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Literature summary for 3.4.24.63 extracted from

  • Arolas, J.; Broder, C.; Jefferson, T.; Guevara, T.; Sterchi, E.; Bode, W.; Stoecker, W.; Becker-Pauly, C.; Gomis-Rueth, F.
    Structural basis for the sheddase function of human meprin beta metalloproteinase at the plasma membrane (2012), Proc. Natl. Acad. Sci. USA, 109, 16131-16136.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
zymogen promeprin beta and the major fragment of the meprin beta-ectoprotein, X-ray diffraction structure determination and analysis, modeling Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular meprin beta is a secreted homodimeric multidomain type-I membrane metallopeptidase Homo sapiens
-
-
additional information meprin beta homodimers are essentially membrane bound but may also be shed from the surface by ADAM-10 and -17 Homo sapiens
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-
plasma membrane meprin beta is a secreted homodimeric multidomain type-I membrane metallopeptidase Homo sapiens 5886
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ metalloproteinase Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
145000
-
-
Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
amyloid precursor protein + H2O Homo sapiens meprin beta cleaves amyloid precursor protein at the beta-secretase site, giving rise to amyloidogenic peptides ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q16820
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-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein
-
Homo sapiens
proteolytic modification zymogen promeprin beta is activated to mature meprin beta by proteolysis of the N-terminal prodomain, which is catalyzed by trypsin in the intestinal lumen and kallikrein-related peptidases (KLK-4, -5, and -8) in other tissues, overview Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
amyloid precursor protein + H2O meprin beta cleaves amyloid precursor protein at the beta-secretase site, giving rise to amyloidogenic peptides Homo sapiens ?
-
?
additional information sheddase mechanism of meprin beta, overview Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
homodimer meprin beta is a homodimeric multidomain type-I membrane metallopeptidase Homo sapiens
More the enzyme assembles into either disulfide-linked homodimers or heterodimers with the closely related meprin alpha-subunit, EC 3.4.24.18. Meprin beta domain structure, detailed overview Homo sapiens

Synonyms

Synonyms Comment Organism
meprin beta
-
Homo sapiens

General Information

General Information Comment Organism
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 Homo sapiens
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 Homo sapiens
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 Homo sapiens