EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.21.B57 | proteolytic modification |
autocatalytic processing, pro-Tk-subtilisin from Thermococcus kodakarensis is fully folded, because it does not require the structural rearrangement upon autoprocessing for the formation of the Ca2+-binding Ca1 site due to the presence of the insertion sequence IS1 between the propeptide and subtilisin domains |
731311 |
| 3.4.21.B57 | proteolytic modification |
prepro-Tk-subtilisin (Prepro-TKS), which consists of the signal sequence [Met (-24)-Ala(-1)], propeptide (Gly1-Leu69), and mature domain (Tk-subtilisin, Gly70-Gly398). Tk-subtilisin matures from Pro-Tk-subtilisin upon autoprocessing and degradation of propeptide. The pro-enzyme form contains the insertion sequence, IS1, at the N-terminus of the mature domain which is required not only for hyperstabilization of Pro-Tk-subtilisin but also for its rapid maturation, Most part of IS1 (Gly70-Gly78) is autocatalytically removed when Pro-TKS matures to Tk-subtilisin, structure and mechanism, overview |
731774 |
| 3.4.21.B57 | proteolytic modification |
pro-subtilisin is inactive in the absence of Ca2+ but is activated upon autoprocessing and degradation of propeptide in the presence of Ca2+ at 80°C. This maturation process is completed within 30 min at 80°C but is bound at an intermediate stage, in which the propeptide is autoprocessed from the mature domain (mat-subtilisin) but forms an inactive complex with mat-subtilisin*, at lower temperatures. At 80°C, approximately 30% of the pro-subtilisin is autoprocessed into propeptide and mat-subtilisin, and the other 70% is completely degraded to small fragments. mat-Subtilisin is inactive in the absence of Ca2+ but is activated upon incubation with Ca2+ at 80°C |
726708 |
| 3.4.21.B57 | proteolytic modification |
produced from its inactive precursor, Pro-Tk-subtilisin (Gly1-Gly398), by autoprocessing and degradation of the propeptide (Tk-propeptide, Gly1-Leu69). This activation process is extremely slow at moderate temperatures owing to the high stability of Tk-propeptide. The refolding rate of Pro-F17H/S324A and autoprocessing rate of Pro-F17H/S324C are nearly identical to those of their parent proteins (Pro-S324A and Pro-S324C). The activation rate of Pro-F17H greatly increases when compared with that of Pro-Tk-subtilisin, such that Pro-F17H is efficiently activated even at 40°C |
728762 |
| 3.4.21.B57 | proteolytic modification |
the enzyme is autoprocessed from its precursor with N- and C-propeptides |
728144 |
| 3.4.21.B57 | proteolytic modification |
the enzyme matures from the inactive precursor, Pro-Tk-subtilisin (Pro-TKS), upon autoprocessing and degradation of the propeptide (Tkpro) |
726988 |
| 3.4.21.B57 | proteolytic modification |
the enzyme needs to be heat-activated for 1 h at 90°C in activation buffer containing 10 mM HEPES, 1 mM CaCl2, pH 8.0, through autoproteolytical cleavage of its N-terminal pro-region from the 55 kDa inactive proform to the 36 kDa active form. The cleavage site of the proregion appears to be between Gln92 and Ala93 |
732679 |
| 3.4.21.B57 | proteolytic modification |
the N-propeptide is autoprocessed first in the maturation process of Pro-Tk-S359C (an enzyme derivative with the mutation of the active-site serine residue to Cys), although the C-propeptide is subsequently autoprocessed and degraded only in the absence of Ca2+. The C-propeptide is not autoprocessed in the presence of Ca2+, suggesting that Pro-Tk-SP derivative lacking N-propeptide (Val114-Gly640) (ProC-Tk-SP) is not an intermediate form but is the mature form of the enzyme. It is shown that the C-propeptide contributes to the stabilization of ProC-Tk-S359C |
727468 |
| 3.4.21.B57 | proteolytic modification |
the purified pernisine has a proregion that is autocleaved during maturation |
-, 728576 |
| 3.4.21.B57 | proteolytic modification |
Tk-subtilisin (the mature domain of Pro-Tk-subtilisin in active form (Gly70-Gly398)) is matured from Pro-Tk-subtilisin (pro form (Gly1-Gly398)) upon autoprocessing and degradation of propeptide. Extremely slow maturation at mild temperatures. Maturation rate is greatly increased by a single Gly56/Ser mutation in the propeptide region |
688387 |
