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(7-methoxycoumarin-4-yl)acetyl-YVADAPK-(K-epsilon-DNP)-NH2 + H2O
?
-
-
-
?
(7-methyloxycoumarin-4-yl)acetyl-EDEDED-(K-epsilon-2,4-dinitrophenyl) + H2O
?
-
-
-
?
(7-methyloxycoumarin-4-yl)acetyl-EDEDED-NH2-(2,4-dinitrophenyl) + H2O
?
-
-
-
?
2-aminobenzoyl-MGWMDEIDK(2,4-dinitrophenyl)SG + H2O
2-aminobenzoyl-MGWM + DEIDK(2,4-dinitrophenyl)SG
-
-
-
?
Abz-MGWMDEIDK(Dnp)SG-OH + H2O
Abz-MGWM + DEIDK(Dnp)SG-OH
-
-
-
?
Abz-VKMDAE-EDDnp + H2O
?
wild-type beta-site fluorogenic substrate sequence
-
-
?
Abz-VNLDAE-EDDnp + H2O
?
Swedish mutant beta-site fluorogenic substrate sequence
-
-
?
Abz-YVAEAPK(Dnp)G-OH + H2O
?
alpha-secretase + H2O
?
meprin beta-mediated activation of the alpha-secretase
-
-
?
amyloid precursor protein + H2O
?
amyloid precursor protein + H2O
amyloid beta peptides
meprin beta initially sheds amyloid precursor protein, releasing different amyloid beta species with several cleavage sites identical with or proximal to the known beta-secretase cleavage site
-
-
?
amyloid precursor protein + H2O
amyloid precursor protein N-terminal fragments + amyloid beta protein
amyloid precursor protein APP751 + H2O
amyloid precursor protein N-terminal fragments + amyloid beta protein
recombinant human substrate, coexpressed with the enzyme in HEK-293T cells, or exogenous soluble meprin beta incubated with APP751 stably overexpressing 7WD10 cells, is able to produce amyloid precursor fragment N-APP20
-
-
?
angiotensin II + H2O
?
-
-
-
-
?
antileucoproteinase + H2O
?
a serine protease inhibitor
-
-
?
Boc-CCK8NH2 + H2O
N-tert-butyloxycarbonyl-L-Asp-L-Tyr-L-Met-Gly-L-Trp-L-Met + L-Asp-L-Phe
-
peptide of the gastrointestinal tract
-
?
CCK4 + H2O
?
-
peptide of the gastrointestinal tract
-
?
CCK5 + H2O
?
-
peptide of the gastrointestinal tract
-
?
CCK6 + H2O
?
-
peptide of the gastrointestinal tract
-
?
CCK7 + H2O
?
-
peptide of the gastrointestinal tract
-
?
CCK8 + H2O
?
-
peptide of the gastrointestinal tract
-
?
CCK8NH2 + H2O
L-Asp-L-Tyr-L-Met-Gly-L-Trp-L-Met + L-Asp-L-Phe
-
peptide of the gastrointestinal tract
-
?
cerulein + H2O
?
-
peptide of the gastrointestinal tract
-
?
Cholecystokinin + H2O
?
-
-
-
?
cholecystokinin 8 sulfate + H2O
?
-
-
-
?
collagen I + H2O
?
-
-
-
?
dentin phosphoprotein + H2O
?
-
-
-
?
dentin sialophosphoprotein + H2O
?
-
-
-
?
elafin + H2O
?
a serine protease inhibitor
-
-
?
fibrillar procollagen type I + H2O
fibrillar collagen type I + fibrillar collagen type I propeptide
fibrillar procollagen type III + H2O
fibrillar collagen type III + fibrillar collagen type I propeptide
gastri-releasing peptide-(14-27) + H2O
?
-
peptide of the gastrointestinal tract
-
?
Glucagon + H2O
?
-
peptide of the gastrointestinal tract
-
?
interleukin-1beta precursor + H2O
interleukin-1beta + interleukin-1beta propeptide
proteolytic cleavage to a biologically active form
-
-
?
KKGYVADAP-4-nitroanilide + H2O
KKGYVA + DAP-4-nitroanilide
-
-
-
?
KKGYVADAP-7-amido-4-methylcoumarin + H2O
KKGYVA + DAP-7-amido-4-methylcoumarin
-
-
-
?
laminin V + H2O
?
-
-
-
-
?
lymphoepithelial Kazal-type-related inhibitor + H2O
?
a serine protease inhibitor
-
-
?
miniprocollagen alpha1(I) homotrimers + H2O
?
-
-
-
?
N-Benzoyl-Tyr 4-aminobenzoate + H2O
?
neuropeptide Y + H2O
?
-
peptide of the gastrointestinal tract
-
?
osteopontin + H2O
?
-
peptide of the gastrointestinal tract
-
?
pro-collagen I + H2O
collagen I + collagen I propeptide
Procollagen + H2O
?
-
-
-
?
procollagen I + H2O
collagen I + propeptide of collagen III
protein kinase A + H2O
?
the enzyme cleaves at defined sites, isoform-specific interactions between the catalytic subunit of PKA (PKA C) and meprins, overview
-
-
?
protein kinase A catalytic subunit Calpha + H2O
?
the enzyme cleaves at defined sites, cytosolic-enriched kidney proteins from meprin alphabeta double knockout mice, and purified forms of recombinant mouse PKA Calpha, Cbeta1, and Cbeta2, are incubated with activated forms of either homomeric meprinA, EC 3.4.24.18, or meprin B, product analysis by mass spectrometry, overview. Meprin B cleaves all three PKA C isoforms
-
-
?
protein kinase A catalytic subunit Cbeta1 + H2O
?
the enzyme cleaves at defined sites, cytosolic-enriched kidney proteins from meprin alphabeta double knockout mice, and purified forms of recombinant mouse PKA Calpha, Cbeta1, and Cbeta2, are incubated with activated forms of either homomeric meprinA, EC 3.4.24.18, or meprin B, product overview. Meprin B cleaves all three PKA C isoforms
-
-
?
protein kinase A catalytic subunit Cbeta2 + H2O
?
the enzyme cleaves at defined sites, cytosolic-enriched kidney proteins from meprin alphabeta double knockout mice, and purified forms of recombinant mouse PKA Calpha, Cbeta1, and Cbeta2, are incubated with activated forms of either homomeric meprinA, EC 3.4.24.18, or meprin B, product overview. Meprin B cleaves all three PKA C isoforms
-
-
?
sCCK8NH2 + H2O
L-Asp-L-Tyr(SO3)-L-Met-Gly-L-Trp-L-Met + L-Asp-L-Phe
-
peptide of the gastrointestinal tract
-
?
Secretin + H2O
?
-
peptide of the gastrointestinal tract
-
?
Succinyl-Ala-Ala-Ala 4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
Succinyl-Ala-Ala-Val-Ala 4-nitroanilide + H2O
?
-
-
-
-
?
tenascin-C + H2O
tenascin-C peptide fragments
-
mapping of proteolytic fragments generated by meprinbeta from the chicken tenascin-C and the human recombinant 250 kDa TN-C variant. In chicken tenascin-C, meprinbeta processes all three major splicing variants by removal of 10 kDa N-terminal and 38 kDa C-terminal peptides, leaving a large central part of subunits intact. A similar cleavage pattern exists for large human tenascin-C variant where two N-terminal peptides of 10 and 15 kDa and two C-terminal fragments of 40 and 55 kDa are removed from the intact subunit. N-terminal sequencing reveals the exact amino acid positions of cleavage sites. In both chicken and human tenascin-C N-terminal cleavages occur just before and/or after the heptad repeats involved in subunit oligomerization. In the human protein, an additional cleavage site is identified in the alternative fibronectin type III repeat, and a unique cleavage by meprinbeta is located to the 7th constant fibronectin type III repeat in both chicken and human tenascin-C, cleavage at this site removes the C-terminal domain involved in its anti-adhesive activity
-
-
?
Tyr-Leu-Val-Cys(SO3-)-Gly-Glu-Arg-Gly + H2O
?
-
synthetic octapeptide, derived from insulin B-chain
-
-
?
additional information
?
-
Abz-YVAEAPK(Dnp)G-OH + H2O
?
-
-
-
?
Abz-YVAEAPK(Dnp)G-OH + H2O
?
-
-
-
ir
actin + H2O
?
-
villin and actin bind to the cytoplasmic tail of meprin beta
-
-
?
actin + H2O
?
-
villin and actin bind to the cytoplasmic tail of meprin beta
-
-
?
ADAM10 + H2O
?
i.e. a disintegrin and metalloproteinase 10
-
-
?
ADAM10 + H2O
?
i.e. a disintegrin and metalloproteinase 10, reombinant C-terminally Myc-tagged substrate, recombinant N-terminally Strep-tagged meprin beta cleaves the ADAM10 prodomain at amino acids Gln198/Glu199 and Glu199/Glu200
-
-
?
ADAM10 + H2O
?
i.e. a disintegrin and metalloproteinase 10
-
-
?
ADAM10 + H2O
?
i.e. a disintegrin and metalloproteinase 10
-
-
?
ADAM17 + H2O
?
i.e. a disintegrin and metalloproteinase 17
-
-
?
ADAM17 + H2O
?
i.e. a disintegrin and metalloproteinase 17, reombinant C-terminally Myc-tagged substrate
-
-
?
ADAM17 + H2O
?
i.e. a disintegrin and metalloproteinase 17
-
-
?
ADAM17 + H2O
?
i.e. a disintegrin and metalloproteinase 17
-
-
?
ADAM9 + H2O
?
i.e. a disintegrin and metalloproteinase 9
-
-
?
ADAM9 + H2O
?
i.e. a disintegrin and metalloproteinase 9, reombinant C-terminally Myc-tagged substrate, recombinant N-terminally Strep-tagged meprin beta cleaves the ADAM9 prodomain at amino acids Gly189/Asp190 and Glu191/Glu192
-
-
?
ADAM9 + H2O
?
i.e. a disintegrin and metalloproteinase 9
-
-
?
ADAM9 + H2O
?
i.e. a disintegrin and metalloproteinase 9
-
-
?
alpha-MSH + H2O
?
-
-
-
-
?
alpha-MSH + H2O
?
-
-
-
?
amyloid precursor protein + H2O
?
-
-
-
?
amyloid precursor protein + H2O
?
-
APP Is Processed by meprin beta in Vivo
-
-
?
amyloid precursor protein + H2O
?
meprin beta cleaves amyloid precursor protein at the beta-secretase site, giving rise to amyloidogenic peptides
-
-
?
amyloid precursor protein + H2O
?
recombinant soluble human APP695, cleavage at the beta-secretase site
-
-
?
amyloid precursor protein + H2O
?
APP, cleavage mechanism by meprin beta, overview
-
-
?
amyloid precursor protein + H2O
?
APP, the precursor protein is cleaved by meprin beta in distinct ways, either at the beta-secretase site resulting in increased levels of amyloid beta (Abeta) peptides, or at the N-terminus releasing 11 kDa, and 20 kDa peptide fragments. The N-terminal 11 kDa and 20 kDa peptide fragments represent physiological cleavage products
-
-
?
amyloid precursor protein + H2O
?
APP, cleavage mechanism by meprin beta, overview. Generation of truncated Abeta2-x peptides
-
-
?
amyloid precursor protein + H2O
?
