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Literature summary for 3.4.21.62 extracted from

  • Lanigan-Gerdes, S.; Dooley, A.N.; Faull, K.F.; Lazazzera, B.A.
    Identification of subtilisin, Epr and Vpr as enzymes that produce CSF, an extracellular signalling peptide of Bacillus subtilis (2007), Mol. Microbiol., 65, 1321-1333.
    View publication on PubMed
Search for more literature for 3.4.21.62

Activating Compound

Activating Compound Comment Organism Structure
dichloroisocoumarin
-
 Bacillus subtilis
additional information sigma-H is required for full expression of the CSF-processing protease Bacillus subtilis

Application

Application Comment Organism
degradation subtilisin releases Phr signalling peptides derived from the C-terminus of their precursor proteins, but does not release Phr peptides derived from an internal portion of its precursor proteins Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
additional information mutant lacking three secreted serine proteases regulated by sigma-H, subtilisin, Epr and Vpr, produce less CSF and has less proCSF-processing activity Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
Phenylmethylsulphonyl fluoride
-
 Bacillus subtilis

Localization

Localization Comment Organism GeneOntology No. Textmining
cell wall
-
 Bacillus subtilis 5618
-

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis
-
-
-
Bacillus subtilis
-
 strains BAL941, BAL1190 and BAL2838
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus licheniformis

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information does not cleave proPhrE Bacillus subtilis ?
-
 ?
proCSF + H2O
-
 Bacillus subtilis CSF
-
 ?
proCSF + H2O
-
 Bacillus licheniformis CSF
-
 ?
proPhrA + H2O
-
 Bacillus subtilis PhrA
-
 ?