1.11.1.10	glycoprotein	-	348317, 695425, 696263, 697597, 712791	
1.11.1.10	glycoprotein	chloroperoxidase (CPO) is a glycosidic hemoprotein enzyme	765249	
1.11.1.10	glycoprotein	contains 25% to 30% of carbohydrate	348318	
1.11.1.10	glycoprotein	contains between 13% and 47% carbohydrate	348312	
1.11.1.10	glycoprotein	CPO enzyme contains thirteen sugars, including five N-acetyl D-glucosamines (NAG) and eight mannoses (MAN), which are attached to the protein via the glycosidic bonds. Analysis of the effects of the sugar segments on the structure and activity of CPO through the simulation of the halo structure and the structures without the sugar segment, overview. According to molecular dynamics simulation (MD), seven channels and fifteen cavities are identified in the CPO structure. Two of the channels provide the substrate access to the active site. The MD simulation results reveal that the removal of NAG decreases the number of the cavities from fifteen to eleven. Besides, the removal of NAG is associated with removing the channel providing the substrate access. The number of the cavities decreases from fifteen to fourteen through the removal of MAN, but, channel providing the substrate access to the active site is partly preserved. The MD simulation results indicate that the structures without the sugar units are more compact in comparison with the halo structures. The removal of the sugar segments induces the significant changes in the flexibility of the residues that affect the catalytic activity of the enzyme. As a result, the enzyme activities, such as the oxidation, alkylation, halogenation, and epoxidation cannot occur when the sugar segments of the enzyme are removed	765247	
1.11.1.10	glycoprotein	CPO is a glycosylated enzyme	764828	
1.11.1.10	glycoprotein	heavily glycosylated protein (25–30% carbohydrates, two high-mannose N-glycosylation sites)	671523	
1.11.1.10	glycoprotein	the chloroperoxidase gene encodes three potential glycosylation sites	348323