APP, the precursor protein is cleaved by meprin beta in distinct ways, either at the beta-secretase site resulting in increased levels of amyloid beta (Abeta) peptides, or at the N-terminus releasing 11 kDa, and 20 kDa peptide fragments
-
-
?
amyloid precursor protein + H2O
?
-
-
-
-
?
amyloid precursor protein + H2O
?
-
-
-
?
amyloid precursor protein + H2O
?
APP, cleavage mechanism by meprin beta, overview
-
-
?
amyloid precursor protein + H2O
?
metalloprotease meprin beta cleaves amyloid precursor protein (APP) predominantly generating N-terminally truncated Abeta2-x variants
-
-
?
amyloid precursor protein + H2O
?
metalloprotease meprin beta cleaves amyloid precursor protein (APP) predominantly generating N-terminally truncated Abeta2-x variants
-
-
?
amyloid precursor protein + H2O
amyloid precursor protein N-terminal fragments + amyloid beta protein
meprin beta can also process amyloid precursor protein in a manner reminiscent of beta-secretase, identification of cleavage sites of meprin beta in the amyloid beta sequence of the wild-type and Swedish mutant of amyloid precursor protein at positions p1 and p2, thereby generating amyloid beta variants starting at the first or second amino acid residue, mass spectrometry analysis, overview
-
-
?
amyloid precursor protein + H2O
amyloid precursor protein N-terminal fragments + amyloid beta protein
catalytic properties and cleavage sites of meprin beta within different amyloid precursor protein peptides, overview
-
-
?
azocasein + H2O
?
-
poor substrate
-
-
?
azocasein + H2O
?
-
-
-
?
azocasein + H2O
?
-
poor substrate
-
-
?
azocasein + H2O
?
-
mouse enzyme: poor substrate unless activated by trypsin treatment (i.e. latent azocaseinase activity)
-
-
?
azocasein + H2O
?
-
poor substrate
-
-
?
azocasein + H2O
?
-
mouse enzyme: poor substrate unless activated by trypsin treatment (i.e. latent azocaseinase activity)
-
-
?
azocasein + H2O
?
-
poor substrate
-
-
?
bradykinin + H2O
?
-
-
-
-
?
bradykinin + H2O
?
-
-
-
?
Collagen IV + H2O
?
-
-
-
-
?
Collagen IV + H2O
?
-
-
-
?
E-cadherin + H2O
?
an extracellular matrix-related substrate
-
-
?
E-cadherin + H2O
?
an extracellular matrix-related substrate
-
-
?
fibrillar procollagen type I + H2O
fibrillar collagen type I + fibrillar collagen type I propeptide
the enzyme is capable of cleaving off the globular C- and N-terminal prodomains of fibrillar collagen type I and type III. Cleavage sites are at positions YYRA1218-/-1219DDAN and VRDR1227/-1228DLEV for the alpha1(I) chain, and additionally GGGY1108-/-1109DFGY for alpha2(I). For the N-terminal propeptide SYGY166-/-167DEKS (alpha1(I)) and AAQY81-/-82DGKG (alpha2(I)) are identified as meprin cleavage sites
-
-
?
fibrillar procollagen type I + H2O
fibrillar collagen type I + fibrillar collagen type I propeptide
the enzyme is capable of cleaving off the globular C- and N-terminal prodomains of fibrillar collagen type I and type III. Cleavage sites are at positions YYRA1218-/-1219DDAN and VRDR1227/-1228DLEV for the alpha1(I) chain, and additionally GGGY1108-/-1109DFGY for alpha2(I). For the N-terminal propeptide SYGY166-/-167DEKS (alpha1(I)) and AAQY81-/-82DGKG (alpha2(I)) are identified as meprin cleavage sites
-
-
?
fibrillar procollagen type III + H2O
fibrillar collagen type III + fibrillar collagen type I propeptide
the enzyme is capable of cleaving off the globular C- and N-terminal prodomains of fibrillar collagen type I and type III
-
-
?
fibrillar procollagen type III + H2O
fibrillar collagen type III + fibrillar collagen type I propeptide
the enzyme is capable of cleaving off the globular C- and N-terminal prodomains of fibrillar collagen type I and type III
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
an extracellular matrix-related substrate
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
an extracellular matrix-related substrate
-
-
?
gastrin + H2O
?
-
-
-
-
?
gastrin + H2O
?
-
-
-
-
?
gastrin 17 + H2O
?
-
-
-
?
gastrin 17 + H2O
?
-
peptide of the gastrointestinal tract
-
?
Insulin B-chain + H2O
?
-
4 cleavage sites (2 major and 2 minor): His5-Leu6, Leu6-Cys(SO3-)7, Ala14-Leu15, Cys(SO3-)19-Gly20
-
-
?
Insulin B-chain + H2O
?
-
yielding at least 7 product peptides
-
-
?
Insulin B-chain + H2O
?
-
mouse enzyme
-
-
?
interleukin-6 + H2O
?
recombinant human substrate expressed in eukaryotic B9 cell line, inactivation. Human meprin B cleaves 35% and 65% of human interleukin-6 of about 22 kDa to a smaller product of about 21 kDa within 30 min and 2 h, respectively
-
-
?
interleukin-6 + H2O
?
recombinant human substrate expressed in Escherichia coli, inactivation
-
-
?
interleukin-6 + H2O
?
recombinant murine substrate expressed in Escherichia coli, inactivation. Rat meprin B cleaves 65% murine interleukin-6 of about 22 kDa to a smaller product of about 21 kDa within 30 min
-
-
?
MMP1 protein + H2O
?
an extracellular matrix-related substrate
-
-
?
MMP1 protein + H2O
?
an extracellular matrix-related substrate
-
-
?
Muc2 protein + H2O
?
an extracellular matrix-related substrate
-
-
?
Muc2 protein + H2O
?
an extracellular matrix-related substrate
-
-
?
N-Benzoyl-Tyr 4-aminobenzoate + H2O
?
-
rat or human enzyme, cleaves arylamide bond
-
-
?
N-Benzoyl-Tyr 4-aminobenzoate + H2O
?
-
rat or human enzyme, cleaves arylamide bond
-
-
?
nidogen 1 + H2O
?
-
-
-
-
?
nidogen 1 + H2O
?
an extracellular matrix-related substrate
-
-
?
nidogen 1 + H2O
?
an extracellular matrix-related substrate
-
-
?
nidogen-1 + H2O
?
-
-
-
?
nidogen-1 + H2O
?
-
-
-
?
orcokinin + H2O
?
-
peptide of the gastrointestinal tract
-
?
orcokinin + H2O
?
-
-
-
?
osteosarcoma-9 + H2O
?
OS-9, specific degradation by meprin beta
-
-
?
osteosarcoma-9 + H2O
?
OS-9, purified recombinant human osteosarcoma-9 protein, specific degradation by meprin beta
-
-
?
osteosarcoma-9 + H2O
?
OS-9, specific degradation by meprin beta
-
-
?
osteosarcoma-9 + H2O
?
OS-9, purified recombinant human osteosarcoma-9 protein, specific degradation by meprin beta
-
-
?
pro-collagen I + H2O
collagen I + collagen I propeptide
maturation
-
-
?
pro-collagen I + H2O
collagen I + collagen I propeptide
cleavage of the C-terminal pro-domain
-
-
?
procollagen I + H2O
collagen I + propeptide of collagen III
meprin beta removes both the C- and N-propeptides of type I procollagen, subsequently releasing fibril-forming mature collagen molecules. The C-terminal cleavage sites in the proalpha1(I) chain generated by the enzyme is identified as Ala1218/Asp1219, identical to the BMP-1 cleavage site, and also Arg1227/Asp1228, nine residues C-terminal to the BMP-1 cleavage site
-
-
?
procollagen I + H2O
collagen I + propeptide of collagen III
recombinant human substrate, generation of mature collagen molecules that spontaneously assemble into collagen fibrils
-
-
?
Reelin + H2O
?
Reelin is a secreted glycoprotein whose function is regulated by proteolysis
-
-
?
Reelin + H2O
?
cleavage between Ala2688 and Asp2689, the specific cleavage site of Reelin called C-t is located approximately between the sixth and seventh Reelin repeat
-
-
?
tenascin-C + H2O
?
-
specific processing by meprinbeta, cleavage mechanism, overview. Meprinbeta-digested human tenascin-C is not able to interfere with fibronectin-mediated cell spreading, confirming cleavage in the anti-adhesive domain. Meprinbeta processing of human tenascin-C neutralizes its inhibitory effect on fibronectin-mediated cell spreading
-
-
?
tenascin-C + H2O
?
an extracellular matrix-related substrate
-
-
?
tenascin-C + H2O
?
an extracellular matrix-related substrate
-
-
?
villin + H2O
?
-
villin and actin bind to the cytoplasmic tail of meprin beta
-
-
?
villin + H2O
?
-
villin and actin bind to the cytoplasmic tail of meprin beta
-
-
?
additional information
?
-
-
residues of the alpha1 subunit involved in the active site are Asp61 and Arg150, catalytic domain structure, overview
-
-
?
additional information
?
-
residues of the alpha1 subunit involved in the active site are Asp61 and Arg150, catalytic domain structure, overview
-
-
?
additional information
?
-
residues of the alpha1 subunit involved in the active site are Asp61 and Arg150, catalytic domain structure, overview
-
-
?
additional information
?
-
residues of the alpha1 subunit involved in the active site are Asp61 and Arg150, catalytic domain structure, overview
-
-
?
additional information
?
-
-
residues of the alpha2 subunit involved in the active site are Glu80 and Lys122, catalytic domain structure, overview
-
-
?
additional information
?
-
residues of the alpha2 subunit involved in the active site are Glu80 and Lys122, catalytic domain structure, overview
-
-
?
additional information
?
-
residues of the alpha2 subunit involved in the active site are Glu80 and Lys122, catalytic domain structure, overview
-
-
?
additional information
?
-
residues of the alpha2 subunit involved in the active site are Glu80 and Lys122, catalytic domain structure, overview
-
-
?
additional information
?
-
-
the residue of the beta subunit involved in the active site is Lys123, catalytic domain structure, overview
-
-
?
additional information
?
-
the residue of the beta subunit involved in the active site is Lys123, catalytic domain structure, overview
-
-
?
additional information
?
-
the residue of the beta subunit involved in the active site is Lys123, catalytic domain structure, overview
-
-
?
additional information
?
-
the residue of the beta subunit involved in the active site is Lys123, catalytic domain structure, overview
-
-
?
additional information
?
-
-
no substrates are nitrobradykinin
-
-
?
additional information
?
-
-
member of astacin family
-
-
?
additional information
?
-
meprin B may play an important role in activation of the proinflammatory cytokine in various pathophysiological conditions
-
-
?
additional information
?
-
-
whereas the expression of meprinbeta and tenascin-C does not overlap in normal colon tissue, inflamed lesions of the mucosa from patients with Crohn's disease exhibit many meprinbeta-positive leukocytes in regions where tenascin-C is strongly induced. At least under pathological conditions, meprinbeta might attack specific functional sites in tenascin-C that are important for its oligomerization and anti-adhesive activity
-
-
?
additional information
?
-
-
meprin interacts with epithelial Na+ channel (ENaC)
-
-
?
additional information
?
-
enzyme cleavage specificity, overview
-
-
?
additional information
?
-
sheddase mechanism of meprin beta, overview
-
-
?
additional information
?
-
meprin beta preferentially cleaves substrates with acidic amino acids in P1'-position
-
-
?
additional information
?
