Literature summary for 3.4.21.B57 extracted from

Tanaka, S.; Takeuchi, Y.; Matsumura, H.; Koga, Y.; Takano, K.; Kanaya, S.
Crystal structure of Tk-subtilisin folded without propeptide: requirement of propeptide for acceleration of folding (2008), FEBS Lett., 582, 3875-3878.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
sitting-drop vapour-diffusion method at 4°C. The crystal structure of the active site mutant of Tk-subtilisin (S324A-subtilisin), which is refolded in the presence of Ca2+ and absence of Tk-propeptide, is determined at 2.16 A resolution. This structure is the same as that of Tk-subtilisin matured from Pro-Tk-subtilisin	Thermococcus kodakarensis

Protein Variants

Protein Variants	Comment	Organism
S324A	the crystal structure of the active site mutant of Tk-subtilisin (S324A-subtilisin), which is refolded in the presence of Ca2+ and absence of Tk-propeptide, is determined at 2.16 A resolution. This structure is the same as that of Tk-subtilisin matured from Pro-Tk-subtilisin. The counting of amino acids refers to the enzyme protein without the signal peptide (amino acid 1-24) and the propeptide (amino acid 25-106)	Thermococcus kodakarensis

Organism

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

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	Tk-subtilisin is matured from Pro-Tk-subtilisin upon autoprocessing and degradation of Tk-propeptide. Tk-subtilisin does not require Tk-propeptide for folding but requires it for acceleration of folding	Thermococcus kodakarensis

Synonyms

Synonyms	Comment	Organism
Tk-subtilisin	-	Thermococcus kodakarensis

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Release 2023.1 (January 2023)