Structure and mechanism of carbonic anhydrase

Lindskog, Sven

doi:10.1016/s0163-7258(96)00198-2

Cited by 1,022Enzyme function and inhibitionChemical Reaction MechanismsEnzyme Structure and Function

Structure and mechanism of carbonic anhydrase

Lindskog, Sven·1997·Pharmacology & Therapeutics

DOI 10.1016/s0163-7258(96)00198-2

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Abstract

Carbonic anhydrase (CA; carbonate hydro-lyase, EC 4.2.1.1) is a zinc-containing enzyme that catalyzes the reversible hydration of carbon dioxide: CO2+ H2O<-->HCO3(-)+H+. The enzyme is the target for drugs, such as acetazolamide, methazolamide, and dichlorphenamide, for the treatment of glaucoma. There are three evolutionarily unrelated CA families, designated alpha, beta, and gamma. All known CAs from the animal kingdom are of the alpha type. There are seven mammalian CA isozymes with different tissue distributions and intracellular locations, CA I-VII. Crystal structures of human CA I and II, bovine CA III, and murine CA V have been determined. All of them have the same tertiary fold, with a central 10-stranded beta-sheet as the dominating secondary structure element. The zinc ion is located in a cone-shaped cavity and coordinated to three histidyl residues and a solvent molecule. Inhibitors bind at or near the metal center guided by a hydrogen-bonded system comprising Glu-106 and Thr-199. The catalytic mechanism of CA II has been studied in particular detail. It involves an attack of zinc-bound OH- on a CO2 molecule loosely bound in a hydrophobic pocket. The resulting zinc-coordinated HCO3- ion is displaced from the metal ion by H2O. The rate-limiting step is an intramolecular proton transfer from the zinc-bound water molecule to His-64, which serves as a proton shuttle between the metal center and buffer molecules in the reaction medium.

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The affinities of CA for carbon dioxide and bicarbonate are low enough that they are not likely to inhibit reactivity of CA with nitrite.
“The affinities of CA for carbon dioxide and bicarbonate are low enough that they are not likely to inhibit reactivity of CA with nitrite [103–105].”
From Mechanisms of nitrite bioactivation (2014) · cites this paper as [104]

