EC Number |
Posttranslational Modification |
Reference |
---|
4.1.1.22 | proteolytic modification |
74000 Da precursor is most probably processed to a carboxy truncated form of 53000-58000 Da |
651162 |
4.1.1.22 | proteolytic modification |
at least three isoforms with molecular masses of 74000 Da, 63000 Da and 53000 Da, the latter two forms derive from the 74000 Da form by carboxyl-terminal truncation, 63000 Da isoform is probably the active form |
653861 |
4.1.1.22 | proteolytic modification |
C-terminal processing of the about 74 kDa full-length protein occurs naturally in vivo, with the production of multiple truncated isoforms. The 74 kDa full-length isoform is deficient in substrate binding, the C-terminally truncated isoforms with molecular masses between 70 kDa and 58 kDa have gradually increasing specific activities |
663937 |
4.1.1.22 | proteolytic modification |
enzyme undergoes processing with a major processed band of 59 kDa being observed in addition to a number of minor bands. Processing to the 59 kDa band is caspase-6 dependent |
726888 |
4.1.1.22 | proteolytic modification |
post-translational cleavage by caspase-9 in a mouse mastocytoma P-815, residues D547-D551 and D517-K527 are important, overview |
-, 680763 |
4.1.1.22 | proteolytic modification |
post-translational processing of 74000 Da HDC is required for activity, carboxyl-terminal processing generates an active 55000 Da isoform and additional isoforms with molecular weights higher than 55000 Da |
652502 |
4.1.1.22 | proteolytic modification |
the 74000 Da precursor form is converted into the mature 53000 Da form |
664842 |
4.1.1.22 | proteolytic modification |
the processing to the active form of mammalian HDC relies on the proteinase activity of caspase 9 and the tandem aspartate residues Asp517-Asp518, Asp550-Asp551 |
748845 |
4.1.1.22 | proteolytic modification |
the protein is processed into major 63, 54 and 58/59 kDa doublet bands. Processing at the HDC SKD 501/502/503 site is likely to be caspase-dependent |
726888 |