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- Title
Molecular and biochemical characterization of Eimeria tenella hexokinase.
- Authors
Sun, Mingfei; Liao, Shenquan; Zhang, Longxian; Wu, Caiyan; Qi, Nanshan; Lv, Minna; Li, Juan; Lin, Xuhui; Zhang, Jianfei; Xie, Mingquan; Zhu, Guan; Cai, Jianping
- Abstract
Hexokinase (HK) is one of the key enzymes in the glycolytic pathway that catalyzes the phosphorylation of glucose. In the present study, we cloned the HK gene from the coccidian Eimeria tenella ( EtHK), expressed EtHK as a His-tagged fusion protein, and characterized its primary biochemical features. Mutagenesis confirmed that residues S159, N216, and D217 are essential or important to the EtHK catalytic activity. EtHK exhibited high affinity for d-glucose ( Km = 0.67 to 0.79 mM), but was also able to utilize 2-deoxy- d-glucose ( Km = 5.66 mM), d-fructose ( Km = 13.76 mM), and d-mannose ( Km = 25.41 mM). We also observed that quercetin and mangiferin could inhibit the EtHK enzyme activity (IC values = 6.52 and 85.82 μM, respectively). Among the two inhibitors, mangiferin also inhibited the growth of E. tenella in vitro (MIC = 0.12 μM). These observations suggest that EtHK may be explored as potential drug target, and mangiferin and its analogs may be explored for developing anti-coccidial therapeutics.
- Subjects
GLUCOKINASE; EIMERIA tenella; PHOSPHORYLATION; MANGIFERIN; QUERCETIN
- Publication
Parasitology Research, 2016, Vol 115, Issue 9, p3425
- ISSN
0932-0113
- Publication type
Article
- DOI
10.1007/s00436-016-5104-4