Structural annotation of human carbonic anhydrases

被引:202
作者
Aggarwal, Mayank [1 ]
Boone, Christopher D. [1 ]
Kondeti, Bhargav [1 ]
McKenna, Robert [1 ]
机构
[1] Univ Florida, Coll Med, Dept Biochem & Mol Biol, Gainesville, FL 32610 USA
基金
美国国家卫生研究院;
关键词
Human carbonic anhydrase; annotation; classification; comparison; thermostability; industrial applications; IN-VIVO SELECTIVITY; CRYSTAL-STRUCTURE; ACTIVE-SITE; THERAPEUTIC APPLICATIONS; GUANIDINE-HYDROCHLORIDE; EXTRACELLULAR DOMAIN; PROBING SUBSTRUCTURE; CIRCULAR-DICHROISM; THERMAL-STABILITY; INHIBITOR BINDING;
D O I
10.3109/14756366.2012.737323
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要
Carbonic anhydrases (CAs, EC 4.2.1.1) are a family of metalloenzymes that catalyze the reversible interconversion of CO2 and HCO3-. Of the 15 isoforms of human (h) alpha-CA, 12 are catalytic (hCAs I-IV, VA, VB, VI, VII, IX, XII-XIV). The remaining three acatalytic isoforms (hCAs VIII, X and XI) lack the active site Zn2+ and are referred to as CA-related proteins (CA-RPs); however, their function remains elusive. Overall these isoforms are very similar to each other in structure but they differ in their expression and distribution. The favourable properties of hCA II such as fast kinetics, easy expression and purification, high solubility and intermediate heat resistance have made it an attractive candidate for numerous industrial applications. This review highlights the structural similarity and stability comparison among hCAs.
引用
收藏
页码:267 / 277
页数:11
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