EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.21.62 | more |
contains no carbohydrate |
29425 |
| 3.4.21.62 | more |
occurrence of the two variant forms of AtSASP can be due to posttranslational modifications |
732247 |
| 3.4.21.62 | proteolytic modification |
autoproteolytic degradation (autoproteolysis) of the purified recombinant Fe protease |
-, 752524 |
| 3.4.21.62 | proteolytic modification |
expressed as pre-pro-proteins whose prodomains are autocatalytically processed |
717456 |
| 3.4.21.62 | proteolytic modification |
in silico analyses predicts signal and pro-peptides at the N-terminus |
718185 |
| 3.4.21.62 | proteolytic modification |
IvaP undergoes extensive post-translational processing. Following secretion, enzyme IvaP is cleaved at least three times to yield a truncated enzyme with serine hydrolase activity, extracellular maturation requires a series of sequential N- and C-terminal cleavage events congruent with the enzyme's mosaic protein domain structure. IvaP can be partially processed in trans, but intramolecular proteolysis is most likely required to generate the mature enzyme. Unlike many other subtilisin-like enzymes, the IvaP cleavage pattern is consistent with stepwise processing of the N-terminal propeptide, which can temporarily inhibit, and be cleaved by, the purified enzyme. IvaP processing results in the loss of about 139 amino acids (about 15 kDa) from the IvaP N-terminus and about 23 amino acids (about 3 kDa) from the IvaP C-terminus, cleavage pattern overview. These sequencing results are consistent with N-terminal cleavage of the 44-kDa IvaP intermediate to the fully cleaved 38-kDa form. A trypsin-like serine protease can cleave the inactive form of IvaP. IvaP exhibits strain-specific processing, comparisons of strains C6706, Haiti, E7946, and N1696 |
-, 754188 |
| 3.4.21.62 | proteolytic modification |
propeptide is absolutely required to fold into a kinetically trapped conformer. Comparison of folding kinetics and intermediates with intracellular serine proteases |
667590 |
| 3.4.21.62 | proteolytic modification |
prosequence regulates ISP activity through two distinct modes: active site blocking and catalytic triad rearrangement. The full-length proenzyme is inactive until specific proteolytic processing removes the first 18 amino acids that comprise the N-terminal extension, with processing appearing to be performed by ISP itself |
718327 |
| 3.4.21.62 | proteolytic modification |
sites of primary autoproteolysis of the purified recombinant Fe protease are Leu2-Thr3, Gly11-Leu12, Trp143-Ala144, Ala173-Ser174, Ala179-Asn180, and Trp219-Tyr220 (numbered according to the amino acids in the mature protease) |
-, 731172 |
| 3.4.21.62 | proteolytic modification |
sites of primary autoproteolysis of the purified recombinant Fe protease areLeu2-Thr3, Gly11-Leu12, Trp143-Ala144, Ala173-Ser174, Ala179-Asn180, and Trp219-Tyr220 (numbered according to the amino acids in the mature protease) |
-, 731172 |
