A simple yet multifaceted 90 years old, evergreen enzyme: Carbonic anhydrase, its inhibition and activation
CT Supuran - Bioorganic & Medicinal Chemistry Letters, 2023 - Elsevier
Advances in the carbonic anhydrase (CA, EC 4.2. 1.1) research over the last three decades
are presented, with an emphasis on the deciphering of the activation mechanism, the …
are presented, with an emphasis on the deciphering of the activation mechanism, the …
Structure and mechanism of carbonic anhydrase
S Lindskog - Pharmacology & therapeutics, 1997 - Elsevier
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 …
that catalyzes the reversible hydration of carbon dioxide: CO2+ H2O↔ HCO3−+ H+. The …
Fast CO2 hydration kinetics impair heterogeneous but improve enzymatic CO2 reduction catalysis
The performance of heterogeneous catalysts for electrocatalytic CO2 reduction suffers from
unwanted side reactions and kinetic inefficiencies at the required large overpotential …
unwanted side reactions and kinetic inefficiencies at the required large overpotential …
A proficient enzyme
A Radzicka, R Wolfenden - Science, 1995 - science.org
Orotic acid is decarboxylated with a half-time (t1/2) of 78 million years in neutral aqueous
solution at room temperature, as indicated by reactions in quartz tubes at elevated …
solution at room temperature, as indicated by reactions in quartz tubes at elevated …
Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein− ligand binding
VM Krishnamurthy, GK Kaufman, AR Urbach… - Chemical …, 2008 - ACS Publications
Carbonic anhydrase (CA, EC 4.2. 1.1) is a protein that is especially well-suited to serve as a
model in many types of studies in biophysics, bioanalysis, the physical-organic chemistry of …
model in many types of studies in biophysics, bioanalysis, the physical-organic chemistry of …
Prokaryotic carbonic anhydrases
Carbonic anhydrases catalyze the reversible hydration of CO2 []. Since the discovery of this
zinc (Zn) metalloenzyme in erythrocytes over 65 years ago, carbonic anhydrase has not only …
zinc (Zn) metalloenzyme in erythrocytes over 65 years ago, carbonic anhydrase has not only …
Voltage-gated proton channels and other proton transfer pathways
TE Decoursey - Physiological reviews, 2003 - journals.physiology.org
Proton channels exist in a wide variety of membrane proteins where they transport protons
rapidly and efficiently. Usually the proton pathway is formed mainly by water molecules …
rapidly and efficiently. Usually the proton pathway is formed mainly by water molecules …
The catalytic mechanism of carbonic anhydrase: implications of a rate-limiting protolysis of water
DN Silverman, S Lindskog - Accounts of Chemical Research, 1988 - ACS Publications
C02+ H20^ HC03-+ H+(1) This is a very simple enzymic reactioninvolving only six substrate
atoms and, at least formally, the transfer of an OH™ moiety from H20 to C02. Extensive …
atoms and, at least formally, the transfer of an OH™ moiety from H20 to C02. Extensive …
Human sulfide: quinone oxidoreductase catalyzes the first step in hydrogen sulfide metabolism and produces a sulfane sulfur metabolite
MR Jackson, SL Melideo, MS Jorns - Biochemistry, 2012 - ACS Publications
Sulfide: quinone oxidoreductase (SQOR) is a membrane-bound enzyme that catalyzes the
first step in the mitochondrial metabolism of H2S. Human SQOR is successfully expressed at …
first step in the mitochondrial metabolism of H2S. Human SQOR is successfully expressed at …
Refined structure of human carbonic anhydrase II at 2.0 Å resolution
AE Eriksson, TA Jones, A Liljas - Proteins: Structure, Function …, 1988 - Wiley Online Library
The structure of human erythrocytic carbonic anhydrase II has been refined by constrained
and restrained structure–factor least‐squares refinement at 2.0 Å resolution. The …
and restrained structure–factor least‐squares refinement at 2.0 Å resolution. The …