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Literature summary 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

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.33 1,10-phenanthroline cannot be reactivated by Zn2+ Pseudomonas fragi
3.4.24.33 Alpha-macroglobulin inhibition at a molar ratio of inhibitor to protease of about 18 to 1 Pseudomonas fragi
3.4.24.33 EDTA
-
 Pseudomonas fragi
3.4.24.33 EGTA
-
 Pseudomonas fragi
3.4.24.33 additional information not inhibited by PMSF Pseudomonas fragi

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.24.33 24440
-
 laser-desorption mass spectrometry Pseudomonas fragi
3.4.24.33 27000
-
 SDS-PAGE Pseudomonas fragi

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.33 Pseudomonas fragi
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.33
-
 Pseudomonas fragi

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
3.4.24.33 monomer
-
 Pseudomonas fragi

Synonyms

EC Number Synonyms Comment Organism
3.4.24.33 Endoproteinase Asp-N
-
 Pseudomonas fragi
3.4.24.33 X-Asp metalloendopeptidase
-
 Pseudomonas fragi

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.24.33 7 8.5
-
 Pseudomonas fragi