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Literature summary for 3.4.21.72 extracted from

  • Vitovski, S.; Sayers, J.R.
    Relaxed cleavage specificity of an immunoglobulin A1 protease from Neisseria meningitidis (2007), Infect. Immun., 75, 2875-2885.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.72

Cloned(Commentary)

Cloned (Comment) Organism
gene iga, DNA and amino acid sequence determination and analysis of NMB IgA1 protease, sequence comparisons, expression of wild-type an dmutant enzymes in Escherichia coli strain XL 1-Blue Neisseria meningitidis

Protein Variants

Protein Variants Comment Organism
additional information construction of deletion or point mutants lacking the previously defined consensus cleavage site, the mutants are still able for self-cleavage and subsequent extracellular release of mature IgA1 protease Neisseria meningitidis
P1004A/S1005T/P1006A site-directed mutagenesis, mutation of the cleavage recognition sequence residues Neisseria meningitidis
P1006X site-directed mutagenesis, mutation of a cleavage recognition sequence residue, the mutant is still able for self-cleavage and subsequent extracellular release of mature IgA1 protease Neisseria meningitidis
S1005E site-directed mutagenesis, mutation of a cleavage recognition sequence residue, the mutant is still able for self-cleavage and subsequent extracellular release of mature IgA1 protease Neisseria meningitidis
S267V site-directed mutagenesis, mutation of the active site catalytic residue, inactive mutant, no self-cleavage and thus no secretion of the enzyme Neisseria meningitidis

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular active mature enzyme, the cleaved and maturated protein is secreted Neisseria meningitidis
-
-
intracellular inactive pro-enzyme, the cleaved and maturated protein is secreted Neisseria meningitidis 5622
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
human immunoglobulin A1 + H2O Neisseria meningitidis bacterial isolates show wide variability in IgA1 protease activity, and those isolated from patients with clinical infection possess the highest levels of activity, overview ?
-
 ?

Organism

Organism UniProt Comment Textmining
Neisseria meningitidis Q51169 iga; gene iga
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification self-cleavage is required for secretion of the mature extracellular enzyme form, cleavage targets contain a proline-rich consensus recognition sequence, Pro-Pro-Ser-Pro, residing in the variable linker region that connects the protease and translocator domains, the precise amino acid sequence of the intervening region, between mature IgA1 protease and the beta-core translocator domain, influences the efficiency of autoproteolytic processing Neisseria meningitidis

Reaction

Reaction Comment Organism Reaction ID
Cleavage of immunoglobulin A molecules at certain Pro-/- bonds in the hinge region. No small molecule substrates are known the catalytic serine residue is Ser267 Neisseria meningitidis
a

Source Tissue

Source Tissue Comment Organism Textmining
additional information bacterial isolates show wide variability in IgA1 protease activity, and those isolated from patients with clinical infection possess the highest levels of activity, overview Neisseria meningitidis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
human immunoglobulin A1 + H2O bacterial isolates show wide variability in IgA1 protease activity, and those isolated from patients with clinical infection possess the highest levels of activity, overview Neisseria meningitidis ?
-
 ?
human immunoglobulin A1 + H2O site-specific proteolytic cleavage Neisseria meningitidis ?
-
 ?
additional information the NMB IgA1 protease shows a broad substrate specificity for human proteins Neisseria meningitidis ?
-
 ?

Subunits

Subunits Comment Organism
More secondary-structure analysis Neisseria meningitidis

Synonyms

Synonyms Comment Organism
IgA1 protease
-
 Neisseria meningitidis
immunoglobulin A1 protease
-
 Neisseria meningitidis
NMB IgA1 protease
-
 Neisseria meningitidis
serine-type IgA1 protease
-
 Neisseria meningitidis
serine-type immunoglobulin A1 protease
-
 Neisseria meningitidis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Neisseria meningitidis