-
comparison of cleavage sites of BACE-1 (EC 3.4.23.46) and meprin beta on APP wild-type and APPswe isoform. The protective A673T mutation in amyloid precursor protein (APP) results in reduced Abeta levels in patients, also prevents from meprin beta cleavage at position p2. 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
-
-
?
additional information
?
-
-
comparison of cleavage sites of BACE-1 (EC 3.4.23.46) and meprin beta on APP wild-type and APPswe isoform. The protective A673T mutation in amyloid precursor protein (APP) results in reduced Abeta levels in patients, also prevents from meprin beta cleavage at position p2. 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
-
-
?
additional information
?
-
specific N-terminal processing of ADAM9, 10, and 17 by meprin beta and identification of cleavage sites within their prodomains. Direct interaction of meprin beta and ADAM proteases. Meprin beta specifically cleaves ADAM9, 10, and 17 N-terminal of the furin cleavage site
-
-
?
additional information
?
-
the cleavage of a meprin beta substrate leads to generation of the prolyl tripeptidyl aminopeptidase (PtP, EC 3.4.14.12) substrate, and the activity of PtP results in release of a chromophore or fluorophore, coupled assay method evaluation, overview
-
-
?
additional information
?
-
-
no substrates are nitrobradykinin
-
-
?
additional information
?
-
-
no substrates are nitrobradykinin
-
-
?
additional information
?
-
-
member of astacin family
-
-
?
additional information
?
-
-
neurotensin is no substrate
-
?
additional information
?
-
-
meprin beta is likely to contribute to leukocyte transmigration events important to intestinal immune responses
-
-
?
additional information
?
-
-
the alpha/beta isoform is deleterious in case of ischemia-reperfusion, overview
-
-
?
additional information
?
-
meprin beta is unable to generate N-terminally truncated Abeta peptides from Swedish mutant APP (APPswe)
-
-
?
additional information
?
-
APP A673T mutant is less prone to cleavage by meprin beta. But, in contrast to BACE-1, meprin beta exhibits the same increased affinity for APPwt peptides and those carrying the Swedish mutation (K670N/M671L) in vitro. The amino acid composition around the beta-site in APP affects meprin beta cleavage preference
-
-
?
additional information
?
-
specific N-terminal processing of ADAM9, 10, and 17 by meprin beta
-
-
?
additional information
?
-
specific N-terminal processing of ADAM9, 10, and 17 by meprin beta
-
-
?
additional information
?
-
meprin beta is unable to generate N-terminally truncated Abeta peptides from Swedish mutant APP (APPswe)
-
-
?
additional information
?
-
APP A673T mutant is less prone to cleavage by meprin beta. But, in contrast to BACE-1, meprin beta exhibits the same increased affinity for APPwt peptides and those carrying the Swedish mutation (K670N/M671L) in vitro. The amino acid composition around the beta-site in APP affects meprin beta cleavage preference
-
-
?
additional information
?
-
-
no substrates are nitrobradykinin
-
-
?
additional information
?
-
-
no substrates are glutaryl-Ala-Ala-Phe 4-methoxynaphthalamine 2-amide
-
-
?
additional information
?
-
-
member of astacin family
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
alpha-secretase + H2O
?
meprin beta-mediated activation of the alpha-secretase
-
-
?
amyloid precursor protein + H2O
?
amyloid precursor protein + H2O
amyloid beta peptides
meprin beta initially sheds amyloid precursor protein, releasing different amyloid beta species with several cleavage sites identical with or proximal to the known beta-secretase cleavage site
-
-
?
amyloid precursor protein + H2O
amyloid precursor protein N-terminal fragments + amyloid beta protein
meprin beta can also process amyloid precursor protein in a manner reminiscent of beta-secretase, identification of cleavage sites of meprin beta in the amyloid beta sequence of the wild-type and Swedish mutant of amyloid precursor protein at positions p1 and p2, thereby generating amyloid beta variants starting at the first or second amino acid residue, mass spectrometry analysis, overview
-
-
?
angiotensin II + H2O
?
-
-
-
-
?
bradykinin + H2O
?
-
-
-
-
?
Collagen IV + H2O
?
-
-
-
-
?
dentin phosphoprotein + H2O
?
-
-
-
?
dentin sialophosphoprotein + H2O
?
-
-
-
?
fibrillar procollagen type I + H2O
fibrillar collagen type I + fibrillar collagen type I propeptide
fibrillar procollagen type III + H2O
fibrillar collagen type III + fibrillar collagen type I propeptide
gastrin + H2O
?
-
-
-
-
?
laminin V + H2O
?
-
-
-
-
?
pro-collagen I + H2O
collagen I + collagen I propeptide
maturation
-
-
?
Procollagen + H2O
?
-
-
-
?
procollagen I + H2O
collagen I + propeptide of collagen III
meprin beta removes both the C- and N-propeptides of type I procollagen, subsequently releasing fibril-forming mature collagen molecules. The C-terminal cleavage sites in the proalpha1(I) chain generated by the enzyme is identified as Ala1218/Asp1219, identical to the BMP-1 cleavage site, and also Arg1227/Asp1228, nine residues C-terminal to the BMP-1 cleavage site
-
-
?
protein kinase A + H2O
?
the enzyme cleaves at defined sites, isoform-specific interactions between the catalytic subunit of PKA (PKA C) and meprins, overview
-
-
?
Reelin + H2O
?
Reelin is a secreted glycoprotein whose function is regulated by proteolysis
-
-
?
additional information
?
-
ADAM10 + H2O
?
i.e. a disintegrin and metalloproteinase 10
-
-
?
ADAM10 + H2O
?
i.e. a disintegrin and metalloproteinase 10
-
-
?
ADAM10 + H2O
?
i.e. a disintegrin and metalloproteinase 10
-
-
?
ADAM17 + H2O
?
i.e. a disintegrin and metalloproteinase 17
-
-
?
ADAM17 + H2O
?
i.e. a disintegrin and metalloproteinase 17
-
-
?
ADAM17 + H2O
?
i.e. a disintegrin and metalloproteinase 17
-
-
?
ADAM9 + H2O
?
i.e. a disintegrin and metalloproteinase 9
-
-
?
ADAM9 + H2O
?
i.e. a disintegrin and metalloproteinase 9
-
-
?
ADAM9 + H2O
?
i.e. a disintegrin and metalloproteinase 9
-
-
?
amyloid precursor protein + H2O
?
-
-
-
?
amyloid precursor protein + H2O
?
meprin beta cleaves amyloid precursor protein at the beta-secretase site, giving rise to amyloidogenic peptides
-
-
?
amyloid precursor protein + H2O
?
APP, cleavage mechanism by meprin beta, overview
-
-
?
amyloid precursor protein + H2O
?
APP, the precursor protein is cleaved by meprin beta in distinct ways, either at the beta-secretase site resulting in increased levels of amyloid beta (Abeta) peptides, or at the N-terminus releasing 11 kDa, and 20 kDa peptide fragments. The N-terminal 11 kDa and 20 kDa peptide fragments represent physiological cleavage products
-
-
?
amyloid precursor protein + H2O
?
-
-
-
?
amyloid precursor protein + H2O
?
APP, cleavage mechanism by meprin beta, overview
-
-
?
amyloid precursor protein + H2O
?
metalloprotease meprin beta cleaves amyloid precursor protein (APP) predominantly generating N-terminally truncated Abeta2-x variants
-
-
?
amyloid precursor protein + H2O
?
metalloprotease meprin beta cleaves amyloid precursor protein (APP) predominantly generating N-terminally truncated Abeta2-x variants
-
-
?
E-cadherin + H2O
?
an extracellular matrix-related substrate
-
-
?
E-cadherin + H2O
?
an extracellular matrix-related substrate
-
-
?
fibrillar procollagen type I + H2O
fibrillar collagen type I + fibrillar collagen type I propeptide
the enzyme is capable of cleaving off the globular C- and N-terminal prodomains of fibrillar collagen type I and type III. Cleavage sites are at positions YYRA1218-/-1219DDAN and VRDR1227/-1228DLEV for the alpha1(I) chain, and additionally GGGY1108-/-1109DFGY for alpha2(I). For the N-terminal propeptide SYGY166-/-167DEKS (alpha1(I)) and AAQY81-/-82DGKG (alpha2(I)) are identified as meprin cleavage sites
-
-
?
fibrillar procollagen type I + H2O
fibrillar collagen type I + fibrillar collagen type I propeptide
the enzyme is capable of cleaving off the globular C- and N-terminal prodomains of fibrillar collagen type I and type III. Cleavage sites are at positions YYRA1218-/-1219DDAN and VRDR1227/-1228DLEV for the alpha1(I) chain, and additionally GGGY1108-/-1109DFGY for alpha2(I). For the N-terminal propeptide SYGY166-/-167DEKS (alpha1(I)) and AAQY81-/-82DGKG (alpha2(I)) are identified as meprin cleavage sites
-
-
?
fibrillar procollagen type III + H2O
fibrillar collagen type III + fibrillar collagen type I propeptide
the enzyme is capable of cleaving off the globular C- and N-terminal prodomains of fibrillar collagen type I and type III
-
-
?
fibrillar procollagen type III + H2O
fibrillar collagen type III + fibrillar collagen type I propeptide
the enzyme is capable of cleaving off the globular C- and N-terminal prodomains of fibrillar collagen type I and type III
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
an extracellular matrix-related substrate
-
-
?
Fibronectin + H2O
?
an extracellular matrix-related substrate
-
-
?
MMP1 protein + H2O
?
an extracellular matrix-related substrate
-
-
?
MMP1 protein + H2O
?
an extracellular matrix-related substrate
-
-
?
Muc2 protein + H2O
?
an extracellular matrix-related substrate
-
-
?
Muc2 protein + H2O
?
an extracellular matrix-related substrate
-
-
?
nidogen 1 + H2O
?
-
-
-
-
?
nidogen 1 + H2O
?
an extracellular matrix-related substrate
-
-
?
nidogen 1 + H2O
?
an extracellular matrix-related substrate
-
-
?
nidogen-1 + H2O
?
-
-
-
?
nidogen-1 + H2O
?
-
-
-
?
osteosarcoma-9 + H2O
?
OS-9, specific degradation by meprin beta
-
-
?
osteosarcoma-9 + H2O
?
OS-9, specific degradation by meprin beta
-
-
?
tenascin-C + H2O
?
-
specific processing by meprinbeta, cleavage mechanism, overview. Meprinbeta-digested human tenascin-C is not able to interfere with fibronectin-mediated cell spreading, confirming cleavage in the anti-adhesive domain. Meprinbeta processing of human tenascin-C neutralizes its inhibitory effect on fibronectin-mediated cell spreading
-
-
?
tenascin-C + H2O
?
an extracellular matrix-related substrate
-
-
?
tenascin-C + H2O
?
an extracellular matrix-related substrate
-
-
?
additional information
?
-
meprin B may play an important role in activation of the proinflammatory cytokine in various pathophysiological conditions
-
-
?
additional information
?
-
-
whereas the expression of meprinbeta and tenascin-C does not overlap in normal colon tissue, inflamed lesions of the mucosa from patients with Crohn's disease exhibit many meprinbeta-positive leukocytes in regions where tenascin-C is strongly induced. At least under pathological conditions, meprinbeta might attack specific functional sites in tenascin-C that are important for its oligomerization and anti-adhesive activity
-
-
?
additional information
?
-
-
meprin interacts with epithelial Na+ channel (ENaC)
-
-
?
additional information
?
