Literature summary for 3.4.21.62 extracted from

Gamble, M.; Kuenze, G.; Dodson, E.J.; Wilson, K.S.; Jones, D.D.
Regulation of an intracellular subtilisin protease activity by a short propeptide sequence through an original combined dual mechanism (2011), Proc. Natl. Acad. Sci. USA, 108, 3536-3541.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of the processed protein is determined at 2.6 A resolution and compared with that of the full-length protein, in which the N-terminal extension binds back over the active site. A conserved proline introduces a backbone kink that shifts the scissile bond beyond reach of the catalytic serine and in addition the catalytic triad is disrupted. In the processed form, access to the active site is unblocked by removal of the N-terminal extension and the catalytic triad rearranges to a functional conformation	Alkalihalobacillus clausii

Crystallization (Comment)

Organism

structure of the processed protein is determined at 2.6 A resolution and compared with that of the full-length protein, in which the N-terminal extension binds back over the active site. A conserved proline introduces a backbone kink that shifts the scissile bond beyond reach of the catalytic serine and in addition the catalytic triad is disrupted. In the processed form, access to the active site is unblocked by removal of the N-terminal extension and the catalytic triad rearranges to a functional conformation

Alkalihalobacillus clausii

Inhibitors

Inhibitors	Comment	Organism	Structure
N1-18[ISP]	synthetic peptide corresponding to the N-terminal extension behaves as a mixed noncompetitive inhibitor of active ISP	Alkalihalobacillus clausii

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
31550	-	mass spectroscopy, processed form	Alkalihalobacillus clausii

Organism

Organism	UniProt	Comment	Textmining
Alkalihalobacillus clausii	D0AB41	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	prosequence regulates ISP activity through two distinct modes: active site blocking and catalytic triad rearrangement. The full-length proenzyme is inactive until specific proteolytic processing removes the first 18 amino acids that comprise the N-terminal extension, with processing appearing to be performed by ISP itself	Alkalihalobacillus clausii

Synonyms

Synonyms	Comment	Organism
intracellular subtilisin protease	-	Alkalihalobacillus clausii
ISP	-	Alkalihalobacillus clausii

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.001	-	N1-18[ISP]	synthetic peptide corresponding to the N-terminal extension behaves as a mixed noncompetitive inhibitor of active ISP, pH and temperature not specified in the publication	Alkalihalobacillus clausii