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Literature summary extracted from

  • Cassone, M.; Gagne, A.L.; Spruce, L.A.; Seeholzer, S.H.; Sebert, M.E.
    The HtrA protease from Streptococcus pneumoniae digests both denatured proteins and the competence-stimulating peptide (2012), J. Biol. Chem., 287, 38449-38459.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.21.107 expression in Escherichia coli Streptococcus pneumoniae

Protein Variants

EC Number Protein Variants Comment Organism
3.4.21.107 S234A catalytic site variant Streptococcus pneumoniae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.21.107 0.0000247
-
 CSP-1 FRET peptide pH 7.4, 37°C Streptococcus pneumoniae

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.107 Streptococcus pneumoniae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.21.107 beta-casein + H2O
-
 Streptococcus pneumoniae ?
-
 ?
3.4.21.107 competence-stimulating peptide CSP-1 + H2O enzyme HtrA constitutes the primary extracytoplasmic competence-stimulating peptide-degrading activity in cultures of Streptococcus pneumoniae. Both substrate isoforms CSP-1 and CSP-2 interact with HtrA with similar efficiencies Streptococcus pneumoniae ? cleavage predominantly follows residue Phe8 of the CSP-1 isoform of the peptide within its central hydrophobic patch ?
3.4.21.107 competence-stimulating peptide CSP-2 + H2O enzyme HtrA constitutes the primary extracytoplasmic competence-stimulating peptide-degrading activity in cultures of Streptococcus pneumoniae. Both substrate isoforms CSP-1 and CSP-2 interact with HtrA with similar efficiencies Streptococcus pneumoniae ?
-
 ?
3.4.21.107 CSP-1 FRET peptide + H2O reporter peptide with incorporation of a QSY-7 quencher and a Cys(Alexa488) fluorophore at theN-erminus andC-terminus of CSP-1, respectively Streptococcus pneumoniae ?
-
 ?
3.4.21.107 additional information enzyme displays a preference for substrates with non-polar residues at the P1 site Streptococcus pneumoniae ?
-
 ?