-
meprin beta preferentially cleaves substrates with acidic amino acids in P1'-position
-
-
?
additional information
?
-
-
meprin beta is likely to contribute to leukocyte transmigration events important to intestinal immune responses
-
-
?
additional information
?
-
-
the alpha/beta isoform is deleterious in case of ischemia-reperfusion, overview
-
-
?
additional information
?
-
meprin beta is unable to generate N-terminally truncated Abeta peptides from Swedish mutant APP (APPswe)
-
-
?
additional information
?
-
meprin beta is unable to generate N-terminally truncated Abeta peptides from Swedish mutant APP (APPswe)
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(4-[[2-(hydroxyamino)-2-oxoethyl]sulfamoyl]phenyl)acetic acid
-
3,3'-([[2-(hydroxyamino)-2-oxoethyl]imino]dimethanediyl)dibenzamide
-
3,3'-([[2-(hydroxyamino)-2-oxoethyl]imino]dimethanediyl)dibenzoic acid
-
3-([(1,3-benzodioxol-5-ylsulfonyl)[2-(hydroxyamino)-2-oxoethyl]amino]methyl)benzoic acid
-
3-([(3-fluoro-4-methoxybenzyl)[2-(hydroxyamino)-2-oxoethyl]amino]methyl)benzoic acid
-
3-([(biphenyl-4-ylsulfonyl)[2-(hydroxyamino)-2-oxoethyl]amino]methyl)benzoic acid
-
3-([[(1R)-2-(hydroxyamino)-2-oxo-1-phenylethyl]amino]methyl)benzoic acid
-
3-([[(1S)-2-(hydroxyamino)-2-oxo-1-phenylethyl]amino]methyl)benzoic acid
-
3-([[(2R)-1-(hydroxyamino)-1-oxo-3-phenylpropan-2-yl]amino]methyl)benzoic acid
-
3-([[(2R)-1-(hydroxyamino)-1-oxopropan-2-yl]amino]methyl)benzoic acid
-
3-([[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]amino]methyl)benzoic acid
-
3-([[(2R)-3-carboxy-1-(hydroxyamino)-1-oxopropan-2-yl]amino]methyl)benzoic acid
-
3-([[(2R)-4-carboxy-1-(hydroxyamino)-1-oxobutan-2-yl]amino]methyl)benzoic acid
-
3-([[(2S)-1-(hydroxyamino)-1-oxo-3-phenylpropan-2-yl]amino]methyl)benzoic acid
-
3-([[(2S)-1-(hydroxyamino)-1-oxopropan-2-yl]amino]methyl)benzoic acid
-
3-([[(2S)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]amino]methyl)benzoic acid
-
3-([[(2S)-3-carboxy-1-(hydroxyamino)-1-oxopropan-2-yl]amino]methyl)benzoic acid
-
3-([[(2S)-4-carboxy-1-(hydroxyamino)-1-oxobutan-2-yl]amino]methyl)benzoic acid
-
3-([[(3-fluoro-4-methoxyphenyl)sulfonyl][2-(hydroxyamino)-2-oxoethyl]amino]methyl)benzoic acid
-
3-([[(4-carboxyphenyl)sulfonyl][2-(hydroxyamino)-2-oxoethyl]amino]methyl)benzoic acid
-
3-([[(4-fluorophenyl)sulfonyl][2-(hydroxyamino)-2-oxoethyl]amino]methyl)benzoic acid
-
3-([[2-(hydroxyamino)-2-oxoethyl]amino]methyl)benzoic acid
-
3-([[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]methyl)benzenecarboperoxoic acid
-
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
-
3-[(3-carboxybenzyl)[2-(hydroxyamino)-2-oxoethyl]sulfamoyl]benzoic acid
-
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
-
3-[[(2,6-difluoro-4-methoxyphenyl)methyl-[2-(hydroxyamino)-2-oxoethyl]amino]methyl]benzoic acid
-
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
-
3-[[(4-chlorophenyl)methyl-[2-(hydroxyamino)-2-oxoethyl]amino]methyl]benzoic acid
-
3-[[(4-cyanophenyl)methyl-[2-(hydroxyamino)-2-oxoethyl]amino]methyl]benzoic acid
-
3-[[(4-fluorophenyl)methyl-[2-(hydroxyamino)-2-oxoethyl]amino]methyl]benzoic acid
-
3-[[1,3-benzodioxol-5-ylmethyl-[2-(hydroxyamino)-2-oxoethyl]amino]methyl]benzoic Acid
-
3-[[2-(hydroxyamino)-2-oxoethyl]sulfamoyl]benzoic acid
-
3-[[3-(hydroxyamino)-3-oxopropyl]sulfamoyl]benzoic acid
-
3-[[benzyl-[2-(hydroxyamino)-2-oxoethyl]amino]methyl]benzoic acid
-
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
-
3-[[[2-(hydroxyamino)-2-oxo-ethyl]-[(4-propoxyphenyl)methyl]amino]methyl]benzoic acid
-
3-[[[2-(hydroxyamino)-2-oxoethyl]-(p-tolylmethyl)amino]methyl]benzoic acid
-
3-[[[2-(hydroxyamino)-2-oxoethyl]-[(3-methoxyphenyl)methyl]amino]methyl]benzoic acid
-
3-[[[2-(hydroxyamino)-2-oxoethyl]-[(4-methoxyphenyl)methyl]-amino]methyl]benzoic acid
-
3-[[[3-(hydroxyamino)-3-oxopropyl]-[(4-methoxyphenyl)-methyl]amino]methyl]benzoic acid
-
3-[[[4-(hydroxyamino)-4-oxobutyl]-[(4-methoxyphenyl)methyl]amino]methyl]benzoic acid
-
4,4'-([[2-(hydroxyamino)-2-oxoethyl]imino]dimethanediyl)dibenzoic acid
-
4-([[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]methyl)benzoic acid
-
4-[[2-(hydroxyamino)-2-oxoethyl]sulfamoyl]benzoic acid
-
Abz-MGWMDEIDK(Dnp)SG-OH
substrate inhibition
diethyl 3,3'-([[2-(hydroxyamino)-2-oxoethyl]imino]dimethanediyl)dibenzoate
-
N-hydroxy-N2-(4-methoxybenzyl)-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
-
N-hydroxy-N2-[(2-methoxy-4-methylphenyl)sulfonyl]glycinamide
-
N-hydroxy-N2-[(3-methoxyphenyl)sulfonyl]glycinamide
-
N-hydroxy-N2-[(4'-methoxybiphenyl-4-yl)sulfonyl]glycinamide
-
N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]-N2-(2-phenylethyl)glycinamide
-
N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]-N2-(3-methylbutyl)glycinamide
-
N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]-N2-methylglycinamide
-
N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
-
N-hydroxy-N2-[(4-phenoxyphenyl)sulfonyl]glycinamide
-
N-isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid
NNGH
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
-
N-[2-(hydroxyamino)-2-oxoethyl]-N-[(4-methoxyphenyl)sulfonyl]-beta-alanine
-
N-[4-(hydroxyamino)-2-(2-methylpropyl)pent-4-enoyl]-3-methylvalyl-N-(2-aminoethyl)-DL-alaninamide
-
N2,N2-bis(1,3-benzodioxol-5-ylmethyl)-N-hydroxyglycinamide
-
N2,N2-bis(2,4-difluoro-3-hydroxybenzyl)-N-hydroxyglycinamide
-
N2,N2-bis(2,4-difluoro-3-methoxybenzyl)-N-hydroxyglycinamide
-
N2,N2-bis(2,6-difluoro-3-hydroxybenzyl)-N-hydroxyglycinamide
-
N2,N2-bis(2-fluoro-3-hydroxybenzyl)-N-hydroxyglycinamide
-
N2,N2-bis(3,5-difluoro-4-hydroxybenzyl)-N-hydroxyglycinamide
-
N2,N2-bis(3-cyanobenzyl)-N-hydroxyglycinamide
-
N2,N2-bis(4-chloro-2-fluoro-3-hydroxybenzyl)-N-hydroxyglycinamide
-
N2,N2-bis(4-chloro-2-fluoro-3-methoxybenzyl)-N-hydroxyglycinamide
-
N2,N2-bis(4-fluoro-3-hydroxybenzyl)-N-hydroxyglycinamide
-
N2,N2-bis[3-(difluoromethoxy)benzyl]-N-hydroxyglycinamide
-
N2-(2,3-dihydro-1,4-benzodioxin-6-ylmethyl)-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
-
N2-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-N-hydroxyglycinamide
-
N2-(bicyclo[2.2.1]hept-2-ylmethyl)-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
-
N2-(biphenyl-4-ylsulfonyl)-N-hydroxyglycinamide
-
N2-benzyl-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
-
N2-butyl-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
-
N2-ethyl-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
-
N2-[(2,4-dimethylphenyl)sulfonyl]-N-hydroxyglycinamide
-
N2-[(3,4-dimethoxyphenyl)sulfonyl]-N-hydroxyglycinamide
-
N2-[(3,5-dichloro-4-hydroxyphenyl)sulfonyl]-N-hydroxyglycinamide
-
N2-[(3-fluoro-4-methoxyphenyl)sulfonyl]-N-hydroxyglycinamide
-
N2-[(4'-chlorobiphenyl-4-yl)sulfonyl]-N-hydroxyglycinamide
-
N2-[(4'-fluorobiphenyl-4-yl)sulfonyl]-N-hydroxyglycinamide
-
N2-[(4-chlorophenyl)sulfonyl]-N-hydroxyglycinamide
-
N2-[(4-fluorophenyl)sulfonyl]-N-hydroxyglycinamide
-
N2-[(5-chloro-2-methylphenyl)sulfonyl]-N-hydroxyglycinamide
-
N2-[[4-chloro-3-(trifluoromethyl)phenyl]sulfonyl]-N-hydroxyglycinamide
-
N3-[(3-chloro-4-hydroxyphenyl)sulfonyl]-N-hydroxy-b-alaninamide
-
N4-hydroxy-N1-[3-(1H-indol-3-yl)-1-(methylamino)-1-oxopropan-2-yl]-2-(2-methylpropyl)butanediamide
-
NF 449
4,4',4'',4'''-[carbonyl- bis[imino-5,1,3-benzenetriyl-bis-(carbonylimino)]]tetrakis-(benzene-1,3-disulfonic acid)
TAPI-2
tumour necrosis factor alpha protease inhibitor
[[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]acetic acid
-
1,10-phenanthroline
-
1,10-phenanthroline
-
strong
actinonin
-
-
actinonin
a hydroxamate derivate and naturally occurring compound produced in actinomycetes. Hydroxamate inhibitors chelate the zinc ion in the active site
actinonin
mixed type inhibition
actinonin
-
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
actinonin
markedly prevents urinary excretion of the cleaved nidogen-1
Ca2+
calcium negatively regulates meprin beta activity and attenuates substrate cleavage
Ca2+
inhibits, a negative regulator of meprin beta
EDTA
enzyme binding structure, modelling
EDTA
a common inhibitor of several astacin metalloproteases
EDTA
a common inhibitor of several astacin metalloproteases
galardin
-
galardin
enzyme binding structure, modelling
NF449
Nf449 is a suramin analogue, mixed competitive/noncompetitive inhibition, binding occurs in meprin beta active site
NF449
a potent and partially selective inhibitor
PPNDS
a potent and partially selective inhibitor
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
Pro-Leu-Gly-hydroxamate
enzyme binding structure, modelling
Pro-Leu-Gly-hydroxamate
-
-
additional information
no inhibition by cystatin C
-
additional information
inhibitor screening, overview
-
additional information
binding sites and binding structure of hydroxamic acid derivative inhibitors, molecular dynamics simulation study, overview
-
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
-
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
-
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
-
additional information
analysis of binding sites of human meprins, screening of inhibitors by molecular dynamics simulation study, molecular docking, overview
-
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
-
additional information
-
compound E-64; phosphoramidon, iodoacetic acid, 3,4-dichloroisocoumarin or soybean trypsin inhibitor
-
additional information
-
no inhibition by captopril, PMSF, pepstatin; phosphoramidon, iodoacetic acid, 3,4-dichloroisocoumarin or soybean trypsin inhibitor
-
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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0.00034 - 0.00503
(4-[[2-(hydroxyamino)-2-oxoethyl]sulfamoyl]phenyl)acetic acid
0.0131
3,3'-([[2-(hydroxyamino)-2-oxoethyl]imino]dimethanediyl)dibenzamide
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.000049
3,3'-([[2-(hydroxyamino)-2-oxoethyl]imino]dimethanediyl)dibenzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.00027
3-([(1,3-benzodioxol-5-ylsulfonyl)[2-(hydroxyamino)-2-oxoethyl]amino]methyl)benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.000375
3-([(3-fluoro-4-methoxybenzyl)[2-(hydroxyamino)-2-oxoethyl]amino]methyl)benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.00108
3-([(biphenyl-4-ylsulfonyl)[2-(hydroxyamino)-2-oxoethyl]amino]methyl)benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.01165
3-([[(1R)-2-(hydroxyamino)-2-oxo-1-phenylethyl]amino]methyl)benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.01215
3-([[(1S)-2-(hydroxyamino)-2-oxo-1-phenylethyl]amino]methyl)benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.00291
3-([[(2R)-1-(hydroxyamino)-1-oxo-3-phenylpropan-2-yl]amino]methyl)benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.00426
3-([[(2R)-1-(hydroxyamino)-1-oxopropan-2-yl]amino]methyl)benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.01185
3-([[(2R)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]amino]methyl)benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.000548
3-([[(2R)-3-carboxy-1-(hydroxyamino)-1-oxopropan-2-yl]amino]methyl)benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.000768
3-([[(2R)-4-carboxy-1-(hydroxyamino)-1-oxobutan-2-yl]amino]methyl)benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.0155
3-([[(2S)-1-(hydroxyamino)-1-oxo-3-phenylpropan-2-yl]amino]methyl)benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.0042
