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
3.4.24.56 insulysinAdvanced search results
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results (Metals Ions
Metals Ions on EC 3.4.24.56 - insulysin
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ca2+
Mg2+
Mn2+
thiol
Zinc
Zn2+
additional information
Mg2+
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activates at concentration up to 0.05 mM, less active than Mn2+, inhibitory at above 0.05 mM
Mn2+
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zinc and manganese are associated with the enzyme, with approximately 10times more zinc than manganese being present, one or both of these two metals are endogenously associated with this enzyme
Mn2+
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zinc and manganese are associated with the enzyme, with approximately 10times more zinc than manganese being present, one or both of these two metals are endogenously associated with this enzyme
Mn2+
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activates, best at 1 mM, preferred divalent cation for both insulin degradation and ATP hydrolysis
thiol
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the enzyme is a neutral thiol metalloprotease requiring both free thiol and divalent cations for activity
thiol
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the enzyme is a neutral thiol metalloprotease requiring both free thiol and divalent cations for activity
thiol
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the enzyme is a neutral thiol metalloprotease requiring both free thiol and divalent cations for activity
Zinc
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zinc and manganese are associated with the enzyme, with approximately 10times more zinc than manganese being present, one or both of these two metals are endogenously associated with this enzyme
Zinc
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zinc and manganese are associated with the enzyme, with approximately 10times more zinc than manganese being present, one or both of these two metals are endogenously associated with this enzyme
Zn2+
a zinc metalloprotease, the catalytic water that is coordinated by a zinc ion also interacts with a glutamate residue, which serves as the general acid/base catalyst
Zn2+
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the enzyme is a neutral thiol metalloprotease requiring both free thiol and divalent cations for activity
Zn2+
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a zinc-binding protease. The metal center in human IDE is chelated by His108, His112, and Glu189. The more external residues Tyr831, Glu111, Thr220, Gly221, Glu182, and Arg824 are also determined. Among these last residues, mainly Glu182, although not directly involved as metal ligand, plays a fundamental role in influencing metal recognition and binding by zinc proteins
Zn2+
dependent on, zinc metallopeptidase, simulated structures of the Zn2+ metal center, overview
Zn2+
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the enzyme is a neutral thiol metalloprotease requiring both free thiol and divalent cations for activity
Zn2+
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one Zn2+ bound at the active site, with the zinc-binding motif HXXEH
Zn2+
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the enzyme is a neutral thiol metalloprotease requiring both free thiol and divalent cations for activity
additional information
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metalloenzyme, removal of the protein-bound metal(s) results in nearly total and irreversible loss of activity
