6ZO0
2.23 A resolution 3,4-dimethylcatechol (3,4-dimethylbenzene-1,2-diol) inhibited Sporosarcina pasteurii urease
This is a non-PDB format compatible entry.
Summary for 6ZO0
| Entry DOI | 10.2210/pdb6zo0/pdb |
| Descriptor | Urease subunit gamma, Urease subunit beta, Urease subunit alpha, ... (8 entities in total) |
| Functional Keywords | urease, nickel, enzyme, inhibitor, metal binding protein |
| Biological source | Sporosarcina pasteurii More |
| Total number of polymer chains | 3 |
| Total formula weight | 88742.22 |
| Authors | Mazzei, L.,Cianci, M.,Musiani, F.,Ciurli, S. (deposition date: 2020-07-07, release date: 2020-12-23, Last modification date: 2024-01-31) |
| Primary citation | Mazzei, L.,Contaldo, U.,Musiani, F.,Cianci, M.,Bagnolini, G.,Roberti, M.,Ciurli, S. Inhibition of Urease, a Ni-Enzyme: The Reactivity of a Key Thiol With Mono- and Di-Substituted Catechols Elucidated by Kinetic, Structural, and Theoretical Studies. Angew.Chem.Int.Ed.Engl., 60:6029-6035, 2021 Cited by PubMed Abstract: The inhibition of urease from Sporosarcina pasteurii (SPU) and Canavalia ensiformis (jack bean, JBU) by a class of six aromatic poly-hydroxylated molecules, namely mono- and dimethyl-substituted catechols, was investigated on the basis of the inhibitory efficiency of the catechol scaffold. The aim was to probe the key step of a mechanism proposed for the inhibition of SPU by catechol, namely the sulfanyl radical attack on the aromatic ring, as well as to obtain critical information on the effect of substituents of the catechol aromatic ring on the inhibition efficacy of its derivatives. The crystal structures of all six SPU-inhibitors complexes, determined at high resolution, as well as kinetic data obtained on JBU and theoretical studies of the reaction mechanism using quantum mechanical calculations, revealed the occurrence of an irreversible inactivation of urease by means of a radical-based autocatalytic multistep mechanism, and indicate that, among all tested catechols, the mono-substituted 3-methyl-catechol is the most efficient inhibitor for urease. PubMed: 33245574DOI: 10.1002/anie.202014706 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.23 Å) |
Structure validation
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