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 | 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 | - |
- |
plasma membrane | meprin beta is a secreted homodimeric multidomain type-I membrane metallopeptidase | Homo sapiens | 5886 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | metalloproteinase | Homo sapiens |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
145000 | - |
- |
Homo sapiens |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q16820 | - |
- |
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 | 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 | 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 | Comment | Organism |
---|---|---|
meprin beta | - |
Homo sapiens |
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 |