3-([[(2S)-1-(hydroxyamino)-1-oxopropan-2-yl]amino]methyl)benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.0158
3-([[(2S)-1-(hydroxyamino)-3-methyl-1-oxobutan-2-yl]amino]methyl)benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.001325
3-([[(2S)-3-carboxy-1-(hydroxyamino)-1-oxopropan-2-yl]amino]methyl)benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.000654
3-([[(2S)-4-carboxy-1-(hydroxyamino)-1-oxobutan-2-yl]amino]methyl)benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.00065
3-([[(3-fluoro-4-methoxyphenyl)sulfonyl][2-(hydroxyamino)-2-oxoethyl]amino]methyl)benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00032
3-([[(4-carboxyphenyl)sulfonyl][2-(hydroxyamino)-2-oxoethyl]amino]methyl)benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00106
3-([[(4-fluorophenyl)sulfonyl][2-(hydroxyamino)-2-oxoethyl]amino]methyl)benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.000377
3-([[2-(hydroxyamino)-2-oxoethyl]amino]methyl)benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.00006
3-([[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]methyl)benzenecarboperoxoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.00006
3-([[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]methyl)benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00006
3-[(3-carboperoxybenzyl)[2-(hydroxyamino)-2-oxoethyl]sulfamoyl]benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.00006
3-[(3-carboxybenzyl)[2-(hydroxyamino)-2-oxoethyl]sulfamoyl]benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00008
3-[(E)-[4-formyl-5-hydroxy-6-methyl-3-[(phosphonooxy)methyl]pyridin-2-yl]diazenyl]-7-nitronaphthalene-1,5-disulfonic acid
Homo sapiens
pH 7.5, 25°C
0.0007
3-[([2-(hydroxyamino)-2-oxoethyl][[4-(trifluoromethoxy)phenyl]sulfonyl]amino)methyl]benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.000347
3-[[(2,6-difluoro-4-methoxyphenyl)methyl-[2-(hydroxyamino)-2-oxoethyl]amino]methyl]benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.000207
3-[[(4-carboxyphenyl)methyl-[2-(hydroxyamino)-2-oxoethyl]amino]methyl]benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.000076
3-[[(4-chlorophenyl)methyl-[2-(hydroxyamino)-2-oxoethyl]amino]methyl]benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.00032
3-[[(4-cyanophenyl)methyl-[2-(hydroxyamino)-2-oxoethyl]amino]methyl]benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.000177
3-[[(4-fluorophenyl)methyl-[2-(hydroxyamino)-2-oxoethyl]amino]methyl]benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.000285
3-[[1,3-benzodioxol-5-ylmethyl-[2-(hydroxyamino)-2-oxoethyl]amino]methyl]benzoic Acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.00031
3-[[2-(hydroxyamino)-2-oxoethyl]sulfamoyl]benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00022
3-[[3-(hydroxyamino)-3-oxopropyl]sulfamoyl]benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.001285
3-[[benzyl-[2-(hydroxyamino)-2-oxoethyl]amino]methyl]benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.00128
3-[[[2-(hydroxyamino)-2-oxo-ethyl]-[(4-biphenyl)methyl]amino]methyl]benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.00225
3-[[[2-(hydroxyamino)-2-oxo-ethyl]-[(4-propoxyphenyl)methyl]amino]methyl]benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.000386
3-[[[2-(hydroxyamino)-2-oxoethyl]-(p-tolylmethyl)amino]methyl]benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.000559
3-[[[2-(hydroxyamino)-2-oxoethyl]-[(3-methoxyphenyl)methyl]amino]methyl]benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.000077
3-[[[2-(hydroxyamino)-2-oxoethyl]-[(4-methoxyphenyl)methyl]-amino]methyl]benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.000643
3-[[[3-(hydroxyamino)-3-oxopropyl]-[(4-methoxyphenyl)-methyl]amino]methyl]benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.000742
3-[[[4-(hydroxyamino)-4-oxobutyl]-[(4-methoxyphenyl)methyl]amino]methyl]benzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.000524
4,4'-([[2-(hydroxyamino)-2-oxoethyl]imino]dimethanediyl)dibenzoic acid
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.00098
4-([[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]methyl)benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00041
4-[[2-(hydroxyamino)-2-oxoethyl]sulfamoyl]benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.002
actinonin
Homo sapiens
pH and temperature not specified in the publication
0.09485
diethyl 3,3'-([[2-(hydroxyamino)-2-oxoethyl]imino]dimethanediyl)dibenzoate
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.03495
N-hydroxy-N2-(4-methoxybenzyl)-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
Homo sapiens
pH and temperature not specified in the publication
0.0257
N-hydroxy-N2-[(2-methoxy-4-methylphenyl)sulfonyl]glycinamide
Homo sapiens
pH and temperature not specified in the publication
0.01885
N-hydroxy-N2-[(3-methoxyphenyl)sulfonyl]glycinamide
Homo sapiens
pH and temperature not specified in the publication
0.00442
N-hydroxy-N2-[(4'-methoxybiphenyl-4-yl)sulfonyl]glycinamide
Homo sapiens
pH and temperature not specified in the publication
0.0429
N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]-N2-(2-phenylethyl)glycinamide
Homo sapiens
pH and temperature not specified in the publication
0.0388
N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]-N2-(3-methylbutyl)glycinamide
Homo sapiens
pH and temperature not specified in the publication
0.03253
N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]-N2-methylglycinamide
Homo sapiens
pH and temperature not specified in the publication
0.00902
N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
Homo sapiens
pH and temperature not specified in the publication
0.0188
N-hydroxy-N2-[(4-phenoxyphenyl)sulfonyl]glycinamide
Homo sapiens
pH and temperature not specified in the publication
0.4
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
Homo sapiens
pH and temperature not specified in the publication
0.00255
N-[2-(hydroxyamino)-2-oxoethyl]-N-[(4-methoxyphenyl)sulfonyl]-beta-alanine
Homo sapiens
pH and temperature not specified in the publication
0.2
N-[4-(hydroxyamino)-2-(2-methylpropyl)pent-4-enoyl]-3-methylvalyl-N-(2-aminoethyl)-DL-alaninamide
Homo sapiens
pH and temperature not specified in the publication
0.00654
N2,N2-bis(1,3-benzodioxol-5-ylmethyl)-N-hydroxyglycinamide
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.000023
N2,N2-bis(2,4-difluoro-3-hydroxybenzyl)-N-hydroxyglycinamide
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.0182
N2,N2-bis(2,4-difluoro-3-methoxybenzyl)-N-hydroxyglycinamide
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.000552
N2,N2-bis(2,6-difluoro-3-hydroxybenzyl)-N-hydroxyglycinamide
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.00291
N2,N2-bis(2-fluoro-3-hydroxybenzyl)-N-hydroxyglycinamide
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.000272
N2,N2-bis(3,5-difluoro-4-hydroxybenzyl)-N-hydroxyglycinamide
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.012
N2,N2-bis(3-cyanobenzyl)-N-hydroxyglycinamide
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.000024
N2,N2-bis(4-chloro-2-fluoro-3-hydroxybenzyl)-N-hydroxyglycinamide
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.0128
N2,N2-bis(4-chloro-2-fluoro-3-methoxybenzyl)-N-hydroxyglycinamide
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.00106
N2,N2-bis(4-fluoro-3-hydroxybenzyl)-N-hydroxyglycinamide
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.05695
N2,N2-bis[3-(difluoromethoxy)benzyl]-N-hydroxyglycinamide
Homo sapiens
40 mM Tris, pH 8.0, 30°C, recombinant enzyme
0.00193
N2-(2,3-dihydro-1,4-benzodioxin-6-ylmethyl)-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
Homo sapiens
pH and temperature not specified in the publication
0.00742
N2-(2,3-dihydro-1,4-benzodioxin-6-ylsulfonyl)-N-hydroxyglycinamide
Homo sapiens
pH and temperature not specified in the publication
0.04387
N2-(bicyclo[2.2.1]hept-2-ylmethyl)-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
Homo sapiens
pH and temperature not specified in the publication
0.00385
N2-(biphenyl-4-ylsulfonyl)-N-hydroxyglycinamide
Homo sapiens
pH and temperature not specified in the publication
0.04047
N2-benzyl-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
Homo sapiens
pH and temperature not specified in the publication
0.0375
N2-butyl-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
Homo sapiens
pH and temperature not specified in the publication
0.0312
N2-ethyl-N-hydroxy-N2-[(4-methoxyphenyl)sulfonyl]glycinamide
Homo sapiens
pH and temperature not specified in the publication
0.01477
N2-[(2,4-dimethylphenyl)sulfonyl]-N-hydroxyglycinamide
Homo sapiens
pH and temperature not specified in the publication
0.0269
N2-[(3,4-dimethoxyphenyl)sulfonyl]-N-hydroxyglycinamide
Homo sapiens
pH and temperature not specified in the publication
0.00043
N2-[(3,5-dichloro-4-hydroxyphenyl)sulfonyl]-N-hydroxyglycinamide
Homo sapiens
pH and temperature not specified in the publication
0.00619
N2-[(3-fluoro-4-methoxyphenyl)sulfonyl]-N-hydroxyglycinamide
Homo sapiens
pH and temperature not specified in the publication
0.00565
N2-[(4'-chlorobiphenyl-4-yl)sulfonyl]-N-hydroxyglycinamide
Homo sapiens
pH and temperature not specified in the publication
0.00731
N2-[(4'-fluorobiphenyl-4-yl)sulfonyl]-N-hydroxyglycinamide
Homo sapiens
pH and temperature not specified in the publication
0.01717
N2-[(4-chlorophenyl)sulfonyl]-N-hydroxyglycinamide
Homo sapiens
pH and temperature not specified in the publication
0.01432
N2-[(4-fluorophenyl)sulfonyl]-N-hydroxyglycinamide
Homo sapiens
pH and temperature not specified in the publication
0.01797
N2-[(5-chloro-2-methylphenyl)sulfonyl]-N-hydroxyglycinamide
Homo sapiens
pH and temperature not specified in the publication
0.01026
N2-[[4-chloro-3-(trifluoromethyl)phenyl]sulfonyl]-N-hydroxyglycinamide
Homo sapiens
pH and temperature not specified in the publication
0.0004
N3-[(3-chloro-4-hydroxyphenyl)sulfonyl]-N-hydroxy-b-alaninamide
Homo sapiens
pH and temperature not specified in the publication
0.000022
NF449
Homo sapiens
pH 7.5, 25°C
0.00598
[[2-(hydroxyamino)-2-oxoethyl][(4-methoxyphenyl)sulfonyl]amino]acetic acid
Homo sapiens
pH and temperature not specified in the publication
0.00034
(4-[[2-(hydroxyamino)-2-oxoethyl]sulfamoyl]phenyl)acetic acid
Homo sapiens
pH and temperature not specified in the publication
0.00503
(4-[[2-(hydroxyamino)-2-oxoethyl]sulfamoyl]phenyl)acetic acid
Homo sapiens
pH and temperature not specified in the publication
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evolution
meprin beta belongs to the astacin family within the metzincins, with a tight 1,4-beta-type Met turn located below the catalytic zinc site, featuring a strictly conserved methionine, M209
evolution
meprin beta is a metalloprotease of the astacin family characterized by a conserved zinc-binding motif (HExxHxxGFxHExxRxDR). Human meprin-alpha, EC 3.4.24.18, and -beta protease subunits are 55% identical at the amino acid level, while the substrate and peptide bond specificities vary markedly
evolution
-
meprin metalloproteases belong to the astacin family of zinc endopeptidases and the metzincin superfamily
evolution
meprin metalloproteases belong to the astacin family of zinc endopeptidases and the metzincin superfamily
evolution
