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Literature summary for 3.4.24.33 extracted from

  • Hagmann, M.
    Peptidyl-Asp metalloendopeptidase (2004), Handbook of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press, 1, 1037-1039.
No PubMed abstract available

Protein Variants

Protein Variants Comment Organism
additional information derepressed mutant of Pseudomonas fragi ATCC 4973 produces 40 times higher proteinase levels Pseudomonas fragi

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline cannot be reactivated by Zn2+ Pseudomonas fragi
Alpha-macroglobulin inhibition at a molar ratio of inhibitor to protease of about 18 to 1 Pseudomonas fragi
EDTA
-
Pseudomonas fragi
EGTA
-
Pseudomonas fragi
additional information not inhibited by PMSF Pseudomonas fragi

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
24440
-
laser-desorption mass spectrometry Pseudomonas fragi
27000
-
SDS-PAGE Pseudomonas fragi

Organism

Organism UniProt Comment Textmining
Pseudomonas fragi
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pseudomonas fragi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Glucagon + H2O
-
Pseudomonas fragi ?
-
?

Subunits

Subunits Comment Organism
monomer
-
Pseudomonas fragi

Synonyms

Synonyms Comment Organism
Endoproteinase Asp-N
-
Pseudomonas fragi
X-Asp metalloendopeptidase
-
Pseudomonas fragi

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 8.5
-
Pseudomonas fragi