Carbonic Anhydrase in Marine Organism

A special issue of Marine Drugs (ISSN 1660-3397).

Deadline for manuscript submissions: closed (31 December 2020) | Viewed by 7183

Special Issue Editor


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Guest Editor
Neurofarba Department, Section of Farmaceutical and Neutraceutical Sciences, University of Florence, Sesto Fiorentino, 50019 Florence, Italy
Interests: drug design; metalloenzymes; carbonic anhydrases; anticancer agents; antiinfectives; sulfonamides; coumarins
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Dear Colleagues,

Carbonic anhydrases (CAs, EC 4.2.1.1) are highly abundant metalloenzymes in many marine organisms, where they play crucial physiological functions connected with pH regulation, calcification, metabolism, etc. In many such organisms, among which diatoms, corals, molluscs, marine algae, etc., such enzymes were thoroughly investigated, whereas, in other phyla (e.g., arthropods), there are quite scarce data regarding them. Furthermore, the climate change due to the raise of CO2 levels in the atmosphere and the oceans may interfere significantly with the life processes all over the planet, and the CAs, which use CO2/bicarbonate as substrates, may play a crucial role in mitigating disastrous consequences. In this Special Issue of Marine Drugs, I invite researchers from all fields to present their recent contributions (original as well as review articles) on the various aspects of the chemistry, biochemistry, physiology and pharmacology of CAs from various marine organisms.

Prof. Dr. Claudiu T. Supuran
Guest Editor

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Keywords

  • Carbonic anhydrase

Published Papers (2 papers)

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Research

9 pages, 603 KiB  
Article
Activation Studies of the γ-Carbonic Anhydrases from the Antarctic Marine Bacteria Pseudoalteromonas haloplanktis and Colwellia psychrerythraea with Amino Acids and Amines
by Andrea Angeli, Sonia Del Prete, Sameh M. Osman, Zeid AlOthman, William A. Donald, Clemente Capasso and Claudiu T. Supuran
Mar. Drugs 2019, 17(4), 238; https://doi.org/10.3390/md17040238 - 22 Apr 2019
Cited by 8 | Viewed by 3084
Abstract
The γ-carbonic anhydrases (CAs, EC 4.2.1.1) present in the Antarctic marine bacteria Pseudoalteromonas haloplanktis and Colwellia psychrerythraea, herein referred to as PhaCA and CpsCA, respectively, were investigated for their activation with a panel of 24 amino acids and amines. Both bacteria are [...] Read more.
The γ-carbonic anhydrases (CAs, EC 4.2.1.1) present in the Antarctic marine bacteria Pseudoalteromonas haloplanktis and Colwellia psychrerythraea, herein referred to as PhaCA and CpsCA, respectively, were investigated for their activation with a panel of 24 amino acids and amines. Both bacteria are considered Antarctic models for the investigation of photosynthetic and metabolic pathways in organisms adapted to live in cold seawater. PhaCA was much more sensitive to activation by these compounds compared to the genetically related enzyme CpsCA. The most effective PhaCA activators were d-Phe, l-/d-DOPA, l-Tyr and 2-pyridyl-methylamine, with the activation constant KA values of 0.72–3.27 µM. d-His, l-Trp, d-Tyr, histamine, dopamine, serotonin anddicarboxylic amino acids were also effective activators of PhaCA, with KA values of 6.48–9.85 µM. CpsCA was activated by d-Phe, d-DOPA, l-Trp, l-/d-Tyr, 4-amino-l-Phe, histamine, 2-pyridyl-methylamine and l-/d-Glu with KA values of 11.2–24.4 µM. The most effective CpsCA activator was l-DOPA (KA of 4.79 µM). Given that modulators of CAs from Antarctic bacteria have not been identified and investigated in detail for their metabolic roles to date, this research sheds some light on these poorly understood processes. Full article
(This article belongs to the Special Issue Carbonic Anhydrase in Marine Organism)
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11 pages, 1802 KiB  
Article
Comparison of the Sulfonamide Inhibition Profiles of the α-Carbonic Anhydrase Isoforms (SpiCA1, SpiCA2 and SpiCA3) Encoded by the Genome of the Scleractinian Coral Stylophora pistillata
by Sonia Del Prete, Silvia Bua, Fatmah A. S. Alasmary, Zeid AlOthman, Sylvie Tambutté, Didier Zoccola, Claudiu T. Supuran and Clemente Capasso
Mar. Drugs 2019, 17(3), 146; https://doi.org/10.3390/md17030146 - 01 Mar 2019
Cited by 5 | Viewed by 3246
Abstract
The ubiquitous metalloenzymes carbonic anhydrases (CAs, EC 4.2.1.1) are responsible for the reversible hydration of CO2 to bicarbonate (HCO3) and protons (H+). Bicarbonate may subsequently generate carbonate used in many functional activities by marine organisms. CAs play [...] Read more.
The ubiquitous metalloenzymes carbonic anhydrases (CAs, EC 4.2.1.1) are responsible for the reversible hydration of CO2 to bicarbonate (HCO3) and protons (H+). Bicarbonate may subsequently generate carbonate used in many functional activities by marine organisms. CAs play a crucial role in several physiological processes, e.g., respiration, inorganic carbon transport, intra and extra-cellular pH regulation, and bio-mineralization. Multiple transcript variants and protein isoforms exist in the organisms. Recently, 16 α-CA isoforms have been identified in the coral Stylophora pistillata. Here, we focalized the interest on three coral isoforms: SpiCA1 and SpiCA2, localized in the coral-calcifying cells; and SpiCA3, expressed in the cytoplasm of the coral cell layers. The three recombinant enzymes were heterologously expressed and investigated for their inhibition profiles with sulfonamides and sulfamates. The three coral CA isoforms differ significantly in their susceptibility to inhibition with sulfonamides. This study provides new insights into the coral physiology and the comprehension of molecular mechanisms involved in the bio-mineralization processes, since CAs interact with bicarbonate transporters, accelerating the trans-membrane bicarbonate movement and modulating the pH at both sides of the plasma membranes. Full article
(This article belongs to the Special Issue Carbonic Anhydrase in Marine Organism)
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