3.4.24.56: insulysin
This is an abbreviated version!
For detailed information about insulysin, go to the full flat file.
Word Map on EC 3.4.24.56
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3.4.24.56
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alzheimer
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neprilysin
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abeta
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hippocampus
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dementia
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mellitus
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cerebral
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morris
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amyloid-beta
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metalloprotease
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maze
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neuroprotective
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amyloidogenic
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tau
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beta-amyloid
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neurodegenerative
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presenilin
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endothelin-converting
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senile
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gamma-secretase
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beta-protein
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125i-insulin
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abeta-degrading
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hyperinsulinemia
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metalloendopeptidase
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bacitracin
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beta-secretase
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late-onset
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amylin
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microglia
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medicine
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adam10
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non-amyloidogenic
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glutathione-insulin
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enzyme-1
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b-chains
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analysis
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ad-like
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anti-ide
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exosite
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beta-peptide
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abeta1-40
- 3.4.24.56
- alzheimer
- neprilysin
- abeta
- hippocampus
- dementia
- mellitus
- cerebral
-
morris
- amyloid-beta
- metalloprotease
-
maze
-
neuroprotective
-
amyloidogenic
- tau
- beta-amyloid
- neurodegenerative
-
presenilin
-
endothelin-converting
-
senile
- gamma-secretase
- beta-protein
- 125i-insulin
-
abeta-degrading
- hyperinsulinemia
- metalloendopeptidase
- bacitracin
- beta-secretase
-
late-onset
- amylin
- microglia
- medicine
- adam10
-
non-amyloidogenic
-
glutathione-insulin
- enzyme-1
- b-chains
- analysis
-
ad-like
-
anti-ide
-
exosite
- beta-peptide
- abeta1-40
Reaction
Degradation of insulin, glucagon and other polypeptides. No action on proteins =
Synonyms
ADE, amyloid degrading enzyme, cgd6_5510, EC 3.4.22.11, EC 3.4.99.10, EC 3.4.99.45, gamma-endorphin-generating enzyme, IDE, INS20-19, insulin degrading enzyme, Insulin protease, Insulin proteinase, Insulin-degrading enzyme, Insulin-degrading neutral proteinase, Insulin-glucagon protease, Insulin-specific protease, Insulinase, Insulysin, Metalloinsulinase, More, pitrilysin metallopeptidase 1, Pitrm1
ECTree
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Subunits
Subunits on EC 3.4.24.56 - insulysin
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dimer
monomer
oligomer
additional information
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x * 113000, native enzyme, x * 56000, isolated C-terminal domain IDE-C, 1 * 60000, isolated N-terminal domain IDE-N, SDS-PAGE
dimer
2 * 113000, homodimer or heterodimer of isoforms 15a-IDE and 15b-IDE, SDS-PAGE
monomer
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mutant with a deleted putative dimer interface in the C-terminal region is created, which results in a monomeric variant. Monomeric IDE retains 25% of the wild type activity substrate (Abz-GGFLRKHGQ-EDDnp). With the peptide substrates beta-endorphin and amyloid beta peptide, monomeric IDE retains 1 to 0.25% of wild type activity. No activation through bradykinin or dynorphin B-9. Monomeric IDE is not activated by polyphosphates
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monomeric IDE is composed of two domains, N- and C-terminal domain, of about 55000 Da, can occur as tetramer or dimer
oligomer
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monomeric IDE is composed of two domains, N- and C-terminal domain, of about 55000 Da, can occur as tetramer or dimer
oligomer
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monomeric IDE is composed of two domains, N- and C-terminal domain, of about 55000 Da, can occur as tetramer or dimer
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human enzyme partially exists as homodimer or heterodimer
additional information
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enzyme interacts with Varicella zoster virus glycoprotein E through its extracellular domain
additional information
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enzyme may be subdivided into roughly equal sized domains IDE-C and IDE-N by limited proteolysis. Separation and analysis of domains show that IDE-N is a monomer and IDE-C serves to oligomerize IDE-N. IDE-C alone does not have catalytic activity, IDE-N alone has 2% of wild-type activity. By complexing IDE-C with IDE-N, activity can be restored to 30% of wild-type
additional information
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the catalytic domain of IDE is located in the amino subunit, the secondary structure of the IDE binding domain is likely important for its interaction with IDE
additional information
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the enzyme is probably part of a multienzyme complex and co-isolates with the multicatalytic proteinase
additional information
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oligomeric forms of IDE treated with H2O2 and GSN, 280-290 kDa, overview
additional information
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the two domains of the monomer form a crypt to enclose the substrate and prevent entry or escape of the substrates
additional information
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the two domains of the monomer form a crypt to enclose the substrate and prevent entry or escape of the substrates
additional information
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the protease is a complex of rather easily dissociating units, which severly complicates its purification
additional information
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sedimentation analysis shows that enzyme in Tris buffers mainly consists of monomers and dimers, in phosphate buffer there are monomers, dimers and tetramers. Tris buffer supplemented with 4 mM triphosphate contains enzyme as monomer and high oligomers, but without dimers
additional information
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both recombinant and brain enzyme are able to form a stable complex with amyloid beta that resists dissociation after treatment with strong denaturants. Amyloid beta sequence 17-27 is sufficient to form a stable complex with IDE. Monomeric as opposed to aggregated amyloid beta is competent to associate irreversibly with IDE following a very slow kinetics. Partial denaturation of IDE as well as preincubation with a 10fold molar excess of insulin prevent complex formation. Amyloid beta remains bound to a 25 kDa N-terminal fragment of IDE in an SDS-resistant manner
additional information
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the two domains of the monomer form a crypt to enclose the substrate and prevent entry or escape of the substrates