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Literature summary for 3.4.24.13 extracted from

  • Romanello, V.; Marcacci, M.; Dal Molin, F.; Moschioni, M.; Censini, S.; Covacci, A.; Baritussio, A.G.; Montecucco, C.; Tonello, F.
    Cloning, expression, purification, and characterization of Streptococcus pneumoniae IgA1 protease (2006), Protein Expr. Purif., 45, 142-149.
    View publication on PubMed

Application

Application Comment Organism
medicine enzyme is a major Streptococcus pneumoniae antigen in humans Streptococcus pneumoniae

Cloned(Commentary)

Cloned (Comment) Organism
three segments of enzyme, comprising amino acids 1032-1964, 708-1964, and 104-1964 Streptococcus pneumoniae

Protein Variants

Protein Variants Comment Organism
E1605A of segment 708-1964, completely inactive Streptococcus pneumoniae

General Stability

General Stability Organism
recombinant proteins are highly instable Streptococcus pneumoniae

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface associated via an N-terminal membrane anchor, release upon proteolytic cleavage Streptococcus pneumoniae 9986
-

Organism

Organism UniProt Comment Textmining
Streptococcus pneumoniae Q59947
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant glutathione S-transferase fusion proteins of three segments of enzyme, comprising amino acids 1032-1964, 708-1964, and 104-1964. Segment 1032-1964 is catalytically inactive. Recombinant proteins are highly instable. Streptococcus pneumoniae