meprin metalloproteases belong to the astacin family of zinc endopeptidases and the metzincin superfamily. Meprins belong to the astacin family of metalloproteases, comprising only six members in humans. These enzymes are characterized by a conserved zinc-binding motif (HExxHxxGxxHxxxRxDR) and by a sequence in close proximity to the active-site cleft, the so called Met-turn, that includes a tyrosine residue as a fifth zinc ligand. Within the astacin family, meprins exhibit a unique domain composition
evolution
the enzyme belongs to the astacin protease family
evolution
human meprin beta ia a single-zinc metalloendoprotease of the astacin family
evolution
-
meprin beta belongs to the astacin family of zinc-endopeptidases and the metzincin superfamily, characterized by the conserved motif HExxHxxGxxHxxxRxDR. Meprin beta is the only membrane-bound member of the astacin family
evolution
meprin beta belongs to the astacins of the metzincin superfamily
evolution
meprin beta belongs to the astacins of the metzincin superfamily
evolution
the astacin proteases meprin alpha and meprin beta are zinc-dependent metalloproteases of the metzincin superfamily
evolution
the enzyme encoded by Mmepb belongs to the BTP cluster of the astacin enzyme family. Structure-activity relationship of astacin metalloproteases, EDTA is used to dock into the active site cleft of the astacins to know the interaction network and to identify the important residues for binding, comparative three-dimensional structure homology modeling and docking study, and potential binding site, detailed overview
evolution
the enzyme encoded by Rmepb belongs to the BTP cluster of the astacin enzyme family. Structure-activity relationship of astacin metalloproteases, EDTA is used to dock into the active site cleft of the astacins to know the interaction network and to identify the important residues for binding, comparative three-dimensional structure homology modeling and docking study, and potential binding site, detailed overview
evolution
-
meprin beta belongs to the astacins of the metzincin superfamily
-
malfunction
-
following ischemia-reperfusion, meprins and villin redistribute from the brush-border membranes to the cytosol. A 37-kDa actin fragment is detected in protein fractions from wild-type, but not in comparable preparations from meprin knockout mice
malfunction
-
following ischemia-reperfusion, meprins and villin redistribute from the brush-border membranes to the cytosol. A 37-kDa actin fragment is detected in protein fractions from wildtype, but not in comparable preparations from meprin knockout mice
malfunction
-
N-terminal amyloid precursor protein fragments of about 11 and 20 kDa are not found in brain lysates of meprin beta -/- mice
malfunction
enzyme downregulation causes impaired intestinal mucin release and barrier function, and decreases tensile strength in the skin, but it also leads to protection against sepsis and renal injury. Enzyme upregulation can cause fibrosis, pulmonary hypertension, the Kawasaki syndrome, inflammatory bowel disease, and is involved in nephritis, cancer, and Alzheimer's disease, overview
malfunction
enzyme-deficient mice show lower amounts of mature collagen I compared with wild-type mice and exhibit significantly reduced collagen deposition in skin, along with markedly decreased tissue tensile strength
malfunction
meprin beta is the highest up-regulated gene in the lungs of Fosl2 transgenic mice compared to wild-type animals. Meprin beta knock-out mice exhibit decreased collagen deposition in skin resulting in impaired tensile strength, overview. Overexpression of meprin metalloproteases occurs under fibrotic conditions in the skin (keloids) and the lung (pulmonary hypertension)
malfunction
meprin beta-deficient mice, but not meprin alpha-deficient mice, subjected to cisplatin nephrotoxicity, significantly suppress excretion of cleaved nidogen-1
malfunction
meprin beta-knockout mice exhibit a reduced activation of the pro-inflammatory interleukin-18 and are therefore less susceptible to intestinal inflammation compared with wild-type mice. Mice lacking meprin alpha and meprin beta are significantly protected against renal ischaemia/reperfusion injury and bladder inflammation. Meprin beta-deficient mice show lower levels of the inflammatory marker interleukin-6 and decreased leucocyte infiltration after renal injury
malfunction
-
the knockdown of meprin expression in zebrafish embryos reveals an important contribution of meprin alpha in angiogenesis with reduced blood vessel formation in the morpholino-injected animals
malfunction
ablation of one of the two zinc metalloproteinases, meprin beta and BMP-1, leads to different collagen I associated phenotypes in vivo
malfunction
absence of N-APP fragments and increased endogenous sAPPalpha levels in the brains of meprin beta knockout mice
malfunction
knockout of meprin beta leads to increased sAPPalpha secretion in cortical neurons. BACE-1 activity is not increased by meprin beta preincubation. Decrease of Abeta2-40 and increase of mature APP in primary neurons of meprin beta knockout mice
malfunction
meprins KO mice exhibit deficiency in cell extravasation. Lack of meprins does not result in improved lung function in bleomycin treated mice. Decreased collagen deposition in meprin beta KO mice is concomitant with lower tissue density in comparison to wild-type mice. Expression of collagen I and III is elevated upon bleomycin in comparison to saline, but no differences are observed between different genotypes, indicating that post-translational modification is responsible for the reduction in collagen content in meprin beta KO mice
malfunction
the change to an arginine residue at position 32 represents an additional activation site used by furin-like proteases in the Golgi, which consequently leads to reduced shedding by ADAM17. The meprin beta G32R variant assesses cell proliferation, invasion through a collagen IV matrix, and outgrowth from tumor spheroids. Increased meprin beta G32R activity at the cell surface reduces cell proliferation, but increases cell invasion. The G32R meprin beta variant shows increased activity
malfunction
the protective A673T mutation in amyloid precursor protein (APP) results in reduced Abeta levels in patients, also prevents from meprin beta cleavage at position p2. 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
malfunction
-
knockout of meprin beta leads to increased sAPPalpha secretion in cortical neurons. BACE-1 activity is not increased by meprin beta preincubation. Decrease of Abeta2-40 and increase of mature APP in primary neurons of meprin beta knockout mice
-
malfunction
-
meprin beta-deficient mice, but not meprin alpha-deficient mice, subjected to cisplatin nephrotoxicity, significantly suppress excretion of cleaved nidogen-1
-
metabolism
calcium negatively regulates meprin beta activity and attenuates substrate cleavage
metabolism
during acute kidney injury induced by cisplatin or ischemia-reperfusion, membrane-bound meprins are shed and their localization is altered from the apical membranes toward the basolateral surface of the proximal tubules. Meprins are capable of cleaving basement membrane proteins in vitro and in vivo
metabolism
meprins show higher substrate and cleavage specificity compared to matrix metalloproteases
metabolism
meprins show higher substrate and cleavage specificity compared to matrix metalloproteases
metabolism
role of interaction of mannan-binding protein with meprins at the initial step of complement activation in ischemia/reperfusion injury to mouse kidney. Co-localization of the enzyme with serum-type mannan-binding protein and C3b on both the cortex and the medulla in the renal I/R-operated mouse kidney
metabolism
BACE-1 acts as the major beta-secretase in vivo generating most of the amyloid beta (Abeta) peptides at position 1, while meprin beta may act as an alternative enzyme responsible for the release of small amounts of N-terminally truncated Abeta species. APP and meprin beta co-localize in the late secretory pathway or at the cell membrane. The aggregation of N-terminally truncated Abeta2-40 peptide is significantly different from that of the non-truncated wt Abeta1-40 peptide. In particular, the Abeta2-40 species aggregate faster and reached a higher aggregation state than Abeta1-40 peptide
metabolism
identification of a proteolytic pathway of meprin beta with ADAM proteases to control protease activities at the cell surface as part of the protease web
metabolism
identification of a proteolytic pathway of meprin beta with ADAM proteases to control protease activities at the cell surface as part of the protease web
metabolism
important beta-site cleaving enzyme 1 (BACE-1)-independent contribution of the metalloprotease meprin beta within the amyloidogenic pathway. The anti-amyloidogenic alpha-secretase a disintegrin and metalloproteinase domain-containing protein 10 (ADAM10) is a direct competitor for APP at the cell surface, but also a sheddase of inactive pro-meprin beta. The activity of meprin beta is strictly extracellularly regulated within the protease web. Meprin beta itself is identified as an inducer of ADAM10 activity
metabolism
meprin metalloproteases play a role in the pathology of ischemia/reperfusion- (IR-) induced renal injury. The endoplasmic reticulum-associated protein, osteosarcoma-9 (OS-9), interacts with the C-terminal tail of meprin beta (two-hybrid system). OS-9 also interacts with the hypoxia inducible factor-1alpha (HIF-1alpha) and the prolyl-hydroxylase, proteins which mediate the cell's response to hypoxia. OS-9 proteins are most abundant in the cytosolic-enriched protein fraction of kidneys and does not occur in the brush border membrane-enriched fraction
metabolism
metalloprotease meprin beta is activated by transmembrane serine protease matriptase-2 at the cell surface thereby enhancing amyloid precursor protein (APP) shedding
metabolism
the zinc metalloproteinases meprin beta and BMP-1 are differentially regulated by CaCl2, overview
metabolism
-
identification of a proteolytic pathway of meprin beta with ADAM proteases to control protease activities at the cell surface as part of the protease web
-
metabolism
-
role of interaction of mannan-binding protein with meprins at the initial step of complement activation in ischemia/reperfusion injury to mouse kidney. Co-localization of the enzyme with serum-type mannan-binding protein and C3b on both the cortex and the medulla in the renal I/R-operated mouse kidney
-
metabolism
-
meprin metalloproteases play a role in the pathology of ischemia/reperfusion- (IR-) induced renal injury. The endoplasmic reticulum-associated protein, osteosarcoma-9 (OS-9), interacts with the C-terminal tail of meprin beta (two-hybrid system). OS-9 also interacts with the hypoxia inducible factor-1alpha (HIF-1alpha) and the prolyl-hydroxylase, proteins which mediate the cell's response to hypoxia. OS-9 proteins are most abundant in the cytosolic-enriched protein fraction of kidneys and does not occur in the brush border membrane-enriched fraction
-
metabolism
-
