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Literature summary extracted from

  • Simpson, D.A.; Hausinger, R.P.; Mulks, M.H.
    Purification, characterization, and comparison of the immunoglobulin A1 proteases of Neisseria gonorrhoeae (1988), J. Bacteriol., 170, 1866-1873.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.13 1,10-phenanthroline
-
 Neisseria gonorrhoeae
3.4.24.13 bathocuproine disulfonic acid
-
 Neisseria gonorrhoeae
3.4.24.13 EDTA
-
 Neisseria gonorrhoeae
3.4.24.13 octyl glucoside
-
 Neisseria gonorrhoeae
3.4.24.13 phenylmethylsulfonyl fluoride inhibition of the type 1 protease, no inhibition of the type 2 protease Neisseria gonorrhoeae
3.4.24.13 Sarcosyl
-
 Neisseria gonorrhoeae
3.4.24.13 SDS
-
 Neisseria gonorrhoeae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.24.13 112000
-
 x * 112000, type 1 protease, SDS-PAGE Neisseria gonorrhoeae
3.4.24.13 114000
-
 x * 114000, the 114000 Da peptide is converted to a still active 109000 Da peptide during isolation, type 2 protease, SDS-PAGE Neisseria gonorrhoeae

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.13 Neisseria gonorrhoeae
-
 type 1 and type 2 enzyme
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.13 type 1 enzyme Neisseria gonorrhoeae
3.4.24.13 type 2 enzyme Neisseria gonorrhoeae

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.24.13 culture medium the enzyme is secreted into the culture medium throughout the exponential growth Neisseria gonorrhoeae
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.24.13 additional information
-
-
 Neisseria gonorrhoeae

Storage Stability

EC Number Storage Stability Organism
3.4.24.13 4°C, 50 mM Tris-acetate, pH 7.5, 20% glycerol, 0.1 mM dithiothreitol, 5 mM EDTA, type 1 protease, less than 10% loss of activity after 2 weeks Neisseria gonorrhoeae
3.4.24.13 4°C, long term storage of the 109000 Da type 2 protease, breakdown yields fragments of 95000 and 15000 Da and loss of activity Neisseria gonorrhoeae
3.4.24.13 50 mM, Tris-HCl, pH 7.5, 20% glycerol, stable for at least 2 months Neisseria gonorrhoeae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.13 immunoglobulin A1 + H2O alpha-chain Neisseria gonorrhoeae oligopeptides derived from immunoglobulin A1
-
 ?
3.4.24.13 immunoglobulin A1 + H2O type 2 enzyme cleaves peptide bond 235-236, type 1 enzyme cleaves bond 237-238 in the alpha chain of IgA Neisseria gonorrhoeae oligopeptides derived from immunoglobulin A1
-
 ?
3.4.24.13 immunoglobulin A1 + H2O the activity level of the type 2 enzyme is 10fold that observed for the type 1 enzyme Neisseria gonorrhoeae oligopeptides derived from immunoglobulin A1
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.24.13 ? x * 112000, type 1 protease, SDS-PAGE Neisseria gonorrhoeae
3.4.24.13 ? x * 114000, the 114000 Da peptide is converted to a still active 109000 Da peptide during isolation, type 2 protease, SDS-PAGE Neisseria gonorrhoeae