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Self-citation
Catalytic and Inhibitor-Binding Properties of Some Active-Site Mutants of Human Carbonic Anhydrase I
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Self-citation
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Self-citation
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Metallo-β-lactamases in the Age of Multidrug Resistance: From Structure and Mechanism to Evolution, Dissemination, and Inhibitor Design
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Pharmacological and ocular hypotensive properties of topical carbonic anhydrase inhibitors
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A genome-wide analysis of biomineralization-related proteins in the sea urchin Strongylocentrotus purpuratus
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Integrated Microfluidic Device for Automated Single Cell Analysis Using Electrophoretic Separation and Electrospray Ionization Mass Spectrometry
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Entrapment of Carbon Dioxide in the Active Site of Carbonic Anhydrase II
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Elemental zinc to zinc nanoparticles: is ZnO NPs crucial for life? Synthesis, toxicological, and environmental concerns
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The carbonic anhydrase isoforms of Chlamydomonas reinhardtii: intracellular location, expression, and physiological roles
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Generation of nitric oxide from nitrite by carbonic anhydrase: a possible link between metabolic activity and vasodilation
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Recombinant PNPLA3 protein shows triglyceride hydrolase activity and its I148M mutation results in loss of function
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Bioinspired Metal–Organic Framework for Trace CO 2 Capture
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Coordination-driven innovations in low-energy catalytic processes: Advancing sustainability in chemical production
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The crystal structure of the DNase domain of colicin E7 in complex with its inhibitor Im7 protein
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Solvent-Mediated Proton Transfer in Catalysis by Carbonic Anhydrase
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Biocatalytic capture of CO2 with carbonic anhydrase and its transformation to solid carbonate
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Structure and Function of Carbonic Anhydrases from Mycobacterium tuberculosis
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A Closer Look at the Active Site of γ-Class Carbonic Anhydrases: High-Resolution Crystallographic Studies of the Carbonic Anhydrase from Methanosarcina thermophila,
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Mechanism of Membrane Insertion of a Multimeric β-Barrel Protein
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Atomic Crystal and Molecular Dynamics Simulation Structures of Human Carbonic Anhydrase II: Insights into the Proton Transfer Mechanism,
Fisher, S. Z., Maupin, C. M., Budayova-Spano, M., Lakshmanan Govindasamy, A., Tu, C., Agbandje‐McKenna, M., Silverman, D. N., Voth, G. A., & McKenna, R. (2007) · Biochemistry · doi:10.1021/bi062066y · Cited by 166 · see citing works
Structural and Kinetic Characterization of Active-Site Histidine as a Proton Shuttle in Catalysis by Human Carbonic Anhydrase II,
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The Roles of Water in the Protein Matrix: A Largely Untapped Resource for Drug Discovery
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Mechanisms of nitrite bioactivation
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A Short, Strong Hydrogen Bond in the Active Site of Human Carbonic Anhydrase II
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Calcite precipitation induced by Bacillus cereus MRR2 cultured at different Ca2+ concentrations: Further insights into biotic and abiotic calcite
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Crystal structure of E. coli β–carbonic anhydrase, an enzyme with an unusual pH–dependent activity
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Nonaromatic Sulfonamide Group as an Ideal Anchor for Potent Human Carbonic Anhydrase Inhibitors: Role of Hydrogen-Bonding Networks in Ligand Binding and Drug Design
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A Role for Iron in an Ancient Carbonic Anhydrase
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Calcium Carbonate
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Mariprofundus ferrooxydans PV-1 the First Genome of a Marine Fe(II) Oxidizing Zetaproteobacterium
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Biomineralization-based conversion of carbon dioxide to calcium carbonate using recombinant carbonic anhydrase
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A light and electron microscopic study of the CB1 cannabinoid receptor in primate brain
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Role of Carbonic Anhydrases and Inhibitors in Acid–Base Physiology: Insights from Mathematical Modeling
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Proton Transfer in the Enzyme Carbonic Anhydrase: An ab Initio Study
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Carbonic Anhydrase Activators. Activation of Isoforms I, II, IV, VA, VII, and XIV with l - and d -Phenylalanine and Crystallographic Analysis of Their Adducts with Isozyme II: Stereospecific Recognition within the Active Site of an Enzyme and Its Consequences for the Drug Design
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Development and Application of Carbonyl Sulfide-Based Donors for H 2 S Delivery
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The mechanism of aqueous humour formation
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Sponge Paleogenomics Reveals an Ancient Role for Carbonic Anhydrase in Skeletogenesis
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Carbonic Anhydrase Activators. Activation of Isozymes I, II, IV, VA, VII, and XIV with L ‐ and D ‐Histidine and Crystallographic Analysis of Their Adducts with Isoform II: Engineering Proton‐Transfer Processes within the Active Site of an Enzyme
Temperini, C., Scozzafava, A., Vullo, D., & Supuran, C. T. (2006) · Chemistry - A European Journal · doi:10.1002/chem.200600159 · Cited by 133 · see citing works
Protonation and Reactivity towards Carbon Dioxide of the Mononuclear Tetrahedral Zinc and Cobalt Hydroxide Complexes, [TpBut,Me]ZnOH and [TpBut,Me]CoOH: Comparison of the Reactivity of the Metal Hydroxide Function in Synthetic Analogues of Carbonic Anhydrase
Bergquist, C., Fillebeen-Khan, T., Morlok, M. M., & Parkin, G. (2003) · Journal of the American Chemical Society · doi:10.1021/ja034711j · Cited by 131 · see citing works
Luminescent transition metal–organic frameworks: An emerging sensor for detecting biologically essential metal ions
Pamei, M., & Пузари, А. (2019) · Nano-Structures & Nano-Objects · doi:10.1016/j.nanoso.2019.100364 · Cited by 130 · see citing works
The use of carbonic anhydrase to accelerate carbon dioxide capture processes
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Authors: Lindskog, S.
Affiliations: Umeå University (SE)
Corresponding author: Lindskog, Sven
Venue: Pharmacology & Therapeutics
Publisher: Elsevier BV
Published: 1997-01
Volume: 74
Issue: 1
Pages: 1-20
ISSN: 0163-7258 (ISSN-L)
DOI: 10.1016/s0163-7258(96)00198-2
OpenAlex: W2035046825
Cited by: 1,022
References: 212
Citations by year: 2026: 38 · 2025: 52 · 2024: 63 · 2023: 50 · 2022: 49 · 2021: 49 · 2020: 34 · 2019: 45 · 2018: 46 · 2017: 38 · 2016: 42 · 2015: 40 · 2014: 41 · 2013: 47 · 2012: 48
FWCI: 1.07
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Pharmacology & Therapeutics (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme function and inhibition
Physical Sciences › Chemistry › Organic Chemistry › Chemical Reaction Mechanisms
Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords: carbonic anhydrase, zinc metalloenzyme, CO2 hydration, bicarbonate, catalytic mechanism, isozymes, crystal structure, acetazolamide, carbonic anhydrase inhibitors, glaucoma, proton transfer, histidine residues
MeSH terms: Animals, Carbonic Anhydrases, Catalysis, Humans, Protein Conformation, Structure-Activity Relationship

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Structure and mechanism of carbonic anhydrase

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