BACE-1 acts as the major beta-secretase in vivo generating most of the amyloid beta (Abeta) peptides at position 1, while meprin beta may act as an alternative enzyme responsible for the release of small amounts of N-terminally truncated Abeta species. APP and meprin beta co-localize in the late secretory pathway or at the cell membrane. The aggregation of N-terminally truncated Abeta2-40 peptide is significantly different from that of the non-truncated wt Abeta1-40 peptide. In particular, the Abeta2-40 species aggregate faster and reached a higher aggregation state than Abeta1-40 peptide
-
metabolism
-
during acute kidney injury induced by cisplatin or ischemia-reperfusion, membrane-bound meprins are shed and their localization is altered from the apical membranes toward the basolateral surface of the proximal tubules. Meprins are capable of cleaving basement membrane proteins in vitro and in vivo
-
physiological function
-
meprins stimulate epithelial Na+ channel (ENaC) expressed exogenously in Xenopus oocytes and endogenously in epithelial cells. Co-expression of ENaC subunits and meprin beta or alpha/beta in Xenopus oocytes increases amiloride-sensitive Na+ currents 2fold. The meprin-mediated increase in ENaC currents in oocytes and epithelial cell monolayers requires meprin beta, but not the alpha subunit
physiological function
basement membrane protein nidogen-1 is a target of meprin beta in cisplatin nephrotoxicity
physiological function
meprin beta acts as a sheddase at the cell surface where it releases the entire ectodomain of amyloid precursor protein, this cleavage event at the so-called beta-site enables gamma-secretase to further cleave the remaining C-terminal fragment of APP within the membrane, thereby releasing amyloid beta-peptides, which are known to be involved in the onset and progression of Alzheimer's disease. The enzyme is involved in inflammation by the release and maturation of cytokines and proteoglycans, it induces extracellular matrix assembly and fibrosis, and enhances cancer progression through transactivation of epidermal growth factor receptors. The cleavage of fibrillar procollagen by the enzyme is required and sufficient to induce collagen fibril assembly
physiological function
meprin beta acts as a sheddase at the cell surface where it releases the entire ectodomain of amyloid precursor protein, this cleavage event at the so-called beta-site enables gamma-secretase to further cleave the remaining C-terminal fragment of APP within the membrane, thereby releasing amyloid beta-peptides, which are known to be involved in the onset and progression of Alzheimer's disease. The enzyme is involved in inflammation by the release and maturation of cytokines and proteoglycans, it induces extracellular matrix assembly and fibrosis, and enhances cancer progression through transactivation of epidermal growth factor receptors. The cleavage of fibrillar procollagen by the enzyme is required and sufficient to induce collagen fibril assembly
physiological function
meprin beta metalloproteinase is an important enzyme in extracellular matrix turnover, inflammation, and neurodegeneration in humans
physiological function
meprin-beta regulates production of pro-inflammatory factors via a disintegrin and metalloproteinase-10 (ADAM-10) dependent pathway in macrophages. Meprin-beta increases the production of pro-inflammatory cytokines, including interleukin-1beta, interleukin-18 and interleukin-6 in macrophages, but shows no effects on the level of ligands of epidermal growth factor receptor and its activation. Activation of NF-kappaB by meprin-beta is mediated by inhibiting ADAM10-downstream extracellular signal regulated kinase (ERK1/2) pathway, molecular mechanism, overview. Meprin-beta significantly induces the phosphorylation of ERK1/2 and its upstream MEK1/2
physiological function
meprins may impact kidney injury, in part, via modulation of protein kinase A signaling pathways, meprins are implicated in ischemia-reperfusion-induced renal injury and diabetic nephropathy. Meprin cleavage decreases the kinase activity of protein kinase A subunits Calpha, Cbeta1, and Cbeta2
physiological function
physiological relevance of the unique ability of meprin alpha, EC 3.4.24.18, and meprin beta to remove the both the C- and N-propeptides of type I procollagen, subsequently releasing fibril-forming mature collagen molecules. The enzyme contributes to the integrity of connective tissue in skin
physiological function
processing of the amyloid precursor protein is of critical importance, the enzyme cleaves amyloid precursor protein and liberates soluble N-terminal amyloid precursor protein fragments
physiological function
procollagen III is processed to its mature form by meprin alpha and meprin beta, an essential step in collagen fibril assembly. The metalloprotease meprin beta is involved in inflammation, neurodegeneration, cancer and fibrosis, overview. The enzyme mediates intestinal leucocyte infiltration, in accordance with its ability to cleave adhesion molecules and components of the extracellular matrix. Meprin beta induces cell death in terminally differentiated keratinocytes. Increased meprin activity at the basement membrane leads to degradation of the renal tubular laminin-nidogen complex and other components of the basement membrane, and to the cleavage of cell-adhesion molecules (E-cadherin and tenascin-C), consequently injuring the tubular basement membrane and leading to leucocyte infiltration
physiological function
serum-type mannan-binding protein interacts with meprins in vivo in the I/R-operated mouse kidney and initiates the complement activation through the interaction with meprins in vitro, overview
physiological function
sheddase function of human meprin beta metalloproteinase at the plasma membrane, structural basis, overview. Ectodomain shedding at the cell surface is a major mechanism to regulate the extracellular and circulatory concentration or the activities of signaling proteins at the plasma membrane. Meprin beta sheds membrane-bound cytokines and growth factors, thereby contributing to inflammatory diseases, angiogenesis, and tumor progression
physiological function
the metalloproteases meprin alpha and meprin beta are involved in inflammation, neurodegeneration, cancer and fibrosis, overview
physiological function
a reduction in activity is reported under increasing calcium concentrations for meprin beta
physiological function
actinonin, a meprin alpha (EC 3.4.24.18) and meprin beta inhibitor, does not inhibit the Reelin-cleaving activity of cerebellar granular neurons (CGN) and the amount of Reelin fragments in brains of meprin beta knock-out mice is not significantly different from that of the wild-type, indicating that meprin beta does not play a major role in Reelin cleavage under basal conditions. Meprin alpha and meprin beta probably join the modulators of Reelin signalling as they cleave Reelin at a specific site and are upregulated under specific pathological conditions
physiological function
meprin B cleaves kidney OS-9 in ischemia/reperfusion
physiological function
-
meprin beta acts at the cell surface as a sheddase, cleaving transmembrane proteins, such as the amyloid precursor protein (APP). Meprins cleave compounds of the extracellular matrix such as laminin-V, collagen IV, fibronectin or nidogen 1, but also growth factors, cytokines and peptide hormones, including bradykinin, angiotensins, and gastrin
physiological function
meprin beta contributes to collagen deposition in lung fibrosis and can also facilitate collagen maturation. They have been shown to cleave cell-cell contact molecules on epithelial cells such as E-cadherin and occludin. Meprin beta is positively regulated by TGF-beta1 in epithelial cells. Meprins are important for epithelial monolayer integrity, but meprins do not influence number and composition of inflammatory cells in the bleomycin treated lungs
physiological function
meprin beta is a membrane-bound metalloprotease involved in extracellular matrix assembly and inflammatory processes in health and disease. A disintegrin and metalloproteinase (ADAM)10 and ADAM17 are physiologically relevant sheddases of inactive promeprin beta, which influences its substrate repertoire and subsequent biologic functions. Specific N-terminal processing of ADAM9, 10, and 17 by meprin beta. Because ADAM prodomains can act as specific inhibitors, meprin beta plays a role in the regulation of ADAM activities. Prodomain cleavage by meprin beta causes increased ADAM protease activities, e.g. demonstrated by increased ectodomain shedding activity. As demonstrated by a bacterial activator of meprin beta and additional measurement of TNF-alpha shedding on bone marrow-derived macrophages, meprin beta/ADAM protease interactions likely influence inflammatory conditions
physiological function
meprin beta is a membrane-bound metalloprotease involved in extracellular matrix assembly and inflammatory processes in health and disease. A disintegrin and metalloproteinase (ADAM)10 and ADAM17 are physiologically relevant sheddases of inactive promeprin beta, which influences its substrate repertoire and subsequent biologic functions. Specific N-terminal processing of ADAM9, 10, and 17 by meprin beta. Because ADAM prodomains can act as specific inhibitors, meprin beta plays a role in the regulation of ADAM activities. Prodomain cleavage by meprin beta causes increased ADAM protease activities, e.g. demonstrated by increased ectodomain shedding activity. As demonstrated by a bacterial activator of meprin beta and additional measurement of TNF-alpha shedding on bone marrow-derived macrophages, meprin beta/ADAM protease interactions likely influence inflammatory conditions. Meprin beta stimulates ADAM17 activity in macrophages because ADAM17-mediated TNF-alpha shedding is diminished in the absence of meprin beta
physiological function
meprin beta is potentially involved in disorders such as fibrosis and Alzheimer's disease
physiological function
metalloprotease meprin beta cleaves the Alzheimer's disease (AD) relevant amyloid precursor protein (APP) as a beta-secretase reminiscent of BACE-1, but predominantly generating N-terminally truncated Abeta2-x variants. Generation of aggregation prone N-terminally truncated amyloid beta peptides by meprin beta depends on the sequence specificity at the cleavage site. The N-terminally truncated Abeta2-40 variant shows increased aggregation propensity compared to Abeta1-40 and acts even as a seed for Abeta1-40 aggregation. Meprin beta cleavage of APP occurs prior to the endocytic compartments, as diminished APP endocytosis has no influence on meprin beta mediated Abeta generation. Mechanism, overview. Cellular interaction between meprin beta and APP occurs prior to endocytosis. The C-terminal motif NPxY (APPDELTANPxY) of APP is critical for proper endocytosis. Meprin beta generated Abeta2-40 promotes and seeds aggregation of Abeta peptides
physiological function
