Information on EC 3.4.24.63 - meprin B

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The expected taxonomic range for this enzyme is: Euteleostomi

EC NUMBER
COMMENTARY
3.4.24.63
-
RECOMMENDED NAME
GeneOntology No.
meprin B
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Hydrolysis of proteins, including azocasein, and peptides. Hydrolysis of -His5-/-Leu-, -Leu6-/-Cys-, -Ala14-/-Leu- and -Cys19-/-Gly- bonds in insulin B chain
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
mephrin beta
-
-
Meprin b
-
-
-
-
Meprin b
-
-
Meprin b
-
-
Meprin b
-
analysis of gene encoding subunit meprinbeta
Meprin b
-
-
meprin B metalloprotease
-
-
meprin beta
-
-
meprin metalloproteinase
-
-
meprin metalloproteinase beta
-
-
meprinbeta
-
-
metalloprotease meprin
-
-
mouse meprin beta
-
-
metalloprotease meprin B
-
-
additional information
-, Q5RHM1, Q5RHM2, Q5RKM1
the enzyme is a member of the astacin family of metalloproteases
CAS REGISTRY NUMBER
COMMENTARY
150679-52-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
meprin alpha1 subunit
SwissProt
Manually annotated by BRENDA team
meprin alpha2 subunit
Q5RHM2
SwissProt
Manually annotated by BRENDA team
C57BL/6 wild-type mice
-
-
Manually annotated by BRENDA team
high IgA mouse used as model of human IgA nephropathy
-
-
Manually annotated by BRENDA team
inbred strain C3H/He; male adults
-
-
Manually annotated by BRENDA team
inbred strain C3H/He; male adults; more than 20 inbred, recombinant and congenic strains
-
-
Manually annotated by BRENDA team
inbred strain C3H/He; male adults; strain C57BL
-
-
Manually annotated by BRENDA team
mouse
-
-
Manually annotated by BRENDA team
mouse strain, ICR and C3H/He
-
-
Manually annotated by BRENDA team
Mus musculus C57BL
strain C57BL
-
-
Manually annotated by BRENDA team
recombinant
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
following ischemia-reperfusion, meprins and villin redistribute from the brush-border membranes to the cytosol. A 37-kDa actin fragment is detected in protein fractions from wildtype, but not in comparable preparations from meprin knockout mice
malfunction
-
following ischemia-reperfusion, meprins and villin redistribute from the brush-border membranes to the cytosol. A 37-kDa actin fragment is detected in protein fractions from wild-type, but not in comparable preparations from meprin knockout mice
malfunction
-
N-terminal amyloid precursor protein fragments of about 11 and 20 kDa are not found in brain lysates of meprin beta -/- mice
physiological function
-
meprins stimulate epithelial Na+ channel (ENaC) expressed exogenously in Xenopus oocytes and endogenously in epithelial cells. Co-expression of ENaC subunits and meprin beta or alpha/beta in Xenopus oocytes increases amiloride-sensitive Na+ currents 2fold. The meprin-mediated increase in ENaC currents in oocytes and epithelial cell monolayers requires meprin beta, but not the alpha subunit
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-MGWM--DEIDK(2,4-dinitrophenyl)SG-OH + H2O
?
show the reaction diagram
-
-
-
?
actin + H2O
?
show the reaction diagram
-
villin and actin bind to the cytoplasmic tail of meprin beta
-
-
?
alpha-MSH + H2O
?
show the reaction diagram
-
-
-
-
-
alpha-MSH + H2O
?
show the reaction diagram
-
-
-
?
amyloid precursor protein + H2O
?
show the reaction diagram
-
-
-
-
?
amyloid precursor protein + H2O
?
show the reaction diagram
-
APP Is Processed by meprin beta in Vivo
-
-
?
azocasein + H2O
?
show the reaction diagram
-
-
-
?
azocasein + H2O
?
show the reaction diagram
-
poor substrate
-
-
-
azocasein + H2O
?
