Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
alpha-tubulin + H2O
?
-
specific for preaspartate cleavage
-
-
?
antithrombin + H2O
?
-
the Asp342 localized in helix I is the AspN cleavage site, found in both heating-induced and citrullination-induced polymers of antithrombin
-
-
?
Apolipoprotein A-I + H2O
Peptides
-
2 CNBr-fragments, cleavage at 12 Asp-residues and 5 out of 18 Glu-residues, cleaves N-terminal to Glu as well as to Asp and cysteic acid
amino acid sequences
?
Azocoll + H2O
?
-
-
-
-
?
Erythrocyte carbonic anhydrase I + H2O
?
-
i.e. EC 4.2.1.1, cleavage at 5 Asp- and 1 Glu-residues
-
-
?
Hemoglobin + H2O
?
-
-
-
-
?
Human erythrocyte D-aspartyl-L-isoaspartyl methyltransferase isozyme I + H2O
?
-
i.e. EC 2.1.1.77, cleavage sites: N-terminal side of Asp and 5 out of 9 Glu-residues
-
-
?
Insulin A-chain + H2O
?
-
-
-
-
?
Pancreatic ribonuclease + H2O
Peptides
peroxiredoxin II + H2O
?
-
-
-
-
?
recombinant histone H1.3 + H2O
C-terminal fragment N.1 of recombinant histone H1.3 + ?
-
-
-
-
?
Sperm whale myoglobin + H2O
?
substrate alpha-parvalbumin + H2O
?
-
-
-
-
?
additional information
?
-
casein + H2O
?
-
-
-
-
?
casein + H2O
?
-
resorufin-labeled casein
-
-
?
casein + H2O
?
-
specific for preaspartate cleavage
-
-
?
Glucagon + H2O
?
-
-
-
-
?
Glucagon + H2O
?
-
specific for preaspartate cleavage
-
-
?
Insulin B-chain + H2O
?
-
specific for preaspartate cleavage
-
-
?
Insulin B-chain + H2O
?
-
oxidized with performic acid
-
-
?
Insulin B-chain + H2O
?
-
cleavage sites: Leu6-Cys7, Leu15-Tyr16, Val18-Cys19, Phe24-Phe25
-
-
?
Insulin B-chain + H2O
?
-
also cleaves bonds with cysteic acid in P1' derived from cysteine residues by oxidation with performic acid and at N-terminal side of some glutamyl residues
-
-
?
Myoglobin + H2O
?
-
AspN and 0.5 microg/microl myoglobin at an enzyme to substrate ratio of 1:70 w/w
-
-
?
Myoglobin + H2O
?
-
AspN and 0.5 microg/microl myoglobin at an enzyme to substrate ratio of 1:70 w/w
-
-
?
Pancreatic ribonuclease + H2O
Peptides
-
oxidized with performic acid, cleavage sites: -Xaa-Asp- and -Xaa-Cys- (not Cys40, Cys84 or Glu-residues)
i.e. peptide(1-13), peptide(14-25), peptide(26-37), peptide(38-52), peptide(53-57), peptide(53-64), peptide(65-71), peptide(72-82), peptide(83-94), peptide(110-120), peptide(121-124)
?
Pancreatic ribonuclease + H2O
Peptides
-
oxidized with performic acid, cleavage sites: -Xaa-Asp- and -Xaa-Cys- (not Cys40, Cys84 or Glu-residues)
i.e. peptide(1-13), peptide(14-25), peptide(26-37), peptide(38-52), peptide(53-57), peptide(53-64), peptide(65-71), peptide(72-82), peptide(83-94), peptide(110-120), peptide(121-124)
?
Sperm whale myoglobin + H2O
?
-
in the presence of 2 M urea cleavage of 4 out of 6 Asp-residues
-
-
?
Sperm whale myoglobin + H2O
?
-
in the presence of 2 M urea cleavage of 4 out of 6 Asp-residues
-
-
?
additional information
?
-
-
cleavage specificity
-
-
?
additional information
?
-
-
cleavage specificity
-
-
?
additional information
?
-
-
the wild-type protease has no well-delineated specificity, some preference for N-terminal side of hydrophilic residues, e.g. aminoethylcysteine, Ser, Thr, Gln and Gly
-
-
?
additional information
?
-
-
endoprotease Asp-N selectively cleaves aspartyl peptides but not the isoaspartyl counterparts
-
-
?
additional information
?
