Literature summary for 3.4.21.B57 extracted from

Uehara, R.; Ueda, Y.; You, D.J.; Koga, Y.; Kanaya, S.
Accelerated maturation of Tk-subtilisin by a Leu->Pro mutation at the C-terminus of the propeptide, which reduces the binding of the propeptide to Tk-subtilisin (2013), FEBS J., 280, 994-1006.

Search for more literature for 3.4.21.B57

Crystallization (Commentary)

Crystallization (Comment)	Organism
the crystal structure of the complex between L69P-propeptide and S324A-subtilisin (i.e. a protease activity-defective mutant) reveals that the C-terminal region of L69P-propeptide does not well fit into the substrate binding pockets of Tk-subtilisin (S1-S4 subsites) as a result of a conformational change caused by the mutation	Thermococcus kodakarensis

Protein Variants

Protein Variants	Comment	Organism
additional information	the Leu69Pro mutation in the propeptide accelerates the maturation of Pro-Tk-subtilisin by reducing the binding ability of Tk-propeptide to Tk-subtilisin	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, a subtilisin homologue (Gly70-Gly398) from Thermococcus kodakarensis, is matured from its precursor, Pro-Tk-subtilisin (Tk-subtilisin in a pro form (Gly1-Gly398)), by autoprocessing and degradation of propeptide (Tk-propeptide, a propeptide of Tk-subtilisin (Gly1-Leu69)). The scissile peptide bond between Leu69 and Gly70 of Pro-Tk-subtilisin is first self-cleaved to produce an inactive Tk-propeptide:Tk-subtilisin complex, in which the C-terminal region of Tk-propeptide binds to the active-site cleft of Tk-subtilisin. Tk-propeptide is then dissociated from Tk-subtilisin and degraded by Tk-subtilisin to release active Tk-subtilisin	Thermococcus kodakarensis

Synonyms

Synonyms	Comment	Organism
Tk-subtilisin	-	Thermococcus kodakarensis

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)