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Literature summary for 3.4.24.63 extracted from

  • Becker-Pauly, C.; Pietrzik, C.U.
    The metalloprotease meprin beta is an alternative beta-secretase of APP (2016), Front. Mol. Neurosci., 9, 159 .
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface
-
Homo sapiens 9986
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membrane membrane-bound Homo sapiens 16020
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Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ a zinc-dependent metalloprotease 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 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 ?
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?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q16820
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-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification matriptase-2 (MT-2), a type 2 transmembrane protein, fully activates meprin beta at the cell surface Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Homo sapiens
-
connective tissue
-
Homo sapiens
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neuron
-
Homo sapiens
-
skin
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 Homo sapiens ?
-
?
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 Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
meprin beta
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Homo sapiens

General Information

General Information Comment Organism
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 Homo sapiens