show the reaction diagram
-
poor substrate
-
-
-
azocasein + H2O
?
show the reaction diagram
-
poor substrate
-
-
-
azocasein + H2O
?
show the reaction diagram
-
mouse enzyme: poor substrate unless activated by trypsin treatment (i.e. latent azocaseinase activity)
-
-
-
azocasein + H2O
?
show the reaction diagram
Mus musculus C57BL
-
poor substrate, mouse enzyme: poor substrate unless activated by trypsin treatment (i.e. latent azocaseinase activity)
-
-
-
Boc-CCK8NH2 + H2O
?
show the reaction diagram
-
peptide of the gastrointestinal tract
-
?
Bradykinin + H2O
?
show the reaction diagram
-
-
-
?
CCK4 + H2O
?
show the reaction diagram
-
peptide of the gastrointestinal tract
-
?
CCK5 + H2O
?
show the reaction diagram
-
peptide of the gastrointestinal tract
-
?
CCK6 + H2O
?
show the reaction diagram
-
peptide of the gastrointestinal tract
-
?
CCK7 + H2O
?
show the reaction diagram
-
peptide of the gastrointestinal tract
-
?
CCK8 + H2O
?
show the reaction diagram
-
peptide of the gastrointestinal tract
-
?
CCK8NH2 + H2O
?
show the reaction diagram
-
peptide of the gastrointestinal tract
-
?
cerulein + H2O
?
show the reaction diagram
-
peptide of the gastrointestinal tract
-
?
Cholecystokinin + H2O
?
show the reaction diagram
-
-
-
?
cholecystokinin 8 sulfate + H2O
?
show the reaction diagram
-
-
-
?
collagen I + H2O
?
show the reaction diagram
-
-
-
?
Collagen IV + H2O
?
show the reaction diagram
-
-
-
?
Fibronectin + H2O
?
show the reaction diagram
-
-
-
?
gastrin 17 + H2O
?
show the reaction diagram
-
-
-
?
gastrin 17 + H2O
?
show the reaction diagram
-
peptide of the gastrointestinal tract
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
?
Glucagon + H2O
?
show the reaction diagram
-
peptide of the gastrointestinal tract
-
?
GRP-(14-27) + H2O
?
show the reaction diagram
-
peptide of the gastrointestinal tract
-
?
Insulin B-chain + H2O
?
show the reaction diagram
-
4 cleavage sites (2 major and 2 minor): His5-Leu6, Leu6-Cys(SO3-)7, Ala14-Leu15, Cys(SO3-)19-Gly20
-
-
-
Insulin B-chain + H2O
?
show the reaction diagram
-
yielding at least 7 product peptides
-
-
-
Insulin B-chain + H2O
?
show the reaction diagram
-
mouse enzyme
-
-
-
interleukin-1beta precursor + H2O
interleukin-1beta + ?
show the reaction diagram
Q16820
proteolytic cleavage to a biologically active form
-
-
?
N-Benzoyl-Tyr 4-aminobenzoate + H2O
?
show the reaction diagram
-
rat or human enzyme, cleaves arylamide bond
-
-
-
neuropeptide Y + H2O
?
show the reaction diagram
-
peptide of the gastrointestinal tract
-
?
orcokinin + H2O
?
show the reaction diagram
-
-
-
?
orcokinin + H2O
?
show the reaction diagram
-
peptide of the gastrointestinal tract
-
?
osteopontin + H2O
?
show the reaction diagram
-
peptide of the gastrointestinal tract
-
?
sCCK8NH2 + H2O
?
show the reaction diagram
-
peptide of the gastrointestinal tract
-
?
Secretin + H2O
?
show the reaction diagram
-
peptide of the gastrointestinal tract
-
?
