Literature summary extracted from
Yuzaki, K.; Sanda, Y.; You, D.J.; Uehara, R.; Koga, Y.; Kanaya, S.
Increase in activation rate of Pro-Tk-subtilisin by a single nonpolar-to-polar amino acid substitution at the hydrophobic core of the propeptide domain (2013), Protein Sci., 22, 1711-1721.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
3.4.21.B57 |
additional information |
destabilization of the hydrophobic core of Tk-propeptide by a nonpolar-to-polar amino acid substitution is an effective way to increase the activation rate of Pro-Tk-subtilisin |
Thermococcus kodakarensis |
|
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
3.4.21.B57 |
the crystal structure of Pro-F17H/S324A is nearly identical to that of Pro-S324A, indicating that the mutation does not affect the structure of Pro-Tk-subtilisin |
Thermococcus kodakarensis |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
3.4.21.B57 |
additional information |
the Pro-Tk-subtilisin derivative with the F17His mutation (Pro-F17H), Tk-propeptide derivative with the same mutation (F17H-propeptide), and two active-site mutants of Pro-F17H (Pro-F17H/S324A and Pro-F17H/S324C) are constructed |
Thermococcus kodakarensis |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.4.21.B57 |
Thermococcus kodakarensis |
P58502 |
sequence including singnal peptide (amino acid 1-24) and propeptide (amino acid 25-106) |
- |
Posttranslational Modification
EC Number |
Posttranslational Modification |
Comment |
Organism |
---|
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 |
Thermococcus kodakarensis |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
3.4.21.B57 |
- |
Thermococcus kodakarensis |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
3.4.21.B57 |
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O |
- |
Thermococcus kodakarensis |
N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
3.4.21.B57 |
Tk-subtilisin |
- |
Thermococcus kodakarensis |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
3.4.21.B57 |
7 |
- |
assay at |
Thermococcus kodakarensis |