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Literature summary for 3.4.24.63 extracted from

  • 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 (2019), FASEB J., 33, 11925-11940 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of C-terminally Flag-tagged meprin beta in HEK-293 cells Homo sapiens
recombinant expression of C-terminally Flag-tagged meprin beta in HEK-293 cells Mus musculus

Protein Variants

Protein Variants Comment Organism
E153A site-directed mutagenesis, a proteolytic inactive mutant enzyme Homo sapiens
additional information generation of enzyme knockout Mep1beta-/- mice from wild-type C57/BL6N, isolation of bone marrow-derived macrophages and phenotype, overview Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface
-
Homo sapiens 9986
-
cell surface
-
Mus musculus 9986
-
membrane membrane-bound Homo sapiens 16020
-
membrane membrane-bound Mus musculus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ a zinc-dependent metalloprotease Homo sapiens
Zn2+ a zinc-dependent metalloprotease Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ADAM10 + H2O Homo sapiens i.e. a disintegrin and metalloproteinase 10 ?
-
?
ADAM10 + H2O Mus musculus i.e. a disintegrin and metalloproteinase 10 ?
-
?
ADAM10 + H2O Mus musculus C57/BL6N i.e. a disintegrin and metalloproteinase 10 ?
-
?
ADAM17 + H2O Homo sapiens i.e. a disintegrin and metalloproteinase 17 ?
-
?
ADAM17 + H2O Mus musculus i.e. a disintegrin and metalloproteinase 17 ?
-
?
ADAM17 + H2O Mus musculus C57/BL6N i.e. a disintegrin and metalloproteinase 17 ?
-
?
ADAM9 + H2O Homo sapiens i.e. a disintegrin and metalloproteinase 9 ?
-
?
ADAM9 + H2O Mus musculus i.e. a disintegrin and metalloproteinase 9 ?
-
?
ADAM9 + H2O Mus musculus C57/BL6N i.e. a disintegrin and metalloproteinase 9 ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q16820
-
-
Mus musculus Q61847
-
-
Mus musculus C57/BL6N Q61847
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant Flag-tagged meprin beta from HEK-293 cells by protein G affinity chromatography. Co-immunoprecipitation of C-terminal Flag-tagged meprin beta and C-terminal Myc-tagged ADAM proteases is performed in HEK-293T cells Homo sapiens
recombinant Flag-tagged meprin beta from HEK-293 cells by protein G affinity chromatography. Co-immunoprecipitation of C-terminal Flag-tagged meprin beta and C-terminal Myc-tagged ADAM proteases is performed in HEK-293T cells Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
macrophage bone marrow-derived Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADAM10 + H2O i.e. a disintegrin and metalloproteinase 10 Homo sapiens ?
-
?
ADAM10 + H2O i.e. a disintegrin and metalloproteinase 10 Mus musculus ?
-
?
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 Homo sapiens ?
-
?
ADAM10 + H2O i.e. a disintegrin and metalloproteinase 10 Mus musculus C57/BL6N ?
-
?
ADAM17 + H2O i.e. a disintegrin and metalloproteinase 17 Homo sapiens ?
-
?
ADAM17 + H2O i.e. a disintegrin and metalloproteinase 17 Mus musculus ?
-
?
ADAM17 + H2O i.e. a disintegrin and metalloproteinase 17, reombinant C-terminally Myc-tagged substrate Homo sapiens ?
-
?
ADAM17 + H2O i.e. a disintegrin and metalloproteinase 17 Mus musculus C57/BL6N ?
-
?
ADAM9 + H2O i.e. a disintegrin and metalloproteinase 9 Homo sapiens ?
-
?
ADAM9 + H2O i.e. a disintegrin and metalloproteinase 9 Mus musculus ?
-
?
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 Homo sapiens ?
-
?
ADAM9 + H2O i.e. a disintegrin and metalloproteinase 9 Mus musculus C57/BL6N ?
-
?
additional information specific N-terminal processing of ADAM9, 10, and 17 by meprin beta Mus musculus ?
-
?
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 Homo sapiens ?
-
?
additional information specific N-terminal processing of ADAM9, 10, and 17 by meprin beta Mus musculus C57/BL6N ?
-
?

Synonyms

Synonyms Comment Organism
meprin beta
-
Homo sapiens
meprin beta
-
Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Homo sapiens
37
-
assay at Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Homo sapiens
7.5
-
assay at Mus musculus

General Information

General Information Comment Organism
evolution meprin beta belongs to the astacins of the metzincin superfamily Homo sapiens
evolution meprin beta belongs to the astacins of the metzincin superfamily Mus musculus
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 Homo sapiens
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 Mus musculus
additional information enzyme sequence analysis and homology modeling of ADAM proteases, overview Homo sapiens
additional information enzyme sequence analysis and homology modeling of ADAM proteases, overview Mus musculus
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 Mus musculus
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 Homo sapiens