ChemInform Abstract: An Inhibitor-Like Binding Mode of a Carbonic Anhydrase Activator within the Active Site of Isoform II.

ChemInform ◽  
2012 ◽  
Vol 43 (10) ◽  
pp. no-no
Author(s):  
Khyati Dave ◽  
Marc A. Ilies ◽  
Andrea Scozzafava ◽  
Claudia Temperini ◽  
Daniela Vullo ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Active Site ◽  
Binding Mode

Kinetic and docking studies of phenol-based inhibitors of carbonic anhydrase isoforms I, II, IX and XII evidence a new binding mode within the enzyme active site

2011 ◽  
Vol 19 (4) ◽  
pp. 1381-1389 ◽  
Author(s):  
Serdar Durdagi ◽  
Murat Şentürk ◽  
Deniz Ekinci ◽  
Halis Türker Balaydın ◽  
Süleyman Göksu ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Active Site ◽  
Binding Mode ◽  
Docking Studies ◽  
Enzyme Active Site

scholarly journals 2-Mercaptobenzoxazoles: a class of carbonic anhydrase inhibitors with a novel binding mode to the enzyme active site

2020 ◽  
Vol 56 (59) ◽  
pp. 8297-8300
Author(s):  
Murat Bozdag ◽  
Claudiu T. Supuran ◽  
Davide Esposito ◽  
Andrea Angeli ◽  
Fabrizio Carta ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Active Site ◽  
Binding Mode ◽  
Lead Compound ◽  
Carbonic Anhydrase Inhibitors ◽  
Enzyme Active Site

2-Mercaptobenzoxazole represents an interesting lead compound alternative to the classical sulfonamides for the development of selective carbonic anhydrase inhibitors.

scholarly journals Catechols: a new class of carbonic anhydrase inhibitors

2020 ◽  
Vol 56 (85) ◽  
pp. 13033-13036 ◽  
Author(s):  
Katia D'Ambrosio ◽  
Simone Carradori ◽  
Stefania Cesa ◽  
Andrea Angeli ◽  
Simona M. Monti ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Water Molecule ◽  
Deep Water ◽  
Active Site ◽  
Bound Water ◽  
Binding Mode ◽  
Carbonic Anhydrase Inhibitors ◽  
New Class

Catechols adopt a peculiar binding mode to the CA active site which involves both the zinc bound water molecule and the “deep water”.

An inhibitor-like binding mode of a carbonic anhydrase activator within the active site of isoform II

2011 ◽  
Vol 21 (9) ◽  
pp. 2764-2768 ◽  
Author(s):  
Khyati Dave ◽  
Marc A. Ilies ◽  
Andrea Scozzafava ◽  
Claudia Temperini ◽  
Daniela Vullo ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Active Site ◽  
Binding Mode

scholarly journals Chromene-Containing Aromatic Sulfonamides with Carbonic Anhydrase Inhibitory Properties

2021 ◽  
Vol 22 (10) ◽  
pp. 5082
Author(s):  
Andrea Angeli ◽  
Victor Kartsev ◽  
Anthi Petrou ◽  
Mariana Pinteala ◽  
Volodymyr Brovarets ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Active Site ◽  
Inhibitory Activity ◽  
Binding Mode ◽  
Carbonic Anhydrases ◽  
Inhibition Activity ◽  
Physiological Conditions ◽  
Computational Procedures ◽  
Living Organisms ◽  
Human Isoforms

Carbonic anhydrases (CAs, EC 4.2.1.1) catalyze the essential reaction of CO2 hydration in all living organisms, being actively involved in the regulation of a plethora of patho/physiological conditions. A series of chromene-based sulfonamides were synthesized and tested as possible CA inhibitors. Their inhibitory activity was assessed against the cytosolic human isoforms hCA I, hCA II and the transmembrane hCA IX and XII. Several of the investigated derivatives showed interesting inhibition activity towards the tumor associate isoforms hCA IX and hCA XII. Furthermore, computational procedures were used to investigate the binding mode of this class of compounds, within the active site of hCA IX.

Recent insights into lytic polysaccharide monooxygenases (LPMOs)

2018 ◽  
Vol 46 (6) ◽  
pp. 1431-1447 ◽  
Author(s):  
Tobias Tandrup ◽  
Kristian E. H. Frandsen ◽  
Katja S. Johansen ◽  
Jean-Guy Berrin ◽  
Leila Lo Leggio
Keyword(s):  
Active Site ◽  
Room Temperature ◽  
Experimental Studies ◽  
Binding Mode ◽  
Structural Features ◽  
Oxygen Species ◽  
Animal Kingdom ◽  
X Ray ◽  
Lytic Polysaccharide Monooxygenases ◽  
Polysaccharide Monooxygenases

Lytic polysaccharide monooxygenases (LPMOs) are copper enzymes discovered within the last 10 years. By degrading recalcitrant substrates oxidatively, these enzymes are major contributors to the recycling of carbon in nature and are being used in the biorefinery industry. Recently, two new families of LPMOs have been defined and structurally characterized, AA14 and AA15, sharing many of previously found structural features. However, unlike most LPMOs to date, AA14 degrades xylan in the context of complex substrates, while AA15 is particularly interesting because they expand the presence of LPMOs from the predominantly microbial to the animal kingdom. The first two neutron crystallography structures have been determined, which, together with high-resolution room temperature X-ray structures, have putatively identified oxygen species at or near the active site of LPMOs. Many recent computational and experimental studies have also investigated the mechanism of action and substrate-binding mode of LPMOs. Perhaps, the most significant recent advance is the increasing structural and biochemical evidence, suggesting that LPMOs follow different mechanistic pathways with different substrates, co-substrates and reductants, by behaving as monooxygenases or peroxygenases with molecular oxygen or hydrogen peroxide as a co-substrate, respectively.

Active-site engineering of carbonic anhydrase and its application to biosensors

2000 ◽  
pp. 221-240 ◽  
Author(s):  
Jennifer A. Hunt ◽  
Charles A. Lesburg ◽  
David W. Christianson ◽  
Richard B. Thompson ◽  
Carol A. Fierke
Keyword(s):  
Carbonic Anhydrase ◽  
Active Site

New hypotheses for the binding mode of 4- and 7-substituted indazoles in the active site of neuronal nitric oxide synthase

2012 ◽  
Vol 20 (17) ◽  
pp. 5296-5304 ◽  
Author(s):  
Elodie Lohou ◽  
Jana Sopkova-de Oliveira Santos ◽  
Pascale Schumann-Bard ◽  
Michel Boulouard ◽  
Silvia Stiebing ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Active Site ◽  
Neuronal Nitric Oxide Synthase ◽  
Binding Mode ◽  
Oxide Synthase
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