EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.21.97 | proteolytic modification |
expressed in virus-infected cells as a 709-residue precursor that undergoes two autocatalytic cleavages to generate the mature enzyme form |
95603 |
| 3.4.21.97 | proteolytic modification |
the enzyme contains an internal (I) cleavage site. Blocking this site for cleavage in I- mutant virus shows increased amounts of a fragment produced by cleavage at the nearby cryptic site, suggesting that its replication may bypass the I-site block by using the C site as an alternative cleavage pathway. I-site cleavage destabilizes assemblin and its fragments, whereas C-site cleavage does not |
666188 |
| 3.4.21.97 | proteolytic modification |
the enzyme is cleaved as an enzymatically active 74000 Da precursor that cleaves itself at four sites |
653074 |
| 3.4.21.97 | proteolytic modification |
the proteinase is synthesized as an enzymatiacally active precursor that undergoes several autoproteolytic cleavages. Two of these are common in all herpes group viruses, one occurs toward the carboxyl end of the precursor, i.e. M-site, and the other near the middle at the R-site. The R-site cleavage divides the precusor into assemblin and a nonproteolytic carboxyl half. CMV proteinase undergoes a third autoproteolytic cleavage that divides assemblin into approximately equal-size An and Ac subunits. None of these cleavages is absolutely necessary for enzyme activity |
95607 |
