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Literature summary for 3.4.24.33 extracted from

  • Ni, W.; Dai, S.; Karger, B.L.; Zhou, Z.S.
    Analysis of isoaspartic acid by selective proteolysis with Asp-N and electron transfer dissociation mass spectrometry (2010), Anal. Chem., 82, 7485-7491.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.33

Application

Application Comment Organism
analysis analysis of isoaspartic acid by selective proteolysis with Asp-N and electron transfer dissociation mass spectrometry, overview. IsoAsp formation and repair is central to the survival and germination of plant seeds. Also once administered into patients and thus exposed to physiological conditions of pH 7 and 37 °C, protein pharmaceuticals, particularly those with long circulation time, may generate significant amount of isoAsp Pseudomonas fragi

Organism

Organism UniProt Comment Textmining
Pseudomonas fragi
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-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Pseudomonas fragi
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information endoprotease Asp-N selectively cleaves aspartyl peptides but not the isoaspartyl counterparts Pseudomonas fragi ?
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 ?

Synonyms

Synonyms Comment Organism
Asp-N
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 Pseudomonas fragi
endoprotease Asp-N
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 Pseudomonas fragi

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Pseudomonas fragi

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Pseudomonas fragi