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In the quest for new targets for pathogen eradication: the adenylosuccinate synthetase from the bacterium Helicobacter pylori (CROSBI ID 254323)

Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija

Bubić, Ante ; Mrnjavac, Natalia ; Stuparević, Igor ; Łyczek, Marta ; Wielgus-Kutrowska, Beata ; Bzowska, Agnieszka ; Luić, Marija ; Leščić Ašler, Ivana In the quest for new targets for pathogen eradication: the adenylosuccinate synthetase from the bacterium Helicobacter pylori // Journal of enzyme inhibition and medicinal chemistry, 33 (2018), 1; 1405-1414. doi: 10.1080/14756366.2018.1506773

Podaci o odgovornosti

Bubić, Ante ; Mrnjavac, Natalia ; Stuparević, Igor ; Łyczek, Marta ; Wielgus-Kutrowska, Beata ; Bzowska, Agnieszka ; Luić, Marija ; Leščić Ašler, Ivana

engleski

In the quest for new targets for pathogen eradication: the adenylosuccinate synthetase from the bacterium Helicobacter pylori

Adenylosuccinate synthetase (AdSS) is an enzyme at regulatory point of purine metabolism. In pathogenic organisms which utilise only the purine salvage pathway, AdSS asserts itself as a promising drug target. One of these organisms is Helicobacter pylori, a wide-spread human pathogen involved in the development of many diseases. The rate of H. pylori antibiotic resistance is on the increase, making the quest for new drugs against this pathogen more important than ever. In this context, we describe here the properties of H. pylori AdSS. This enzyme exists in a dimeric active form independently of the presence of its ligands. Its narrow stability range and pH-neutral optimal working conditions reflect the bacterium’s high level of adaptation to its living environment. Efficient inhibition of H. pylori AdSS with hadacidin and adenylosuccinate gives hope of finding novel drugs that aim at eradicating this dangerous pathogen.

Helicobacter pylori ; adenylosuccinate synthetase ; enzyme kinetics ; enzyme inhibition ; oligomeric state ; analytical ultracentrifugation

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Podaci o izdanju

33 (1)

2018.

1405-1414

objavljeno

1475-6366

1475-6374

10.1080/14756366.2018.1506773

Trošak objave rada u otvorenom pristupu

Povezanost rada

Biologija, Interdisciplinarne prirodne znanosti, Kemija

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