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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Subunits
Subunits on EC 3.4.24.63 - meprin B
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dimer
homodimer
oligomer
additional information
meprin beta is a multidomain metalloprotease and a dimeric type 1 transmembrane protein, enzyme domain structure, overview. The enzyme consists of a propeptide (PRO), a catalytic domain (CAT), a MAM (meprin A5 protein tyrosine phosphatase mu) domain, a TRAF (tumor-necrosis-factor-receptor-associated factor) domain, an EGF (epidermal growth factor) like domain, a transmembrane region and a C-terminal part
dimer
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the mature protease forms dimers which are stabilized by an intermolecular disulfide bond between the MAM domains
dimer
meprin beta is a multidomain metalloprotease and a dimeric type 1 transmembrane protein, enzyme domain structure, overview. The enzyme consists of a propeptide (PRO), a catalytic domain (CAT), a MAM (meprin A5 protein tyrosine phosphatase mu) domain, a TRAF (tumor-necrosis-factor-receptor-associated factor) domain, an EGF (epidermal growth factor) like domain, a transmembrane region and a C-terminal part
dimer
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a model of the meprin B dimer structure is proposed that provides insight into the relationship between structure and function of thus isoforms
homodimer
homodimer linked by a disulfide bridge, domain structure of human meprins, overview
homodimer
meprin beta is a homodimeric multidomain type-I membrane metallopeptidase
homodimer
domain composition and dimeric structure of the metalloprotease meprin beta, overview. The enzyme consists of propeptide, catalytic domain, meprin A5 protein tyrosine phosphatase micro domain, tumour-necrosis-factor-receptor-associated factor domain, epidermal growth factor-like domain, transmembrane region, and C-terminal part
homodimer
the enzyme consists of the protease domain with a 39 amino acid long inhibitory pro-peptide, a MAM domain, a TRAF domain, an EGF-like domain, a transmembrane helix, and a small C-terminal cytosolic domain
homodimer
domain composition and dimeric structure of the metalloprotease meprin beta, overview. The enzyme consists of propeptide, catalytic domain, meprin A5 protein tyrosine phosphatase micro domain, tumour-necrosis-factor-receptor-associated factor domain, epidermal growth factor-like domain, transmembrane region, and C-terminal part
oligomer
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x * 90000, mouse, SDS-PAGE under reducing or non-reducing conditions
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oligomer
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x * 74000, deglycosylated enzyme, SDS-PAGE under reducing conditions
oligomer
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x * 84000, expressed in human kidney 293 cells, deglycosylated form, SDS-PAGE under reducing conditions
oligomer
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x * 97000, expressed in human kidney 293 cells, SDS-PAGE under reducing conditions
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all three meprin subunits identified in zebrafish contain the typical astacin domain, the Met-turn SxMHY, and the four cysteine residues that form two disulfide bonds
additional information
all three meprin subunits identified in zebrafish contain the typical astacin domain, the Met-turn SxMHY, and the four cysteine residues that form two disulfide bonds
additional information
all three meprin subunits identified in zebrafish contain the typical astacin domain, the Met-turn SxMHY, and the four cysteine residues that form two disulfide bonds
additional information
all three meprin subunits identified in zebrafish contain the typical astacin domain, the Met-turn SxMHY, and the four cysteine residues that form two disulfide bonds
additional information
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
additional information
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the enzyme is formed by alpha and/or beta subunits, the alpha/beta isoform is deleterious in case of ischemia-reperfusion, overview