Literature DB >> 23137351

Structural annotation of human carbonic anhydrases.

Mayank Aggarwal1, Christopher D Boone, Bhargav Kondeti, Robert McKenna.   

Abstract

Carbonic anhydrases (CAs, EC 4.2.1.1) are a family of metalloenzymes that catalyze the reversible interconversion of CO(2) and HCO(3)(-). Of the 15 isoforms of human (h) α-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 Zn(2+) 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.

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Year:  2012        PMID: 23137351     DOI: 10.3109/14756366.2012.737323

Source DB:  PubMed          Journal:  J Enzyme Inhib Med Chem        ISSN: 1475-6366            Impact factor:   5.051


  33 in total

1.  Preliminary X-ray crystallographic analysis of β-carbonic anhydrase psCA3 from Pseudomonas aeruginosa.

Authors:  Melissa Pinard; Shalaka Lotlikar; Marianna A Patrauchan; Robert McKenna
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2013-07-27

2.  Structural and catalytic effects of proline substitution and surface loop deletion in the extended active site of human carbonic anhydrase II.

Authors:  Christopher D Boone; Valerio Rasi; Chingkuang Tu; Robert McKenna
Journal:  FEBS J       Date:  2015-03-23       Impact factor: 5.542

3.  α-Carbonic Anhydrases Possess Thioesterase Activity.

Authors:  Muhammet Tanc; Fabrizio Carta; Andrea Scozzafava; Claudiu T Supuran
Journal:  ACS Med Chem Lett       Date:  2015-01-19       Impact factor: 4.345

4.  Saccharin: a lead compound for structure-based drug design of carbonic anhydrase IX inhibitors.

Authors:  Brian P Mahon; Alex M Hendon; Jenna M Driscoll; Gregory M Rankin; Sally-Ann Poulsen; Claudiu T Supuran; Robert McKenna
Journal:  Bioorg Med Chem       Date:  2014-12-23       Impact factor: 3.641

Review 5.  Carbon dioxide-sensing in organisms and its implications for human disease.

Authors:  Eoin P Cummins; Andrew C Selfridge; Peter H Sporn; Jacob I Sznajder; Cormac T Taylor
Journal:  Cell Mol Life Sci       Date:  2013-09-18       Impact factor: 9.261

6.  Structural and catalytic characterization of a thermally stable and acid-stable variant of human carbonic anhydrase II containing an engineered disulfide bond.

Authors:  Christopher D Boone; Andrew Habibzadegan; Chingkuang Tu; David N Silverman; Robert McKenna
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2013-07-13

7.  Carbon Dioxide "Trapped" in a β-Carbonic Anhydrase.

Authors:  Mayank Aggarwal; Teck Khiang Chua; Melissa A Pinard; Doletha M Szebenyi; Robert McKenna
Journal:  Biochemistry       Date:  2015-10-16       Impact factor: 3.162

8.  A sucrose-binding site provides a lead towards an isoform-specific inhibitor of the cancer-associated enzyme carbonic anhydrase IX.

Authors:  Melissa A Pinard; Mayank Aggarwal; Brian P Mahon; Chingkuang Tu; Robert McKenna
Journal:  Acta Crystallogr F Struct Biol Commun       Date:  2015-09-23       Impact factor: 1.056

9.  Structural, catalytic and stabilizing consequences of aromatic cluster variants in human carbonic anhydrase II.

Authors:  Christopher D Boone; Sonika Gill; Chingkuang Tu; David N Silverman; Robert McKenna
Journal:  Arch Biochem Biophys       Date:  2013-09-10       Impact factor: 4.013

10.  Effects of cryoprotectants on the structure and thermostability of the human carbonic anhydrase II-acetazolamide complex.

Authors:  Mayank Aggarwal; Christopher D Boone; Bhargav Kondeti; Chingkuang Tu; David N Silverman; Robert McKenna
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2013-04-19
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