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Literature summary for 3.4.21.B57 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.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
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)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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

Organism UniProt Comment Textmining
Thermococcus kodakarensis P58502 sequence including singnal peptide (amino acid 1-24) and propeptide (amino acid 25-106)
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Posttranslational Modification

Posttranslational Modification Comment Organism
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)

Purification (Comment) Organism
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Thermococcus kodakarensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide + H2O
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Thermococcus kodakarensis N-succinyl-Ala-Ala-Pro-Phe + 4-nitroaniline
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?

Synonyms

Synonyms Comment Organism
Tk-subtilisin
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Thermococcus kodakarensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
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assay at Thermococcus kodakarensis