EC Number   |
Posttranslational Modification |
Reference |
|---|
    3.1.8.1 | glycoprotein |
- |
665960, 690419, 691849, 695051, 750483 |
| 3.1.8.1 | glycoprotein |
at least 2 N-linked sugar chains, contains sialic acid residues |
646527 |
| 3.1.8.1 | glycoprotein |
contains high-mannose N-glycan chains. Enzymatic deglycosylation does not inhibit antioxidant activity of rPON1A |
652704 |
| 3.1.8.1 | glycoprotein |
the enzyme has up to three sugar chains per molecule, and carbohydrate represents 15.8% of the total weight |
35212 |
| 3.1.8.1 | lipoprotein |
purified enzyme OPH is modified with the fatty acids palmitate and stearate, identification of fatty acids attached to the enzyme. Mature OPH is linked to myristic and oleic fatty acids |
751084 |
| 3.1.8.1 | more |
the deduced rabbit amino acid sequence contains five potential N-glycosylation sites, whereas the human sequence predicts four possible N-glycosylation sites |
646507 |
| 3.1.8.1 | proteolytic modification |
the enzyme precursor contains a 36 amino acid N-terminal signal peptide |
-, 666813 |
| 3.1.8.1 | proteolytic modification |
the N-terminal signal peptide of OPH is cleaved off during biosynthesis and therefore cannot serve as a signal anchor. In silico analysis of the OPH signal peptide predicts the existence of both signal peptidase II (SpaseII) and multiple signal peptidase I (SpaseI) cleavage sites in pre-OPH, with the SpaseII cleavage site predicted with the highest level of confidence |
751084 |
| 3.1.8.1 | proteolytic modification |
the premature enzyme contains a signal peptide that is cleaved off during maturation |
750118 |
