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Biochemical and Biophysical Characterization of the Enolase from Helicobacter pylori
المؤلفون المشاركون
Lara-Ramírez, Edgar E.
Rodríguez-Luna, Isabel C.
López-Hidalgo, Marisol
Benítez-Cardoza, Claudia G.
Guo, Xianwu
López-López, María de Jesús
المصدر
العدد
المجلد 2018، العدد 2018 (31 ديسمبر/كانون الأول 2018)، ص ص. 1-12، 12ص.
الناشر
Hindawi Publishing Corporation
تاريخ النشر
2018-12-17
دولة النشر
مصر
عدد الصفحات
12
التخصصات الرئيسية
الملخص EN
Enolase, which catalyses the conversion of 2-phospho-D-glycerate to phosphoenolpyruvate, is an important enzyme in the classic glycolysis pathway in cells.
Enolase is highly conserved in organisms from bacteria to humans, indicating its importance in cells.
Thus, enolase is a good target for developing new drugs.
In the last decade, new functions of this enzyme have been found.
Helicobacter pylori is a common human pathogen that causes gastric diseases and even gastric cancer.
In this study, the sequence of H.
pylori enolase (HpEno) was analysed; the conservation (at least partial) of binding sites for cofactor, plasminogen, and host extracellular RNA, as well as catalytic site, indicates that HpEno should be capable of performing the functions.
Recombinant HpEno was overexpressed and purified from E.
coli.
Compared to the enolases from other species, HpEno had similar characteristics for its secondary structure.
The temperature-induced profiles indicate that HpEno is quite stable to temperature, compared to other homologs.
Regarding the kinetics of the unfolding reaction, we found that the activation enthalpy associated with the thermal unfolding reaction is equivalent to the reported activation enthalpy for yeast enolase, indicating a similar scaffold and kinetic stability.
Although a wide range of experimental conditions were assayed, it was not possible to detect any enzymatic activity of HpEno.
To prove the lack of activity, still a much wider range of experiments should be carried out.
نمط استشهاد جمعية علماء النفس الأمريكية (APA)
López-López, María de Jesús& Rodríguez-Luna, Isabel C.& Lara-Ramírez, Edgar E.& López-Hidalgo, Marisol& Benítez-Cardoza, Claudia G.& Guo, Xianwu. 2018. Biochemical and Biophysical Characterization of the Enolase from Helicobacter pylori. BioMed Research International،Vol. 2018, no. 2018, pp.1-12.
https://search.emarefa.net/detail/BIM-1129858
نمط استشهاد الجمعية الأمريكية للغات الحديثة (MLA)
López-López, María de Jesús…[et al.]. Biochemical and Biophysical Characterization of the Enolase from Helicobacter pylori. BioMed Research International No. 2018 (2018), pp.1-12.
https://search.emarefa.net/detail/BIM-1129858
نمط استشهاد الجمعية الطبية الأمريكية (AMA)
López-López, María de Jesús& Rodríguez-Luna, Isabel C.& Lara-Ramírez, Edgar E.& López-Hidalgo, Marisol& Benítez-Cardoza, Claudia G.& Guo, Xianwu. Biochemical and Biophysical Characterization of the Enolase from Helicobacter pylori. BioMed Research International. 2018. Vol. 2018, no. 2018, pp.1-12.
https://search.emarefa.net/detail/BIM-1129858
نوع البيانات
مقالات
لغة النص
الإنجليزية
الملاحظات
Includes bibliographical references
رقم السجل
BIM-1129858
قاعدة معامل التأثير والاستشهادات المرجعية العربي "ارسيف Arcif"
أضخم قاعدة بيانات عربية للاستشهادات المرجعية للمجلات العلمية المحكمة الصادرة في العالم العربي
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