ملخص
Arginine metabolism mediated by arginases plays a critical role in cell and tissue function. The arginine hydrolysis is deeply
involved in the urea cycle, which helps the kidney excrete ammonia from blood. Upregulation of arginases affects microenvironment
stability due to the presence of excess urea in blood. To regulate the arginase activities properly, a synthetic peptide
based on the structure of human arginase I was designed and assessed. Preliminary data shows it inhibits human arginase
I and II with an IC50
of 2.4 ± 0.3 and 1.8 ± 0.1 mmol, respectively. Our kinetic analysis indicates the inhibition is not competitive
with substrate – suggesting an allosteric mechanism. This result provides a step towards specific inhibitors design.
involved in the urea cycle, which helps the kidney excrete ammonia from blood. Upregulation of arginases affects microenvironment
stability due to the presence of excess urea in blood. To regulate the arginase activities properly, a synthetic peptide
based on the structure of human arginase I was designed and assessed. Preliminary data shows it inhibits human arginase
I and II with an IC50
of 2.4 ± 0.3 and 1.8 ± 0.1 mmol, respectively. Our kinetic analysis indicates the inhibition is not competitive
with substrate – suggesting an allosteric mechanism. This result provides a step towards specific inhibitors design.
| اللغة الأصلية | English |
|---|---|
| الصفحات (من إلى) | 1959–1966 |
| عدد الصفحات | 9 |
| دورية | Molecular Biology Reports |
| حالة النشر | Published - 2021 |