Succinyl-Ala-Ala-Ala 4-methylcoumarin 7-amide + H2O
?
show the reaction diagram
-
-
-
-
-
Succinyl-Ala-Ala-Val-Ala 4-nitroanilide + H2O
?
show the reaction diagram
-
-
-
-
-
tenascin-C + H2O
?
show the reaction diagram
-
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
-
-
?
tenascin-C + H2O
tenascin-C peptide fragments
show the reaction diagram
-
mapping of proteolytic fragments generated by meprinbeta from the chicken tenascin-C and the human recombinant 250 kDa TN-C variant. In chicken tenascin-C, meprinbeta processes all three major splicing variants by removal of 10 kDa N-terminal and 38 kDa C-terminal peptides, leaving a large central part of subunits intact. A similar cleavage pattern exists for large human tenascin-C variant where two N-terminal peptides of 10 and 15 kDa and two C-terminal fragments of 40 and 55 kDa are removed from the intact subunit. N-terminal sequencing reveals the exact amino acid positions of cleavage sites. In both chicken and human tenascin-C N-terminal cleavages occur just before and/or after the heptad repeats involved in subunit oligomerization. In the human protein, an additional cleavage site is identified in the alternative fibronectin type III repeat, and a unique cleavage by meprinbeta is located to the 7th constant fibronectin type III repeat in both chicken and human tenascin-C, cleavage at this site removes the C-terminal domain involved in its anti-adhesive activity
-
-
?
Tyr-Leu-Val-Cys(SO3-)-Gly-Glu-Arg-Gly + H2O
?
show the reaction diagram
-
synthetic octapeptide, derived from insulin B-chain
-
-
-
villin + H2O
?
show the reaction diagram
-
villin and actin bind to the cytoplasmic tail of meprin beta
-
-
?
Laminin + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
-
no substrates are nitrobradykinin
-
-
-
additional information
?
-
-
no substrates are nitrobradykinin
-
-
-
additional information
?
-
-
no substrates are glutaryl-Ala-Ala-Phe 4-methoxynaphthalamine 2-amide
-
-
-
additional information
?
-
-
member of astacin family
-
-
-
additional information
?
-
-
neurotensin is no substrate
-
?
additional information
?
-
Q16820
meprin B may play an important role in activation of the proinflammatory cytokine in various pathophysiological conditions
-
-
-
additional information
?
-
-
meprin beta is likely to contribute to leukocyte transmigration events important to intestinal immune responses
-
-
-
additional information
?
-
-
the alpha/beta isoform is deleterious in case of ischemia-reperfusion, overview
-
-
-
additional information
?
-
-, Q5RHM1, Q5RHM2, Q5RKM1
residues of the alpha1 subunit involved in the active site are Asp61 and Arg150, catalytic domain structure, overview
-
-
-
additional information
?
-
-, Q5RHM1, Q5RHM2, Q5RKM1
residues of the alpha2 subunit involved in the active site are Glu80 and Lys122, catalytic domain structure, overview
-
-
-
additional information
?
-
-, Q5RHM1, Q5RHM2, Q5RKM1
the residue of the beta subunit involved in the active site is Lys123, catalytic domain structure, overview
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
meprin interacts with epithelial Na+ channel (ENaC)
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
tenascin-C + H2O
?
show the reaction diagram
-
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
-
-
?
additional information
?
-
Q16820
meprin B may play an important role in activation of the proinflammatory cytokine in various pathophysiological conditions
-
-
-
additional information
?
-
-
meprin beta is likely to contribute to leukocyte transmigration events important to intestinal immune responses
-
-
-
additional information
?
