3.4.24.63: meprin B
This is an abbreviated version!
For detailed information about meprin B, go to the full flat file.
Word Map on EC 3.4.24.63
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3.4.24.63
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alzheimer
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amyloid
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abeta
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gamma-secretase
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beta-amyloid
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plaque
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amyloid-beta
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beta-site
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amyloidogenic
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alpha-secretase
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aspartyl
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cerebral
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presenilins
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senile
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neurodegenerative
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bace-1
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swedish
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sappalpha
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neuropathology
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tau
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neurotoxic
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app-cleaving
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neuroblastoma
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beta-peptide
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ectodomains
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dementia
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protein-cleaving
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medicine
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nicastrin
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drug development
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amyloidogenesis
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tangles
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isostere
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memapsin
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peptidomimetic
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abeta1-40
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appswe
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ad-like
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hydroxyethylene
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neurofibrillary
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adam10
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beta-protein
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ad-associated
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endoproteolytic
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insulin-degrading
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non-amyloidogenic
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betaapp
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neprilysin
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pharmacology
- 3.4.24.63
- alzheimer
-
amyloid
- abeta
- gamma-secretase
- beta-amyloid
- plaque
- amyloid-beta
-
beta-site
-
amyloidogenic
- alpha-secretase
-
aspartyl
- cerebral
-
presenilins
-
senile
- neurodegenerative
- bace-1
-
swedish
-
sappalpha
-
neuropathology
- tau
-
neurotoxic
-
app-cleaving
- neuroblastoma
- beta-peptide
- ectodomains
- dementia
-
protein-cleaving
- medicine
-
nicastrin
- drug development
-
amyloidogenesis
-
tangles
-
isostere
-
memapsin
-
peptidomimetic
- abeta1-40
-
appswe
-
ad-like
-
hydroxyethylene
-
neurofibrillary
- adam10
- beta-protein
-
ad-associated
-
endoproteolytic
-
insulin-degrading
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non-amyloidogenic
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betaapp
- neprilysin
- pharmacology
Reaction
Hydrolysis of proteins, including azocasein, and peptides. Hydrolysis of -His5-/-Leu-, -Leu6-/-Cys-, -Ala14-/-Leu- and -Cys19-/-Gly- bonds in insulin B chain =
Synonyms
beta-secretase, cell surface sheddase, h-meprin beta, MEP1B, mephrin beta, meprin A subunit beta, Meprin b, meprin B metalloprotease, meprin beta, meprin beta metalloproteinase, meprin metalloprotease, meprin metalloproteinase, meprin metalloproteinase beta, meprin-beta, meprinbeta, metalloprotease meprin, metalloprotease meprin B, metalloprotease meprin beta, metalloproteinase meprin beta, Mmepb, More, mouse meprin beta, procollagen proteinase, Rmepb
ECTree
3.4.24.63 meprin BAdvanced search results
results (
results (Inhibitors
Inhibitors on EC 3.4.24.63 - meprin B
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
3-([(1,3-benzodioxol-5-ylsulfonyl)[2-(hydroxyamino)-2-oxoethyl]amino]methyl)benzoic acid
