Information on EC 3.4.24.33 - peptidyl-Asp metalloendopeptidase

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The expected taxonomic range for this enzyme is: Gammaproteobacteria

EC NUMBER
COMMENTARY hide
3.4.24.33
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RECOMMENDED NAME
GeneOntology No.
peptidyl-Asp metalloendopeptidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Cleavage of Xaa-/-Asp, Xaa-/-Glu and Xaa-/-cysteic acid bonds
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
55576-49-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain Me1
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Manually annotated by BRENDA team
mutant strain
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-Tubulin + H2O
?
show the reaction diagram
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specific for preaspartate cleavage
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-
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antithrombin + H2O
?
show the reaction diagram
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the Asp342 localized in helix I is the AspN cleavage site, found in both heating-induced and citrullination-induced polymers of antithrombin
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-
?
Apolipoprotein A-I + H2O
Peptides
show the reaction diagram
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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
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Azocoll + H2O
?
show the reaction diagram
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-
-
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casein + H2O
?
show the reaction diagram
Erythrocyte carbonic anhydrase I + H2O
?
show the reaction diagram
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i.e. EC 4.2.1.1, cleavage at 5 Asp- and 1 Glu-residues
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-
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Glucagon + H2O
?
show the reaction diagram
Hemoglobin + H2O
?
show the reaction diagram
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-
-
-
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Human erythrocyte D-aspartyl-L-isoaspartyl methyltransferase isozyme I + H2O
?
show the reaction diagram
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i.e. EC 2.1.1.77, cleavage sites: N-terminal side of Asp and 5 out of 9 Glu-residues
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Insulin A-chain + H2O
?
show the reaction diagram
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Insulin B-chain + H2O
?
show the reaction diagram
Myoglobin + H2O
?
show the reaction diagram
Pancreatic ribonuclease + H2O
Peptides
show the reaction diagram
peroxiredoxin II + H2O
?
show the reaction diagram
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-
-
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?
recombinant histone H1.3 + H2O
C-terminal fragment N.1 of recombinant histone H1.3 + ?
show the reaction diagram
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?
Sperm whale myoglobin + H2O
?
show the reaction diagram
substrate alpha-parvalbumin + H2O
?
show the reaction diagram
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?
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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data obtained from inhibition experiments support metalloproteinase character
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
acetonitrile
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1% v/v, activation at 5-10% v/v
Alpha-macroglobulin
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inhibition at a molar ratio of inhibitor to protease of about 18 to 1
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additional information
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not inhibited by PMSF
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetonitrile
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slight activation at 5-10% v/v, inhibits at 1%
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24440
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laser-desorption mass spectrometry
additional information
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partial amino acid sequences
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Stable in up to 2 M urea, 0.01% w/v SDS or 0.1 M guanidine hydrochloride
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetonitrile
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stable in 5-10% v/v acetonitrile
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, lyophilized in the presence of Tris-HCl buffer, pH 7.5, at least 2 years, 4 mg lyophilizate in 100 ml H2O, 2 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to near homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
proteolytic digestion of alpha-parvalbumin using endoproteinase Asp-N for subsequent examination by MALDI-TOF
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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derepressed mutant of Pseudomonas fragi ATCC 4973 produces 40 times higher proteinase levels
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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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
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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