3.4.24.13: IgA-specific metalloendopeptidase
This is an abbreviated version!
For detailed information about IgA-specific metalloendopeptidase, go to the full flat file.
Word Map on EC 3.4.24.13
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3.4.24.13
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medicine
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hinge
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gonorrhoeae
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influenzae
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haemophilus
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proteinases
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neisserial
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20-year
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colostrum
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nontypeable
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fcalpha
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hexxh
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meningitidis
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airways
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tetrapeptide
- 3.4.24.13
- medicine
- hinge
- gonorrhoeae
- influenzae
-
haemophilus
- proteinases
-
neisserial
-
20-year
-
colostrum
-
nontypeable
- fcalpha
-
hexxh
- meningitidis
- airways
- tetrapeptide
Reaction
Cleavage of Pro-/-Thr bond in the hinge region of the heavy chain of human IgA =
Synonyms
HP1022, Iga, IgA protease, IgA protease A2, IgA protease B1, IgA1 protease, IgA1 proteinase, IgA1-protease, IgA1-specific proteinase, IgA1P, IgA1pr, igA2, IgaA2, igaB, igaB1, IgaB2, immunoglobulin A1 protease, proteinase, immunoglobulin A1, Streptococcus pneumoniae IgA1 protease, zinc metalloprotease zmpC
ECTree
3.4.24.13 IgA-specific metalloendopeptidaseAdvanced search results
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results (Engineering
Engineering on EC 3.4.24.13 - IgA-specific metalloendopeptidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DELTA1003-1006
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mutant lacking the confirmed self-cleavage recognition site shows only little reduction in secreted protease
DELTA1005-1006
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mutant containing modified consensus recognition sites shows only slight reduction in protease secretion
DELTA974-1002
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mutant lacking the putative self-cleavage recognition site and the intervening residues shows only little reduction in secreted protease
DELTA974-978
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mutant lacking the putative self-cleavage recognition site shows only little reduction in secreted protease
DELTA974-978/DELTA1003-1007
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double deletion mutant lacking both self-cleavage recognition sites shows only a 40% reduced secretion
P1004T/S1005E/S1006A
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mutant containing modified consensus recognition sites shows only slight reduction in protease secretion
P975E/P1004E
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mutant containing modified consensus recognition sites shows 30% lower secreted protease levels than wild-type
S1005E
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mutant containing modified consensus recognition sites shows only slight reduction in protease secretion
S267V
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this mutant fails to undergo self-cleavage and shows no enzymatic activity
DELTA1005-1006
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mutant containing modified consensus recognition sites shows only slight reduction in protease secretion
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P1004T/S1005E/S1006A
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mutant containing modified consensus recognition sites shows only slight reduction in protease secretion
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S1005E
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mutant containing modified consensus recognition sites shows only slight reduction in protease secretion
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S267V
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this mutant fails to undergo self-cleavage and shows no enzymatic activity
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E1605A
E1628A
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site-directed mutagenesis, the IgA1P mutation reduces the proteolytic activity of the enzyme
E1661A
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site-directed mutagenesis, the IgA1P mutation shows proteolytic activity similar to the wild-type
E1695A
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site-directed mutagenesis, the IgA1P mutation shows proteolytic activity similar to the wild-type
E1698A
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site-directed mutagenesis, the IgA1P mutation shows proteolytic activity similar to the wild-type
additional information
E1605A
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site-directed mutagenesis, the IgA1P mutation completely abrogates the proteolytic activity
additional information
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Blastx analysis shows that the igaB gene is homologous to the IgA1 protease genes of Neisseria gonorrhoeae and Neisseria meningitidis. The degree of homology of igaB to neisserial iga genes is greater than the homology of igaB to Haemophilus iga genes
additional information
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mutants that are deficient in iga, igaB, and both genes are constructed in Haemophilus influenzae strain 11P6H. Analysis of these mutants indicates that igaB is the primary mediator of IgA1 protease activity in this strain
additional information
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a mutant in which the entire region spanning the putative (residues 974-978) and the confirmed self-cleavage site (residues 1003-1006) is replaced by a hexahistidine linker fails to produce any detectable secreted protease
additional information
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a mutant in which the entire region spanning the putative (residues 974-978) and the confirmed self-cleavage site (residues 1003-1006) is replaced by a hexahistidine linker fails to produce any detectable secreted protease
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additional information
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disruption of the region between the signal peptidase cleavage site and the LPNTG sorting motif results in a localization defect, premature degradation, and an alteration of the ability of the enzyme to act on a monoclonal human IgA1 substrate
additional information
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an antigenic sequence corresponding to amino acids 420-457 (epiA) of the iga gene product is identified by screening a pneumococcal phage display library with patient's sera. The epiA peptide is conserved in all pneumococci and in two out of three Sreptococcus mitis strains. This epitope is specifically recognized by antibodies present in sera from 90% of healthy adults, thus representing an important target of the humoral response to Streptococcus pneumoniae and Streptococcus mitis infection
additional information
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polymeric IgA and secretory IgA are tested for killing of an IgA1 protease producing strain and a congenic IgA1 protease-negative strain of Streptococcus pneumoniae after a 2 h bacterium-antibody exposure time. Exposure of polymeric IgA and secretory IgA to the protease-producing strain inhibits IgA-mediated killing compared with the results seen with polymeric IgA and secretory IgA exposed to a protease-negative mutant. No difference in killing is observed between the two bacterial strains when polymeric IgA and secretory IgA of subclass IgA2 are used
additional information
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proteolytic preparation of wild-type and mutant N- and C-terminal constructs of the recombinant enzyme: IgA1P154-1963, E1605A-IgA1P, IgA1P154-1611, IgA1P1612-1963, and IgA1P1593-1963 and the combination of IgA1P154-1611 and IgA1P1612-196. The Streptococcus pneumoniae IgA1P activity can be reconstituted in trans by the independently purified N-terminal and C-terminal domains