-
-
the alpha/beta isoform is deleterious in case of ischemia-reperfusion, overview
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
meprin interacts with epithelial Na+ channel (ENaC)
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Zn2+
-
zinc-dependent endopeptidase
Zn2+
-
zinc-metalloendopeptidase
Zn2+
-, Q5RHM1, Q5RHM2, Q5RKM1
a zinc metalloprotease with the zinc-binding motif HExxHxxGxxHE(or M); a zinc metalloprotease with the zinc-binding motif HExxHxxGxxHE(or M); a zinc metalloprotease with the zinc-binding motif HExxHxxGxxHE(or M); a zinc metalloprotease with the zinc-binding motif HExxHxxGxxHE(or M)
Zn2+
-
zinc-metalloprotease
additional information
-
metalloendopeptidase according to inhibition profile
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
strong
2-mercaptoethanol
-
-
actinonin
-
-
actinonin
-
in vivo inhibition of meprins by actinonin exacerbates some parameters of renal injury in mice afflicted with anti-glomerular basement membrane antibody-associated nephritis
actinonin
-
-
Pro-Leu-Gly-hydroxamate
-
-
additional information
-
compound E-64; phosphoramidon, iodoacetic acid, 3,4-dichloroisocoumarin or soybean trypsin inhibitor
-
additional information
-
no inhibition by captopril, PMSF, pepstatin; phosphoramidon, iodoacetic acid, 3,4-dichloroisocoumarin or soybean trypsin inhibitor
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Trypsin
-
activation, 5-20fold; by limited proteolysis (2 h at 37C, with tosyl-Phe chloromethyl ketone treated trypsin, in 20 mM Tris-HCl buffer, pH 7.5); only with larger substrates (azocasein or insulin B), not smaller substrates
-
Trypsin
-
by limited proteolysis (2 h at 37C, with tosyl-Phe chloromethyl ketone treated trypsin, in 20 mM Tris-HCl buffer, pH 7.5); only with larger substrates (azocasein or insulin B), not smaller substrates
-
Trypsin
-
activation is accompanied by reduction in size of 8 kDa; by limited proteolysis; peptidase activity of expressed meprin B precursor is absolutely dependent on activation by trypsin
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00073
-
Actin
-
pH 7.5, 37C
-
0.282
-
alpha-MSH
-
pH 7.5, 37C, mutant K185Y
0.00104
-
bradykinin
-
pH 7.5, 37C
0.211
-
cholecystokinin 8 sulfate
-
pH 7.5, 37C
0.22
-
cholecystokinin 8 sulfate
-
pH 7.5, 37C, mutant K185Y
0.0071
-
gastrin
-
pH 7.5, 37C
0.00104
-
gastrin 17
-
pH 7.5, 37C, 150 mM NaCl
0.0185
-
gastrin 17
-
pH 7.5, 37C, 500 mM NaCl
0.02
-
gastrin 17
-
pH 7.5, 37C, 150 mM NaCl, mutant K185Y
0.0296
-
gastrin 17
-
pH 7.5, 37C, 500 mM NaCl, mutant K185Y
0.22
-
Glucagon
-
pH 7.5, 37C
0.0481
-
GRP-(14-27)
-
pH 7.5, 37C
0.1
-
orcokinin
-
pH 7.5, 37C
-
0.211
-
sCCK8NH2
-
pH 7.5, 37C
-
0.00117
-
villin
-
pH 7.5, 37C
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.625
-
Actin
-
pH 7.5, 37C
-
15
-
alpha-MSH
-
pH 7.5, 37C, mutant K185Y
11
-
bradykinin
-
pH 7.5, 37C
13.9
-
cholecystokinin 8 sulfate
-
pH 7.5, 37C
15
-
cholecystokinin 8 sulfate
-
pH 7.5, 37C, mutant K185Y
12.4
-
gastrin
-
pH 7.5, 37C
10.5
-
gastrin 17
-
pH 7.5, 37C, 500 mM NaCl, mutant K185Y
11
-
gastrin 17
-
pH 7.5, 37C, 150 mM NaCl
11.1
-
gastrin 17
-
pH 7.5, 37C, 500 mM NaCl
17.8
-
gastrin 17
-
pH 7.5, 37C, 150 mM NaCl, mutant K185Y
15.9
-
Glucagon
-
pH 7.5, 37C
26.8
-
Glucagon
-
pH 7.5, 37C
12.6
-
GRP-(14-27)
-
pH 7.5, 37C
23.4
-
orcokinin
-
pH 7.5, 37C
-
13.9
-
sCCK8NH2
-
pH 7.5, 37C
-
150
-
villin
-
pH 7.5, 37C
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
860
-
Actin
-
pH 7.5, 37C
0
128200
-
villin
-
