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”.

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.

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

scholarly journals Mutagenesis and crystallographic studies of the catalytic residues of the papain family protease bleomycin hydrolase: new insights into active-site structure

2006 ◽  
Vol 401 (2) ◽  
pp. 421-428 ◽  
Author(s):  
Paul A. O'Farrell ◽  
Leemor Joshua-Tor
Keyword(s):  
Water Molecule ◽  
Active Site ◽  
Bound Water ◽  
Active Site Residues ◽  
Site Structure ◽  
Active Site Cysteine ◽  
C Terminus ◽  
Bleomycin Hydrolase ◽  
Active Site Mutants

Bleomycin hydrolase (BH) is a hexameric papain family cysteine protease which is involved in preparing peptides for antigen presentation and has been implicated in tumour cell resistance to bleomycin chemotherapy. Structures of active-site mutants of yeast BH yielded unexpected results. Replacement of the active-site asparagine with alanine, valine or leucine results in the destabilization of the histidine side chain, demonstrating unambiguously the role of the asparagine residue in correctly positioning the histidine for catalysis. Replacement of the histidine with alanine or leucine destabilizes the asparagine position, indicating a delicate arrangement of the active-site residues. In all of the mutants, the C-terminus of the protein, which lies in the active site, protrudes further into the active site. All mutants were compromised in their catalytic activity. The structures also revealed the importance of a tightly bound water molecule which stabilizes a loop near the active site and which is conserved throughout the papain family. It is displaced in a number of the mutants, causing destabilization of this loop and a nearby loop, resulting in a large movement of the active-site cysteine. The results imply that this water molecule plays a key structural role in this family of enzymes.

Out of the active site binding pocket for carbonic anhydrase inhibitors

2015 ◽  
Vol 51 (2) ◽  
pp. 302-305 ◽  
Author(s):  
Katia D'Ambrosio ◽  
Simone Carradori ◽  
Simona M. Monti ◽  
Martina Buonanno ◽  
Daniela Secci ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Active Site ◽  
Binding Pocket ◽  
Carbonic Anhydrase Ii ◽  
Carbonic Anhydrase Inhibitors ◽  
Human Carbonic Anhydrase ◽  
Site Binding

2-Benzylsulfinylbenzoic acid binds to human carbonic anhydrase II in a mode completely different from any other class of carbonic anhydrase inhibitors investigated so far.

Selenols: a new class of carbonic anhydrase inhibitors

2019 ◽  
Vol 55 (5) ◽  
pp. 648-651 ◽  
Author(s):  
Andrea Angeli ◽  
Damiano Tanini ◽  
Alessio Nocentini ◽  
Antonella Capperucci ◽  
Marta Ferraroni ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Inhibitors ◽  
New Class

Aryl selenols effectively inhibit carbonic anhydrase.

Cooperative protein–solvent tuning of proton transfer energetics: carbonic anhydrase as a case study

2020 ◽  
Vol 22 (35) ◽  
pp. 19975-19981
Author(s):  
Laura Zanetti-Polzi ◽  
Massimiliano Aschi ◽  
Isabella Daidone
Keyword(s):  
Carbonic Anhydrase ◽  
Water Molecule ◽  
Proton Transfer ◽  
Active Site ◽  
Point Mutations ◽  
Transfer Energetics

Point mutations induce the active site dehydration and the formation of bridges of only one water molecule that efficiently transfers protons.

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