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Literature summary for 3.4.21.62 extracted from

  • Takeuchi, Y.; Tanaka, S.; Matsumura, H.; Koga, Y.; Takano, K.; Kanaya, S.
    Requirement of a unique Ca(2+)-binding loop for folding of Tk-subtilisin from a hyperthermophilic archaeon (2009), Biochemistry, 48, 10637-10643.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
prosubtilisn, DELTAloop-subtilisin, DELTACa2-Pro-S324A, and DELTACa3-Pro-S324A cloned into pET25b vector and overexpressed in Escherichia coli in inclusion bodies Thermococcus kodakarensis

Protein Variants

Protein Variants Comment Organism
DELTACa2-Pro-S324A does not completely lose the ability to fold into a native structure, probably because binding of the water molecule to the position corresponding to the Ca2 site and movement of the epsilon-amino group of Lys213 to the position corresponding to the Ca3 site compensate at least partly for the destabilization of the structure of the Ca2+-binding loop caused by the removal of the Ca2 or Ca3 site Thermococcus kodakarensis
DELTACa3-Pro-S324A does not completely lose the ability to fold into a native structure, probably because binding of the water molecule to the position corresponding to the Ca2 site and movement of the epsilon-amino group of Lys213 to the position corresponding to the Ca3 site compensate at least partly for the destabilization of the structure of the Ca2+-binding loop caused by the removal of the Ca2 or Ca3 site Thermococcus kodakarensis
DELTAloop-subtilisin the unique insertion sequence of subtilisin (Pro207-Asp226) is removed and Gly206,Ala228, and Glu229 are replaced with Asn, Met, and Asp, respectively. Lacks the Ca2+-binding loop, completely loses the ability to fold into a native structure Thermococcus kodakarensis
S324A Pro-S324A represents the active site mutant of pro-subtilisin, Pro-S324A is used to construct mutant proteins to prevent their autoprocessing and self-degradation Thermococcus kodakarensis

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ Ca2+-binding loop is required for folding of subtilisin but does not seriously contribute to the stabilization of subtilisin in a native structure Thermococcus kodakarensis

Organism

Organism UniProt Comment Textmining
Thermococcus kodakarensis
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-
-

Purification (Commentary)

Purification (Comment) Organism
mutants purified in a urea-denatured form Thermococcus kodakarensis

Synonyms

Synonyms Comment Organism
subtilisin
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Thermococcus kodakarensis