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3-([(3-fluoro-4-methoxybenzyl)[2-(hydroxyamino)-2-oxoethyl]amino]methyl)benzoic acid
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3-([(biphenyl-4-ylsulfonyl)[2-(hydroxyamino)-2-oxoethyl]amino]methyl)benzoic acid
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3-([[(1R)-2-(hydroxyamino)-2-oxo-1-phenylethyl]amino]methyl)benzoic acid
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3-([[(1S)-2-(hydroxyamino)-2-oxo-1-phenylethyl]amino]methyl)benzoic acid
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3-([[(2R)-1-(hydroxyamino)-1-oxo-3-phenylpropan-2-yl]amino]methyl)benzoic acid
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3-([[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]amino]methyl)benzoic acid
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3-([[(2R)-3-carboxy-1-(hydroxyamino)-1-oxopropan-2-yl]amino]methyl)benzoic acid
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3-([[(2R)-4-carboxy-1-(hydroxyamino)-1-oxobutan-2-yl]amino]methyl)benzoic acid
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3-([[(2S)-1-(hydroxyamino)-1-oxo-3-phenylpropan-2-yl]amino]methyl)benzoic acid
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3-([[(2S)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]amino]methyl)benzoic acid
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3-([[(2S)-3-carboxy-1-(hydroxyamino)-1-oxopropan-2-yl]amino]methyl)benzoic acid
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3-([[(2S)-4-carboxy-1-(hydroxyamino)-1-oxobutan-2-yl]amino]methyl)benzoic acid
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3-([[(3-fluoro-4-methoxyphenyl)sulfonyl][2-(hydroxyamino)-2-oxoethyl]amino]methyl)benzoic acid
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3-([[(4-carboxyphenyl)sulfonyl][2-(hydroxyamino)-2-oxoethyl]amino]methyl)benzoic acid
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3-([[(4-fluorophenyl)sulfonyl][2-(hydroxyamino)-2-oxoethyl]amino]methyl)benzoic acid
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3-([[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]methyl)benzenecarboperoxoic acid
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3-([[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]methyl)benzoic acid
not only a potent inhibitor of meprin beta, but also a very potent inhibitor of MMP2, 9 and 13
3-[(3-carboperoxybenzyl)[2-(hydroxyamino)-2-oxoethyl]sulfamoyl]benzoic acid
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3-[(3-carboxybenzyl)[2-(hydroxyamino)-2-oxoethyl]sulfamoyl]benzoic acid
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3-[(E)-[4-formyl-5-hydroxy-6-methyl-3-[(phosphonooxy)methyl]pyridin-2-yl]diazenyl]-7-nitronaphthalene-1,5-disulfonic acid
competitive inhibition, binding occurs in meprin beta active site
3-[([2-(hydroxyamino)-2-oxoethyl][[4-(trifluoromethoxy)phenyl]sulfonyl]amino)methyl]benzoic acid
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3-[[(2,6-difluoro-4-methoxyphenyl)methyl-[2-(hydroxyamino)-2-oxoethyl]amino]methyl]benzoic acid
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3-[[(3-carboxyphenyl)sulfonyl-[2-(hydroxyamino)-2-oxo-ethyl]amino]methyl]benzoic acid
hyperbolic noncompetitive/mixed-type inhibition; mixed type inhibition
3-[[(4-carboxyphenyl)methyl-[2-(hydroxyamino)-2-oxoethyl]amino]methyl]benzoic acid
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3-[[(4-chlorophenyl)methyl-[2-(hydroxyamino)-2-oxoethyl]amino]methyl]benzoic acid
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3-[[(4-cyanophenyl)methyl-[2-(hydroxyamino)-2-oxoethyl]amino]methyl]benzoic acid
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3-[[(4-fluorophenyl)methyl-[2-(hydroxyamino)-2-oxoethyl]amino]methyl]benzoic acid
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3-[[1,3-benzodioxol-5-ylmethyl-[2-(hydroxyamino)-2-oxoethyl]amino]methyl]benzoic Acid
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3-[[[2-(hydroxyamino)-2-oxo-ethyl]-(4-methoxyphenyl)sulfonylamino]methyl]benzoic acid
hyperbolic noncompetitive/mixed-type inhibition; mixed type inhibition
3-[[[2-(hydroxyamino)-2-oxo-ethyl]-[(4-biphenyl)methyl]amino]methyl]benzoic acid
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3-[[[2-(hydroxyamino)-2-oxo-ethyl]-[(4-propoxyphenyl)methyl]amino]methyl]benzoic acid
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3-[[[2-(hydroxyamino)-2-oxoethyl]-(p-tolylmethyl)amino]methyl]benzoic acid
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3-[[[2-(hydroxyamino)-2-oxoethyl]-[(3-methoxyphenyl)methyl]amino]methyl]benzoic acid
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3-[[[2-(hydroxyamino)-2-oxoethyl]-[(4-methoxyphenyl)methyl]-amino]methyl]benzoic acid
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3-[[[3-(hydroxyamino)-3-oxopropyl]-[(4-methoxyphenyl)-methyl]amino]methyl]benzoic acid
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3-[[[4-(hydroxyamino)-4-oxobutyl]-[(4-methoxyphenyl)methyl]amino]methyl]benzoic acid
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4-([[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]methyl)benzoic acid