neurotoxic amyloid-beta (Abeta) plaques are one of the pathological hallmarks in Alzheimer disease patient brains. Abeta accumulates in the brain upon sequential, proteolytic processing of the amyloid precursor protein (APP) by beta- and gamma-secretases. The metalloproteinase meprin beta acts as an alternative beta-secretase, besides BACE-1, capable of generating truncated Abeta2-x peptides. Regulation of the alternative beta-secretase meprin beta by ADAM-mediated shedding. In the small intestine, meprin beta is essential for the detachment of the mucus by cleaving mucine 2 (MUC2). This is crucial for the functionality of the mucus barrier to impede bacterial overgrowth and infection. Meprin beta is an alternative beta-secretase within the complex protease web, regulating APP processing in health and disease, overview. Shed meprin beta does not act as sheddase
physiological function
neurotoxic amyloid-beta (Abeta) plaques are one of the pathological hallmarks in Alzheimer disease patient brains. Abeta accumulates in the brain upon sequential, proteolytic processing of the amyloid precursor protein (APP) by beta- and gamma-secretases. The metalloproteinase meprin beta acts as an alternative beta-secretase, besides BACE-1, capable of generating truncated Abeta2-x peptides. Regulation of the alternative beta-secretase meprin beta by ADAM-mediated shedding. Regulation of the alternative beta-secretase meprin beta by ADAM-mediated shedding. In the small intestine, meprin beta is essential for the detachment of the mucus by cleaving mucine 2 (MUC2). This is crucial for the functionality of the mucus barrier to impede bacterial overgrowth and infection. Meprin beta co-fractionates with APP and PS1 in the same high molecular weight fraction in wild-type mouse brains, and this fraction is responsible for the majority of Abeta generation
physiological function
protease meprin beta is expressed as an inactive zymogen and requires proteolytic maturation by tryptic serine proteases. Maturation of full-length meprin beta is required for its activity as a cell surface sheddase, releasing the ectodomains of transmembrane proteins, e.g. amyloid precursor protein (APP)
physiological function
the precursor protein APP is cleaved by meprin beta in distinct ways, either at the beta-secretase site resulting in increased levels of amyloid beta (Abeta) peptides, or at the N-terminus releasing 11 kDa, and 20 kDa peptide fragments. The latter event is discussed to be rather neuroprotective, whereas the ectodomain shedding of APP by meprin beta reminiscent to BACE-1 is in line with the amyloid hypothesis of Alzheimer's disease, promoting neurodegeneration. The N-terminal 11 kDa and 20 kDa peptide fragments represent physiological cleavage products, since they are found in human brains under different diseased or non-diseased states, whereas the fragments are completely missing in brains of meprin bata knock-out animals. Meprin beta generates N-APP fragments that have neither negative nor positive influence on neuronal cell viability
physiological function
-
meprin beta is a membrane-bound metalloprotease involved in extracellular matrix assembly and inflammatory processes in health and disease. A disintegrin and metalloproteinase (ADAM)10 and ADAM17 are physiologically relevant sheddases of inactive promeprin beta, which influences its substrate repertoire and subsequent biologic functions. Specific N-terminal processing of ADAM9, 10, and 17 by meprin beta. Because ADAM prodomains can act as specific inhibitors, meprin beta plays a role in the regulation of ADAM activities. Prodomain cleavage by meprin beta causes increased ADAM protease activities, e.g. demonstrated by increased ectodomain shedding activity. As demonstrated by a bacterial activator of meprin beta and additional measurement of TNF-alpha shedding on bone marrow-derived macrophages, meprin beta/ADAM protease interactions likely influence inflammatory conditions
-
physiological function
-
serum-type mannan-binding protein interacts with meprins in vivo in the I/R-operated mouse kidney and initiates the complement activation through the interaction with meprins in vitro, overview
-
physiological function
-
meprin B cleaves kidney OS-9 in ischemia/reperfusion
-
physiological function
-
metalloprotease meprin beta cleaves the Alzheimer's disease (AD) relevant amyloid precursor protein (APP) as a beta-secretase reminiscent of BACE-1, but predominantly generating N-terminally truncated Abeta2-x variants. Generation of aggregation prone N-terminally truncated amyloid beta peptides by meprin beta depends on the sequence specificity at the cleavage site. The N-terminally truncated Abeta2-40 variant shows increased aggregation propensity compared to Abeta1-40 and acts even as a seed for Abeta1-40 aggregation. Meprin beta cleavage of APP occurs prior to the endocytic compartments, as diminished APP endocytosis has no influence on meprin beta mediated Abeta generation. Mechanism, overview. Cellular interaction between meprin beta and APP occurs prior to endocytosis. The C-terminal motif NPxY (APPDELTANPxY) of APP is critical for proper endocytosis. Meprin beta generated Abeta2-40 promotes and seeds aggregation of Abeta peptides
-
physiological function
-
basement membrane protein nidogen-1 is a target of meprin beta in cisplatin nephrotoxicity
-
additional information
homology modeling of the protease domain of meprin beta on the astacin crystal structure and molecular dynamics simulation study, overview
additional information
meprin beta homodimers are essentially membrane bound but may also be shed fromthe surface byADAM-10 and -17. Multidomain structure, zymogenic determinants, catalytic domain, and MAM and TRAF domains in promeprin beta, and structure-activity analysis, homology modeling, overview
additional information
transcriptional regulation of meprin beta expression by the heterodimeric transcription factor AP-1 (activator protein 1), overview
additional information
transcriptional regulation of meprin beta expression by the heterodimeric transcription factor AP-1 (activator protein 1), overview
additional information
enzyme sequence analysis and homology modeling of ADAM proteases, overview
additional information
enzyme sequence analysis and homology modeling of ADAM proteases, overview
additional information
human meprin beta is modelled using the template structure of astacin
additional information
meprin beta activity and localization is strictly regulated
additional information
-
meprin beta activity and localization is strictly regulated
additional information
meprin beta activity and localization is strictly regulated
additional information
molecular structure modelling of promeprin beta nd meprin beta, overview
additional information
structural differences between meprin beta and BMP-1 (EC 3.4.24.21). Molecular dynamics simulation
additional information
the extracellular metalloprotease meprin beta is expressed as a homodimer and is primarily membrane bound. Meprin beta can be released from the cell surface by its known sheddases ADAM10 and ADAM17. Activation of pro-meprin beta at the cell surface prevents its shedding, thereby stabilizing its proteolytic activity at the plasma membrane
additional information
the hydrogen bonding residues of the enzyme are Cys125, Glu154, and Arg239, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 4GWN) and docking study, and potential binding site, detailed overview
additional information
the hydrogen bonding residues of the enzyme are Cys125, Thr150, Tyr212, and His211, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 4GWN) and docking study, and potential binding site, detailed overview
additional information
the S1 and S2' subpockets within the active site of meprin beta are formed by arginines Arg184 and Arg146, respectively
additional information
-
enzyme sequence analysis and homology modeling of ADAM proteases, overview
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Kounnas, M.Z.; Woltz, R.L.; Gorbea, C.M.; Bond, J.S.
Meprin-A and -B. Cell surface endopeptidases of the mouse kidney
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Homo sapiens
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Homo sapiens (Q16820)
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Homo sapiens (Q16820), Homo sapiens, Mus musculus (Q61847)
brenda
Chaudhuri, A.; Bera, A.K.; Sarkar, I.; Chakraborty, S.
Insights from analysis of binding sites of human meprins screening of inhibitors by molecular dynamics simulation study
Comb. Chem. High Throughput Screen.
19
246-258
2016
Homo sapiens (Q16820)
brenda
Chaudhuri, A.; Chakraborty, S.
Structure-activity relationship of astacin metalloproteases A comparative study using EDTA
Curr. Enzyme Inhib.
14
131-140
2018
Mus musculus (Q61847), Rattus norvegicus (P28826)
-
brenda
Wichert, R.; Scharfenberg, F.; Colmorgen, C.; Koudelka, T.; Schwarz, J.; Wetzel, S.; Potempa, B.; Potempa, J.; Bartsch, J.W.; Sagi, I.; Tholey, A.; Saftig, P.; Rose-John, S.; Becker-Pauly, C.
Meprin beta induces activities of A disintegrin and metalloproteinases 9, 10, and 17 by specific prodomain cleavage
FASEB J.
33
11925-11940
2019
Homo sapiens (Q16820), Mus musculus (Q61847), Mus musculus C57/BL6N (Q61847)
brenda
Becker-Pauly, C.; Pietrzik, C.U.
The metalloprotease meprin beta is an alternative beta-secretase of APP
Front. Mol. Neurosci.
9
159
2016
Homo sapiens (Q16820), Homo sapiens
brenda
Martin, B.L.; Conley, S.M.; Harris, R.S.; Stanley, C.D.; Niyitegeka, J.M.; Ongeri, E.M.
Hypoxia associated proteolytic processing of OS-9 by the metalloproteinase meprin beta
Int. J. Nephrol.
2016
2851803
2016
Mus musculus (Q61847), Mus musculus C57BL/6 (Q61847)
brenda
Sato, Y.; Kobayashi, D.; Kohno, T.; Kidani, Y.; Prox, J.; Becker-Pauly, C.; Hattori, M.
Determination of cleavage site of Reelin between its sixth and seventh repeat and contribution of meprin metalloproteases to the cleavage
J. Biochem.
159
305-312
2015
Mus musculus (Q61847)
brenda
Schaeffler, H.; Li, W.; Helm, O.; Krueger, S.; Boeger, C.; Peters, F.; Roecken, C.; Sebens, S.; Lucius, R.; Becker-Pauly, C.; Arnold, P.
The cancer-associated meprin beta variant G32R provides an additional activation site and promotes cancer cell invasion
J. Cell Sci.
132
jes220665
2019
Homo sapiens (Q16820)
brenda
Ramsbeck, D.; Hamann, A.; Richter, G.; Schlenzig, D.; Geissler, S.; Nykiel, V.; Cynis, H.; Schilling, S.; Buchholz, M.
Structure-guided design, synthesis, and characterization of next-generation meprin beta inhibitors
J. Med. Chem.
61
4578-4592
2018
Homo sapiens (Q16820)
brenda
Becker-Pauly, C.; Rose-John, S.
Meprin and ADAM metalloproteases two sides of the same coin?
Matrix Metalloproteinase Biology (ed. Sagi I. and Gaffney J.P.)
2015
115-130
2015
Homo sapiens
-
brenda
Schoenherr, C.; Bien, J.; Isbert, S.; Wichert, R.; Prox, J.; Altmeppen, H.; Kumar, S.; Walter, J.; Lichtenthaler, S.F.; Weggen, S.; Glatzel, M.; Becker-Pauly, C.; Pietrzik, C.U.
Generation of aggregation prone N-terminally truncated amyloid beta peptides by meprin beta depends on the sequence specificity at the cleavage site
Mol. Neurodegener.
11
19
2016
Mus musculus (Q61847), Mus musculus C57BL/6 (Q61847)
brenda
Schlenzig, D.; Wermann, M.; Ramsbeck, D.; Moenke-Wedler, T.; Schilling, S.
Expression, purification and initial characterization of human meprin beta from Pichia pastoris
Protein Expr. Purif.
116
75-81
2015
Homo sapiens (Q16820)
brenda
Biasin, V.; Wygrecka, M.; Marsh, L.M.; Becker-Pauly, C.; Brcic, L.; Ghanim, B.; Klepetko, W.; Olschewski, A.; Kwapiszewska, G.
Meprin beta contributes to collagen deposition in lung fibrosis
Sci. Rep.
7
39969
2017
Homo sapiens (Q16820), Mus musculus (Q61847)
brenda