On origin and evolution of carbonic anhydrase isozymes: A phylogenetic analysis from whole-enzyme to active site

被引：11

作者：

Banerjee, Srijoni ^{[1
]}

Deshpande, Parag A. ^{[1
,2
]}

机构：

[1] Indian Inst Technol, Dept Chem Engn, Quantum & Mol Engn Lab, Kharagpur 721302, W Bengal, India

[2] Indian Inst Technol, Ctr Theoret Studies, Kharagpur 721302, W Bengal, India

来源：

COMPUTATIONAL BIOLOGY AND CHEMISTRY | 2016年 / 61卷

关键词：

Kingdom-specificity; Active site; Sequence alignment; Carbonic anhydrases; Biological function; Structural similarity; BETA; EXPRESSION; IRON;

D O I：

10.1016/j.compbiolchem.2016.01.003

中图分类号：

Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Genetic evolution of carbonic anhydrase enzyme provides an interesting instance of functional similarity in spite of structural diversity of the members of a given family of enzymes. Phylogenetic analysis of alpha-, beta- and gamma-carbonic anhydrase was carried out to determine the evolutionary relationships among various members of the family with the enzyme marking its presence in a wide range of cellular and chromosomal locations. The presence of more than one class of enzymes in a particular organism was revealed by phylogenetic time tree. The evolutionary relationships among the members of animal, plant and microbial kingdom were developed. The study revises a long-established notion of kingdom-specificity of the different classes of carbonic anhydrases and provides a new version of the presence of multiple classes of carbonic anhydrases in a single organism and the presence of a given class of carbonic anhydrase across different kingdoms. (C) 2016 Elsevier Ltd. All rights reserved.

引用

页码：121 / 129

页数：9

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