 31.5% amino acid sequence identity to Escherichia coli taurine/alpha-ketoglutarate dioxygenase and 27% identity to Ralstonia eutropha TfdA, a herbicide-degrading enzyme. Purified recombinant yeast protein is shown to be an Fe(II)-dependent sulfonate/alpha-ketoglutarate dioxygenase, Although taurine is a poor substrate, a variety of other sulfonates are utilized, with the best natural substrates being isethionate and taurocholate, Disruption of the gene encoding this enzyme negatively affects the use of isethionate and taurine as sulfur sources by S. cerevisiae, providing strong evidence that YLL057c plays a role in sulfonate catabolism.