血管紧张素转化酶结构与功能的生物信息学分析  

Bioinformatics Analysis of Angiotensin Converting Enzyme(ACE) Structure and Function of Human

作　　者：谢晓明[1] 邱芝青 谢丽明[2] 雷桅[1] 

机构地区：[1]广东医学院附属医院心血管内科,广东湛江524001 [2]广东医学院附属医院药剂科,广东湛江524001

出　　处：《中国医药指南》2014年第34期3-4,10,共3页Guide of China Medicine

基　　金：国家自然科学基金(编号:81300035);广东省自然科学基金(编号:S2013040012115)

摘　　要：目的血管紧张素转化酶(angiotensin converting enzyme,ACE,EC 3.4.15.1)是人类血压控制系统的关键酶,其抑制剂也是广泛应用于临床的降压和心力衰竭治疗一线药物。方法本文采用Protparam等生物信息学方法和工具对ACE基因及其编码蛋白的序列特征、分子结构和理化性质等进行了预测分析。结果表明该基因的核苷酸序列全长2473 bp,包括3'-UTR、ORF和5'-UTR序列,其蛋白分子式C3752H5724N1020O1086S26,含732个氨基酸残基,以Leu含量最高,定位于分泌途径,含跨膜结构域,是一种含有21个碱基的质体转运肽和Glu Zincin功能域的疏水性不稳定蛋白质。其二级结构和三维模型解析完成,结果显示以随机卷曲和α-螺旋为主。结论本研究可为深入开展人ACE蛋白的酶学特性和血流动力学调节机制研究提供理论参考。Objective Angiotensin converting enzyme （ACE, EC 3.4.15.1） is the key enzyme in human blood press control system, and its inhibitor has been used widely as the clinic first-line drug of antihypertensive-and heart-failure treatment. Method The sequence characteristics, molecular structure and physicochemical properties of ACE gene and its coding protein were predicted and analyzed by bioinformatic methods and tools like Protparam. Results The length of nucleotide acid sequence was 2473 bp, including 3＇-UTR, ORF and 5＇-UTR; the molecular formula of the ACE protein was C3752H5724N102001086S26 containing 732 aa, and Leu was the most abundant amino acid; ACE was anchored in the secretory pathway, with transmembrane domain, it was an unstable protein with a 21 aa plastidial transit-peptide. At last, its secondary and 3-D modelling was successfully established and it contained mainly alpha helix and random coil. Conclusion This study can provide the theory references for the enzymatic properties and hemodynamics regulation mechanism of human ACE protein.

关 键 词：血管紧张素转化酶 生物信息学 核酸 蛋白 

分 类 号：R972.4[医药卫生—药品]