3.4.24.63: meprin B
This is an abbreviated version!
For detailed information about meprin B, go to the full flat file.
Word Map on EC 3.4.24.63
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3.4.24.63
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alzheimer
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amyloid
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abeta
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gamma-secretase
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beta-amyloid
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plaque
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amyloid-beta
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beta-site
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amyloidogenic
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alpha-secretase
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aspartyl
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cerebral
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presenilins
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senile
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neurodegenerative
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bace-1
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swedish
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sappalpha
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neuropathology
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tau
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neurotoxic
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app-cleaving
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neuroblastoma
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beta-peptide
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ectodomains
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dementia
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protein-cleaving
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medicine
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nicastrin
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drug development
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amyloidogenesis
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tangles
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isostere
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memapsin
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peptidomimetic
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abeta1-40
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appswe
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ad-like
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hydroxyethylene
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neurofibrillary
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adam10
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beta-protein
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ad-associated
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endoproteolytic
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insulin-degrading
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non-amyloidogenic
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betaapp
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neprilysin
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pharmacology
- 3.4.24.63
- alzheimer
-
amyloid
- abeta
- gamma-secretase
- beta-amyloid
- plaque
- amyloid-beta
-
beta-site
-
amyloidogenic
- alpha-secretase
-
aspartyl
- cerebral
-
presenilins
-
senile
- neurodegenerative
- bace-1
-
swedish
-
sappalpha
-
neuropathology
- tau
-
neurotoxic
-
app-cleaving
- neuroblastoma
- beta-peptide
- ectodomains
- dementia
-
protein-cleaving
- medicine
-
nicastrin
- drug development
-
amyloidogenesis
-
tangles
-
isostere
-
memapsin
-
peptidomimetic
- abeta1-40
-
appswe
-
ad-like
-
hydroxyethylene
-
neurofibrillary
- adam10
- beta-protein
-
ad-associated
-
endoproteolytic
-
insulin-degrading
-
non-amyloidogenic
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betaapp
- neprilysin
- pharmacology
Reaction
Hydrolysis of proteins, including azocasein, and peptides. Hydrolysis of -His5-/-Leu-, -Leu6-/-Cys-, -Ala14-/-Leu- and -Cys19-/-Gly- bonds in insulin B chain =
Synonyms
beta-secretase, cell surface sheddase, h-meprin beta, MEP1B, mephrin beta, meprin A subunit beta, Meprin b, meprin B metalloprotease, meprin beta, meprin beta metalloproteinase, meprin metalloprotease, meprin metalloproteinase, meprin metalloproteinase beta, meprin-beta, meprinbeta, metalloprotease meprin, metalloprotease meprin B, metalloprotease meprin beta, metalloproteinase meprin beta, Mmepb, More, mouse meprin beta, procollagen proteinase, Rmepb
ECTree
3.4.24.63 meprin BAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.4.24.63 - meprin B
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
alpha-secretase + H2O
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meprin beta-mediated activation of the alpha-secretase
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?
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
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?
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
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?
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
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
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?
protein kinase A + H2O
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the enzyme cleaves at defined sites, isoform-specific interactions between the catalytic subunit of PKA (PKA C) and meprins, overview
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?
Reelin + H2O
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Reelin is a secreted glycoprotein whose function is regulated by proteolysis
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?
amyloid precursor protein + H2O
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meprin beta cleaves amyloid precursor protein at the beta-secretase site, giving rise to amyloidogenic peptides
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?
amyloid precursor protein + H2O
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APP, cleavage mechanism by meprin beta, overview
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?
amyloid precursor protein + H2O
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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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?
amyloid precursor protein + H2O
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APP, cleavage mechanism by meprin beta, overview
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?
amyloid precursor protein + H2O
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metalloprotease meprin beta cleaves amyloid precursor protein (APP) predominantly generating N-terminally truncated Abeta2-x variants
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?
amyloid precursor protein + H2O
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metalloprotease meprin beta cleaves amyloid precursor protein (APP) predominantly generating N-terminally truncated Abeta2-x variants
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?
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
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?
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
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?
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
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?
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
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?
osteosarcoma-9 + H2O
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OS-9, specific degradation by meprin beta
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?
tenascin-C + H2O
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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
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?
additional information
?
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meprin B may play an important role in activation of the proinflammatory cytokine in various pathophysiological conditions
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?
additional information
?
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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
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additional information
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meprin interacts with epithelial Na+ channel (ENaC)
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additional information
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meprin beta preferentially cleaves substrates with acidic amino acids in P1'-position
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?
additional information
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meprin beta is likely to contribute to leukocyte transmigration events important to intestinal immune responses
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?
additional information
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the alpha/beta isoform is deleterious in case of ischemia-reperfusion, overview
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?
additional information
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meprin beta is unable to generate N-terminally truncated Abeta peptides from Swedish mutant APP (APPswe)
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?
additional information
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meprin beta is unable to generate N-terminally truncated Abeta peptides from Swedish mutant APP (APPswe)
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?
