Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search Posttranslational Modification

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 9 of 9
EC Number Posttranslational Modification Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 3.1.22.1glycoprotein - 134280, 134286, 134288, 665045
Display the word mapDisplay the reaction diagram Show all sequences 3.1.22.1glycoprotein Both enzymes alpha and beta contain four predicted N-glycosylation sites, including one site that is found in both proteins and one site found in enzyme beta for which the corresponding site in enzyme alpha does not fit the consensus. The N-glycosylation inhibitor tunicamycin diminishes the activity, but the deglycosylation with peptide N-glycosidase has no effect on protein activity 649749
Display the word mapDisplay the reaction diagram Show all sequences 3.1.22.1glycoprotein glucosamine and neutral sugar residues 134308
Display the word mapDisplay the reaction diagram Show all sequences 3.1.22.1glycoprotein glycosylation is apparently required for maximal enzyme activity 649593
Display the word mapDisplay the reaction diagram Show all sequences 3.1.22.1proteolytic modification enzyme precursor Leukocyte Elastase Inhibitor is cleaved by elastase at its reactive center loop. Cleavage abolishes the antiprotease activity and leads to a conformational modification that exposes an endonuclease active site and a nuclear localization signal. Both endonuclease activity and nuclear translocation are needed to induce cell death 681920
Display the word mapDisplay the reaction diagram Show all sequences 3.1.22.1proteolytic modification epidermal growth factor triggers a cleavage of Leukocyte Elastase Inhibitor precursor into L-DNase II, its subsequent enzymatic activation and nuclear translocation 677615
Display the word mapDisplay the reaction diagram Show all sequences 3.1.22.1proteolytic modification post-translational proteolytic processing (from a 48000 Da protein to a 37000 Da protein) is not an essential step for the activation of DNase. 751444
Display the word mapDisplay the reaction diagram Show all sequences 3.1.22.1proteolytic modification processing of DNase II in vivo is greatly altered in the liver of mice lacking cathepsin L. DNase II is extracellularly secreted from cells overexpressing DNase II and is detected as a pro-form, which is activated under acidic conditions. In transgenic COS1 cells, a band of 45 kDa colocalizeswith ER marker protein Bip and two bands with strong immunoreactivity appear at molecular masses of 30 and 23 kDa in lysosomes 730727
Display the word mapDisplay the reaction diagram Show all sequences 3.1.22.1proteolytic modification protein is synthesized as a precursor with a signal sequence 679773
Results 1 - 9 of 9