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Literature summary for 3.4.24.13 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

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
112000
-
x * 112000, type 1 protease, SDS-PAGE Neisseria gonorrhoeae
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

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

Purification (Commentary)

Purification (Comment) Organism
type 1 enzyme Neisseria gonorrhoeae
type 2 enzyme Neisseria gonorrhoeae

Source Tissue

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

Specific Activity [micromol/min/mg]

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

Storage Stability

Storage Stability Organism
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
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
50 mM, Tris-HCl, pH 7.5, 20% glycerol, stable for at least 2 months Neisseria gonorrhoeae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
immunoglobulin A1 + H2O alpha-chain Neisseria gonorrhoeae oligopeptides derived from immunoglobulin A1
-
?
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
-
?
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

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