8A18

1.63 A resolution hydroquinone inhibited Sporosarcina pasteurii urease

これはPDB形式変換不可エントリーです。

8A18 の概要

• エントリーDOI: 10.2210/pdb8a18/pdb
• 分子名称: Urease subunit gamma, Urease subunit beta, Urease subunit alpha, ... (9 entities in total)
• 機能のキーワード: urease, nickel, enzyme inhibition, hydroquinone, hydrolase
• 由来する生物種: Sporosarcina pasteurii; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 89468.65

構造登録者

Mazzei, L.,Ciurli, S.,Cianci, M. (登録日: 2022-06-01, 公開日: 2023-06-14, 最終更新日: 2024-02-07)

主引用文献

Mazzei, L.,Cianci, M.,Ciurli, S.
Inhibition of Urease by Hydroquinones: A Structural and Kinetic Study.
Chemistry, 28:e202201770-e202201770, 2022

PubMed Abstract: Hydroquinones are a class of organic compounds abundant in nature that result from the full reduction of the corresponding quinones. Quinones are known to efficiently inhibit urease, a Ni -containing enzyme that catalyzes the hydrolysis of urea to yield ammonia and carbonate and acts as a virulence factor of several human pathogens, in addition to decreasing the efficiency of soil organic nitrogen fertilization. Here, we report the molecular characterization of the inhibition of urease from Sporosarcina pasteurii (SPU) and Canavalia ensiformis (jack bean, JBU) by 1,4-hydroquinone (HQ) and its methyl and tert-butyl derivatives. The 1.63-Å resolution X-ray crystal structure of the SPU-HQ complex discloses that HQ covalently binds to the thiol group of αCys322, a key residue located on a mobile protein flap directly involved in the catalytic mechanism. Inhibition kinetic data obtained for the three compounds on JBU reveals the occurrence of an irreversible inactivation process that involves a radical-based autocatalytic mechanism.

PubMed: 35994380
DOI: 10.1002/chem.202201770

実験手法

X-RAY DIFFRACTION (1.63 Å)