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Literature summary for 3.4.21.72 extracted from

  • He, S.; Su, Y.; Lin, Y.; Kuo, H.
    The surface domain of neisserial IgA1 protease plays a role in induction of bacterial adherence to human epithelial cells (2010), Asian Biomed., 4, 231-241.
No PubMed abstract available
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Cloned(Commentary)

Cloned (Comment) Organism
expression of the isolated surface-exposed SD domain in Escherichia coli Neisseria meningitidis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Neisseria meningitidis the enzyme performs autoproteolysis at the SD domain ?
-
 ?

Organism

Organism UniProt Comment Textmining
Neisseria meningitidis Q0PVD3 gene iga
-

Purification (Commentary)

Purification (Comment) Organism
recombinant isolated surface-exposed SD domain from Escherichia coli to homogeneity Neisseria meningitidis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme performs autoproteolysis at the SD domain Neisseria meningitidis ?
-
 ?
surface-exposed SD domain + H2O the enzyme cleaves its own isolated recombinant SD domain, single or linked with the alpha-protein, giving the L1 domain Neisseria meningitidis ?
-
 ?

Subunits

Subunits Comment Organism
More the surface-exposed SD domain, resulting fromn autoproteolysis during autotransportation, of the enzyme is involved in the bacterial adherence to human host epithelial cell surfaces Neisseria meningitidis

Synonyms

Synonyms Comment Organism
IgA1 protease
-
 Neisseria meningitidis

General Information

General Information Comment Organism
physiological function the enzyme performs autoproteolysis at the SD domain, which is important for bacterial adherence to host cells Neisseria meningitidis