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Journal ArticleDOI

Anion inhibition profiles of the complete domain of the η-carbonic anhydrase from Plasmodium falciparum.

TLDR
Cloned, purified and investigated the catalytic activity and anion inhibition profiles of a full catalytic domain (358 amino acid residues) carbonic anhydrase from Plasmodium falciparum, PfCAdom, an enzyme belonging to the η-CA class and identified in the genome of the malaria-producing protozoa.
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This article is published in Bioorganic & Medicinal Chemistry.The article was published on 2016-09-15. It has received 32 citations till now. The article focuses on the topics: Carbonic anhydrase & Enzyme.

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Citations
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Journal ArticleDOI

An Overview of the Bacterial Carbonic Anhydrases

TL;DR: Investigation of bacterial CA inhibitors and activators may be relevant for finding antibiotics with a new mechanism of action, and afford the opportunity to design both novel therapeutic agents, as well as biomimetic processes for CO2 capture.
Journal ArticleDOI

Biomedical applications of prokaryotic carbonic anhydrases.

TL;DR: An overview of the potential use of CAs in biomedical applications, as drug targets, bioindicators, and within artificial organs is presented.
Journal ArticleDOI

Bacterial ι-carbonic anhydrase: a new active class of carbonic anhydrase identified in the genome of the Gram-negative bacterium Burkholderia territorii .

TL;DR: For the first time, the recombinant bacterial ι-CA (acronym BteCAι) identified in the genome of Burkholderia territorii is cloned, expressed, and purified and showed that the enzyme is formed by two equivalent monomers having a structure similar to a butterfly.
Journal ArticleDOI

Carbonic Anhydrase from Porphyromonas Gingivalis as a Drug Target.

TL;DR: This work focuses on the study of the carbonic anhydrases encoded in the genome of the Gram-negative bacterium Porphyromonas gingivalis as a possible drug target for periodontitis.
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Escherichia coli γ -carbonic anhydrase: characterisation and effects of simple aromatic/heterocyclic sulphonamide inhibitors.

TL;DR: The hypothesis that the synthesis of new drugs capable of interfering selectively with the bacterial CA activity, avoiding the inhibition of the human α -CAs, is achievable and may lead to novel antibacterials is reinforced.
References
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Journal ArticleDOI

Carbonic anhydrases: novel therapeutic applications for inhibitors and activators

TL;DR: The biological rationale for the novel uses of inhibitors or activators of CA activity in multiple diseases is discussed, and progress in the development of specific modulators of the relevant CA isoforms is highlighted, some of which are now being evaluated in clinical trials.
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The Carbon Dioxide Hydration Activity of Carbonic Anhydrase I. STOP-FLOW KINETIC STUDIES ON THE NATIVE HUMAN ISOENZYMES B AND C

TL;DR: The present kinetic results are interpreted as representing a great specificity of carbonic anhydrase for the binding of its substrate CO2, and it is proposed that the enzyme-catalyzed hydration of CO2 requires, not only water activation by a basic group, but also charge neutralization in the transition state by an electron acceptor function.
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How many carbonic anhydrase inhibition mechanisms exist

TL;DR: Recent findings in the field of CA inhibition may be useful for a structure-based drug design approach of more selective/potent modulators of the activity of these enzymes.
Journal ArticleDOI

Carbonic anhydrases--an overview.

TL;DR: Several important physiological and physio-pathological functions are played by CA isozymes present in organisms all over the phylogenetic tree, related to respiration and transport of CO(2)/bicarbonate between metabolizing tissues and the lungs, pH andCO(2) homeostasis, electrolyte secretion in a variety of tissues/organs, biosynthetic reactions, and more.
Journal ArticleDOI

An overview of the alpha-, beta- and gamma-carbonic anhydrases from Bacteria: can bacterial carbonic anhydrases shed new light on evolution of bacteria?

TL;DR: It is proposed that bacterial CAs can be used as markers for understanding the evolution and genetic variability of the Gram-positive and Gram-negative bacteria.
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