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
-
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
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Posttranslational Modification
Posttranslational Modification on EC 3.4.24.63 - meprin B
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glycoprotein
proteolytic modification
glycoprotein
deglycosylation of recombinant enzyme by peptide-N-glycosidase
glycoprotein
the recombinant enzyme expressed in Pichia pastoris is N-glycosylated. Deglycosylation by endoglycosidase H does not alter the kinetics of the enzyme significantly
proteolytic modification
meprins are secreted as zymogens and are activated by trypsin-like serine proteases (e.g., human kallikrein related peptidases, KLK)
proteolytic modification
the recombinant N-terminally His-tagged human meprin beta zymogen is activated by cleavage with trypsin
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
proteolytic modification
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activation of meprin beta by proteolytic cleavage. Meprin beta contains a conserved sequence motif, which gives rise to enzymatic activation by tryptic serine proteases. Pancreatic trypsin performs this activation in the gut. Meprin beta cannot be activated by plasmin in the gut. In skin, the human tissue kallikrein-related peptidase 4 (KLK4), KLK5, and KLK8, cleave off the propeptide of meprin beta
proteolytic modification
matriptase-2 (MT-2), a type 2 transmembrane protein, fully activates meprin beta at the cell surface
proteolytic modification
metalloprotease meprin beta is activated by transmembrane serine protease matriptase-2 (MT2) at the cell surface. No processing by TMPRSS4 or pancreatic trypsin. The cleavage site for maturation within the propeptide of meprin beta is in close proximity to the plasma membrane, crystal structure analysis, PDB ID 4GWM. Proteomic identification of the MT2-dependent cleavage in pro-meprin beta by mass spectrometry
proteolytic modification
pro-meprin beta is activated by trypsin (15:1 w/w) at room temperature in the presence of 10 mM CaCl2 for 10 min. Subsequently, trypsin is inactivated by the addition of 5 mM 4-(2-aminoethyl)benzenesulfonyl fluoride (AEBSF)
proteolytic modification
proteolytic activation and shedding of meprin beta are mutually exclusive events. Cleavage of the pro-peptide completely blocks shedding of meprin beta by ADAM10 and ADAM17. The anti-amyloidogenic alpha-secretase a disintegrin and metalloproteinase domain-containing protein 10 (ADAM10) is a direct competitor for APP at the cell surface, but also a sheddase of inactive pro-meprin beta. Shedding of meprin beta by ADAM10/17 is completely abolished upon its activation by matrilysin-2 (MT-2, 3.4.24.23) at the cell surface. Only the proform of meprin beta can be shed. Meprin beta requires activation by tryptic proteases
proteolytic modification
proteolytic activation of pro-meprin beta at the cell surface, serine protease matriptase-2 (MT-2) is a membrane-bound activator of meprin beta. Shedding of meprin beta is mediated by endogenous ADAM10 or ADAM17. Shedding of meprin beta mutant G32R mediated by ADAM17 is impaired
proteolytic modification
the crystal structure of the zymogen form of meprin beta revealsthat the active side is shielded by the pro-peptide. Gln62 is directed away from the salt bridge that is formed by Glu163 and Lys248. The new N-terminus is formed by Asp62 after removal of the pro-peptide by tryptic serine protease cleavage between Arg61 and Gln62. In active meprin beta N62 forms a salt bridge with E163 and thus removes the new N-terminus from the active site, overview
proteolytic modification
the recombinant His6-tagged enzyme is activated by cleavage through trypsin
proteolytic modification
meprins are secreted as zymogens and are activated by trypsin-like serine proteases
proteolytic modification
meprin beta is activated using limited trypsin proteolysis
proteolytic modification
proteolytic activation and shedding of meprin beta are mutually exclusive events. Cleavage of the pro-peptide completely blocks shedding by ADAM10/17
proteolytic modification
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meprin beta is activated using limited trypsin proteolysis
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proteolytic modification
activation of recombinant zymogen enzyme by trypsin