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diethyl 3,3'-([[2-(hydroxyamino)-2-oxoethyl]imino]dimethanediyl)dibenzoate
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N-hydroxy-N2-(4-methoxybenzyl)-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
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N-[1-[(1-amino-1-oxopropan-2-yl)amino]-3-(naphthalen-1-yl)-1-oxopropan-2-yl]-4-(hydroxyamino)-2-(2-methylpropyl)pent-4-enamide
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N-[2-(hydroxyamino)-2-oxoethyl]-N-[(4-methoxyphenyl)sulfonyl]-beta-alanine
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N-[4-(hydroxyamino)-2-(2-methylpropyl)pent-4-enoyl]-3-methylvalyl-N-(2-aminoethyl)-DL-alaninamide
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N2-(2,3-dihydro-1,4-benzodioxin-6-ylmethyl)-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
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N2-(bicyclo[2.2.1]hept-2-ylmethyl)-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
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N4-hydroxy-N1-[3-(1H-indol-3-yl)-1-(methylamino)-1-oxopropan-2-yl]-2-(2-methylpropyl)butanediamide
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NF 449
4,4',4'',4'''-[carbonyl- bis[imino-5,1,3-benzenetriyl-bis-(carbonylimino)]]tetrakis-(benzene-1,3-disulfonic acid)
[[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]acetic acid
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actinonin
a hydroxamate derivate and naturally occurring compound produced in actinomycetes. Hydroxamate inhibitors chelate the zinc ion in the active site
actinonin
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in vivo inhibition of meprins by actinonin exacerbates some parameters of renal injury in mice afflicted with anti-glomerular basement membrane antibody-associated nephritis
actinonin
a hydroxamate derivate and naturally occurring compound produced in actinomycetes. Hydroxamate inhibitors chelate the zinc ion in the active site
Ca2+
calcium negatively regulates meprin beta activity and attenuates substrate cleavage
NF449
Nf449 is a suramin analogue, mixed competitive/noncompetitive inhibition, binding occurs in meprin beta active site
Pro-Leu-Gly-hydroxamate
binding structure in S subsites, overview. A decrease in solvent accessibility values at specific residues upon inhibitor binding occurs. The S subsite of the enzyme interacts with residues at P site of the inhibitor
additional information
binding sites and binding structure of hydroxamic acid derivative inhibitors, molecular dynamics simulation study, overview
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additional information
structure-activity relationships of selective meprin beta inhibitors, synthesis and inhibitory potency, overview. Preference of meprin beta for acidic residues in the P1' position. Acidic modifications induce potent inhibition and over 100fold selectivity over other structurally related metalloproteases such as MMP-2 or ADAM10
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additional information
alterations of the amino acid composition close to the beta-secretase cleavage site may inhibit meprin beta activity on the generation of N-terminal truncated Abeta peptides
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additional information
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alterations of the amino acid composition close to the beta-secretase cleavage site may inhibit meprin beta activity on the generation of N-terminal truncated Abeta peptides
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additional information
analysis of binding sites of human meprins, screening of inhibitors by molecular dynamics simulation study, molecular docking, overview
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additional information
structure-guided design, synthesis, and characterization of next-generation meprin beta inhibitors, overview. Molecular docking of compounds 6a, 8a, and 8i, to meprin beta using the crystal structure, PDB ID 4GWN, with manual replacement of Cd2+ by Zn2+. Cell viability assay is assessed in human hepatocellular carcinoma cell line Hep-G2 and in human neuroblastoma cell line SH-SY5Y
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additional information
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compound E-64; phosphoramidon, iodoacetic acid, 3,4-dichloroisocoumarin or soybean trypsin inhibitor
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additional information
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no inhibition by captopril, PMSF, pepstatin; phosphoramidon, iodoacetic acid, 3,4-dichloroisocoumarin or soybean trypsin inhibitor
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additional information
alterations of the amino acid composition close to the beta-secretase cleavage site may inhibit meprin beta activity on the generation of N-terminal truncated Abeta peptides
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