Seery L T, McCabe B D, Schoenberg D R, Whitehead A S
Department of Genetics and Biotechnology Institute, Trinity College, Dublin 2, Ireland.
Biochem Biophys Res Commun. 1994 Dec 30;205(3):1539-46. doi: 10.1006/bbrc.1994.2842.
S-Adenosyl-L-homocysteine hydrolase (EC 3.3.1.1) is an important enzyme in the trans-sulphuration pathway, mediating the conversion of S-adenosyl-L-homocysteine to adenosine and L-homocysteine. We have identified a cDNA clone from Xenopus laevis, encoding a protein of 433 aa, which is highly conserved with S-Adenosyl-L-homocysteine hydrolases (Adohcyases) from other species. Expression of Adohcyase mRNA in X.laevis tadpoles is detectable from developmental Stage 27 onwards. Phylogenetic analysis of available Adohcyase sequences indicates that species cluster essentially as predicted from morphological data. Furthermore, we estimate that S-adenosyl-L-homocysteine hydrolase is evolving very slowly, almost 10 times slower than the average rate.
S-腺苷-L-高半胱氨酸水解酶(EC 3.3.1.1)是转硫途径中的一种重要酶,介导S-腺苷-L-高半胱氨酸转化为腺苷和L-高半胱氨酸。我们从非洲爪蟾中鉴定出一个cDNA克隆,其编码一个433个氨基酸的蛋白质,该蛋白质与其他物种的S-腺苷-L-高半胱氨酸水解酶(Adohcyases)高度保守。从发育的第27阶段开始,可检测到Adohcyase mRNA在非洲爪蟾蝌蚪中的表达。对现有Adohcyase序列的系统发育分析表明,物种聚类基本与形态学数据预测的一致。此外,我们估计S-腺苷-L-高半胱氨酸水解酶的进化非常缓慢,几乎比平均速率慢10倍。