EC Number   |
Posttranslational Modification |
Reference |
|---|
   1.1.3.4 | glycoprotein |
- |
-, 389792, 389805, 389827, 712533, 728114, 742213, 743193, 743597, 762774, 762785, 763123 |
| 1.1.3.4 | glycoprotein |
13 putative N-glycosylation sites |
-, 763051 |
| 1.1.3.4 | glycoprotein |
approx. 95% of the carbohydrate moiety is cleaved from the protein by incubation of glucose oxidase with endoglycosidase H and alpha-mannosidase. Cleavage of the carbohydrate moiety effects a 23-30% decrease in the molecular weight and a reduction in the number of isoforms of glucose oxidase. No significant changes were observed in the circular dichroism spectra of the deglyeosylated enzyme. Other properties, such as thermal stability, pH and temperature optima of glucose oxidase activity and substrate specificity are not affected. However, removal of the carbohydrate moiety marginally affect the kinetics of glucose oxidation and stability at low pH. From these results it appears that the carbohydrate chain of glucose oxidase does not contribute significantly to the structure, stability and activity of glucose oxidase |
727055 |
| 1.1.3.4 | glycoprotein |
carbohydrate content between 10.7 and 16.5%, major component: mannose |
389815 |
| 1.1.3.4 | glycoprotein |
eight potential N-glycosylation at N43, N89, N161, N168, N258, N355, N388, and N473 |
762774 |
| 1.1.3.4 | glycoprotein |
GOD-His6 expressed in wild-type strain of Saccharomyces cerevisiae is hyperglycosylated, GOD-His6 expressed in pmr1DELTA strain of Saccharomyces cerevisiae is not hyperglycosylated. The catalytic efficiency and physical properties of pmr1DELTA mutant-derived GOD-His6 are very similar to those of natural GOD |
657249 |
| 1.1.3.4 | glycoprotein |
most of the carbohydrate moieties contain mannose |
743857 |
| 1.1.3.4 | glycoprotein |
N- and O-linked sugar chains, the enzyme contains 15.2% carbohydrates |
389788 |
| 1.1.3.4 | glycoprotein |
native enzyme contains 12% carbohydrate by weight, main component: mannose, the carbohydrate moiety plays a role in increasing the stability of the protein moiety, but does not directly participate in the catalytic activity, in the immunological reactivity, or in maintaining the conformation of the enzyme protein, periodate treatment decreases the carbohydrate content to about 40% of its original value |
389801 |
| 1.1.3.4 | glycoprotein |
no significant differences in catalytic properties of glyco- and aglyco-GOD |
389826 |