-
-
high substrate specificity of AspN, that ensures that all of the non-N-terminal peptides having aspartic acid or glutamic acid at their N-termini can be converted. An artificially targeted N-blocked protein is digested with AspN, method overview. The proposed method is applicable to proteins, whether N blocked or N free
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
molecular biology
-
many eukaryotic proteins are blocked at the alpha-amino group of their N-terminal with various modifications, thereby making it difficult to determine their N-terminal sequence by protein sequencer, development of a method for selectively isolating the blocked N-terminal peptide from the peptide mixture generated by endoproteinase AspN digestion of N-blocked protein by removal of all peptides other than the N-terminal one (non-N-terminal peptides) through their carbonyl group introduced by a chemical transamination reaction
additional information
-
AspN is shown to be an alternative protease for in-capillary digestion (during capillary electrophoresis), AspN behaves very similarly to trypsin
additional information
-
AspN is shown to be an alternative protease for in-capillary digestion (during capillary electrophoresis), AspN behaves very similarly to trypsin
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ingrosso, D.; Fowler, A.V.; Bleibaum, J.; Clarke, S.
Specificity of endoproteinase Asp-N (Pseudomonas fragi): cleavage at glutamyl residues in two proteins
Biochem. Biophys. Res. Commun.
162
1528-1534
1989
Pseudomonas fragi
brenda
Noreau, J.; Drapeau, G.R.
Isolation and properties of the protease from the wild-type and mutant strains of Pseudomonas fragi
J. Bacteriol.
140
911-916
1979
Pseudomonas fragi
brenda
Drapeau, G.R.
Substrate specificity of a proteolytic enzyme isolated from a mutant of Pseudomonas fragi
J. Biol. Chem.
255
839-840
1980
Pseudomonas fragi, Pseudomonas fragi Me1
brenda
Gagmann, M.L.; Geuss, U.; Fischer, S.; Kresse, G.B.
Peptidyl-Asp metalloendopeptidase
Methods Enzymol.
248
782-787
1995
Pseudomonas fragi
brenda
Tetaz, T.; Morrison, J.R.; Andreou, J.; Fidge, N.H.
Relaxed specificity of endoproteinase Asp-N: this enzyme cleaves at peptide bonds N-terminal to glutamate as well as aspartate and cysteic acid residues
Biochem. Int.
22
561-566
1990
Pseudomonas fragi
brenda
Hagmann, M.
Peptidyl-Asp metalloendopeptidase
Handbook of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
1037-1039
2004
Pseudomonas fragi
-
brenda
Nesbitt, C.A.; Yeung, K.K.
In-capillary enrichment, proteolysis and separation using capillary electrophoresis with discontinuous buffers: application on proteins with moderately acidic and basic isoelectric points
Analyst
134
65-71
2009
Pseudomonas fragi, Pseudomonas fragi mutant
brenda
Permyakov, S.E.; Karnoup, A.S.; Bakunts, A.G.; Permyakov, E.A.
Sequence microheterogeneity of parvalbumin pI 5.0 of pike: a mass spectrometric study
Biochim. Biophys. Acta
1794
129-136
2009
Pseudomonas fragi
brenda
Ordonez, A.; Martinez-Martinez, I.; Corrales, F.J.; Miqueo, C.; Minano, A.; Vicente, V.; Corral, J.
Effect of citrullination on the function and conformation of antithrombin
FEBS J.
276
6763-6772
2009
Pseudomonas fragi
brenda
Seo, J.H.; Lim, J.C.; Lee, D.Y.; Kim, K.S.; Piszczek, G.; Nam, H.W.; Kim, Y.S.; Ahn, T.; Yun, C.H.; Kim, K.; Chock, P.B.; Chae, H.Z.
Novel protective mechanism against irreversible hyperoxidation of peroxiredoxin: Nalpha-terminal acetylation of human peroxiredoxin II
J. Biol. Chem.
284
13455-13465
2009
Pseudomonas fragi
brenda
Soslau, G.; Prest, P.J.; Class, R.; Jost, M.; Mathews, L.
Inhibition of gamma-thrombin-induced human platelet aggregation by histone H1 subtypes and H1.3 fragments
Platelets
20
349-356
2009
Vibrio proteolyticus
brenda
Sonomura, K.; Kuyama, H.; Matsuo, E.; Tsunasawa, S.; Futaki, S.; Nishimura, O.
Selective isolation of N-blocked peptide by combining AspN digestion, transamination, and tosylhydrazine glass treatment
Anal. Biochem.
410
214-223
2011
Pseudomonas fragi
brenda
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
Anal. Chem.
82
7485-7491
2010
Pseudomonas fragi
brenda