IgA specific serine endopeptidase
|IgA-specific serine endopeptidase|
|PDB structures||RCSB PDB PDBe PDBsum|
IgA protease (EC 126.96.36.199, IgA-specific serine endopeptidase, IgA proteinase, IgA-specific proteinase, immunoglobulin A protease, immunoglobulin A proteinase) is an enzyme. This enzyme catalyses the following chemical reaction
- Cleavage of immunoglobulin A molecules at certain Pro- bonds in the hinge region. No small molecule substrates are known
The action of IgA protease allows the above mentioned bacteria to adhere to mucous membranes.
An IgA protease is a highly specific 106kDa enzyme that cleaves amino acid sequences of certain proteins. The natural substrate of IgA proteases is immunoglobulin A, hence its name. The enzyme is in fact capable of cleavage of proteins with the amino acid sequence Cleaves N-X-Z-Pro-Pro/-Y-Pro-C, where the X in the squence preferably is a Proline or Serine; the Y = Threonine, Serine or Alanine; and Z preferably is Arginine or Threonine. Because of the sequence that the enzyme is able to cleave, it is also called IgAse Pro-Pro-Y-Pro. Thus, the IgA protease act by cleaving the proline-rich hinge region of the heavy chain of IgA1. Three major bacteria, Neisseria gonorrhœae (which causes gonorrhea), Streptococcus pneumoniae, and Haemophilus influenzae type B, release the IgA protease which destroys IgA.
- Plaut AG (1983). "The IgA1 proteases of pathogenic bacteria". Annual Review of Microbiology. 37 (1): 603–22. doi:10.1146/annurev.mi.37.100183.003131. PMID 6416146.
- Bachovchin WW, Plaut AG, Flentke GR, Lynch M, Kettner CA (March 1990). "Inhibition of IgA1 proteinases from Neisseria gonorrhoeae and Hemophilus influenzae by peptide prolyl boronic acids". The Journal of Biological Chemistry. 265 (7): 3738–43. PMID 2105953.
- Qiu J, Brackee GP, Plaut AG (March 1996). "Analysis of the specificity of bacterial immunoglobulin A (IgA) proteases by a comparative study of ape serum IgAs as substrates". Infection and Immunity. 64 (3): 933–7. PMC 173859. PMID 8641803.