3.4.24.33: peptidyl-Asp metalloendopeptidase
This is an abbreviated version!
For detailed information about peptidyl-Asp metalloendopeptidase, go to the full flat file.
Word Map on EC 3.4.24.33
Reaction
Cleavage of Xaa-/-Asp, Xaa-/-Glu and Xaa-/-cysteic acid bonds =
Synonyms
Asp-N, Asp-N endoproteinase, AspN, AspN endoproteinase, endoprotease Asp-N, Endoproteinase Asp-N, endoproteinase AspN, Peptidyl-Asp metalloproteinase, Proteinase, peptidyl-Asp metallo-, X-Asp metalloendopeptidase
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3.4.24.33 peptidyl-Asp metalloendopeptidaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.4.24.33 - peptidyl-Asp metalloendopeptidase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
?
Erythrocyte carbonic anhydrase I + H2O
?
-
i.e. EC 4.2.1.1, cleavage at 5 Asp- and 1 Glu-residues
-
-
?
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
-
-
?
recombinant histone H1.3 + H2O
C-terminal fragment N.1 of recombinant histone H1.3 + ?
-
-
-
-
?
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
?
-
-
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
-
-
?