pH 7.5, 37C
0
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.367
0.467
-
Tyr-Leu-Val-Cys(SO3-)-Gly-Glu-Arg-Gly as substrate
1.82
-
-
insulin B-chain as substrate
additional information
-
-
0.4763 mg azocasein/min mg protein
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-, Q5RHM1, Q5RHM2, Q5RKM1
-
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-, Q5RHM1, Q5RHM2, Q5RKM1
-
Manually annotated by BRENDA team
-, Q5RHM1, Q5RHM2, Q5RKM1
-
Manually annotated by BRENDA team
-, Q5RHM1, Q5RHM2, Q5RKM1
-
Manually annotated by BRENDA team
-
brush border membrane
Manually annotated by BRENDA team
-
proximal tubules, high expression level
Manually annotated by BRENDA team
-, Q5RHM1, Q5RHM2, Q5RKM1
-
Manually annotated by BRENDA team
Mus musculus male ICR
-
brush border membrane
-
Manually annotated by BRENDA team
-
leukocytes of mesenteric lymph node, leukocytes of the draining lymph node of the intestine
Manually annotated by BRENDA team
-, Q5RHM1, Q5RHM2, Q5RKM1
intestinal; intestinal; intestinal; intestinal
Manually annotated by BRENDA team
-, Q5RHM1, Q5RHM2, Q5RKM1
-
Manually annotated by BRENDA team
-, Q5RHM1, Q5RHM2, Q5RKM1
-
Manually annotated by BRENDA team
-
meprin beta is expressed in leukocytes of the draining lymph node of the intestine, regardless of the inflammatory status of the animal
Manually annotated by BRENDA team
-
cortical and medullary macrophages of lymph node
Manually annotated by BRENDA team
-, Q5RHM1, Q5RHM2, Q5RKM1
-
Manually annotated by BRENDA team
Mus musculus C57BL
-
-
-
Manually annotated by BRENDA team
-
leukocytes and cortical and medullary macrophages, the enzyme is not decreased during intestinal inflammation
Manually annotated by BRENDA team
additional information
-
tissue distribution of mRNA
Manually annotated by BRENDA team
additional information
Mus musculus C57BL
-
tissue distribution of mRNA
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
renal brush-border membrane
Manually annotated by BRENDA team
-
membrane anchor: COOH-terminal hydrophobic domain; renal brush-border membrane
Manually annotated by BRENDA team
-
microvillar membrane, integral membrane protein
Manually annotated by BRENDA team
Mus musculus C57BL
-
membrane anchor: COOH-terminal hydrophobic domain; renal brush-border membrane
-
Manually annotated by BRENDA team
Mus musculus male ICR
-
renal brush-border membrane
-
Manually annotated by BRENDA team
additional information
-
cell surface endopeptidase
-
Manually annotated by BRENDA team
additional information
Mus musculus male ICR
-
cell surface endopeptidase
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
76100
-
-
homooligomeric isoform, active, monomer, MALDI-TOF mass spectroscopy
85500
-
-
homooligomeric isoform, latent, monomer, MALDI-TOF mass spectroscopy
154000
-
-
homooligomeric isoform, active, dimer, MALDI-TOF mass spectroscopy
171000
-
-
homooligomeric isoform, latent, dimer, MALDI-TOF mass spectroscopy
additional information
-
-
amino acid composition and secondary structure similar to meprin A
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-, Q5RHM1, Q5RHM2, Q5RKM1
x * 73000, SDS-PAGE; x * 73000, SDS-PAGE; x * 73000, SDS-PAGE; x * 73000, SDS-PAGE
oligomer
-
x * 90000, mouse, SDS-PAGE under reducing or non-reducing conditions
oligomer
-
x * 74000, rat, deglycosylated enzyme, SDS-PAGE under reducing conditions; x * 84000, rat, expressed in human kidney 293 cells, deglycosylated form, SDS-PAGE under reducing conditions; x * 97000, rat, expressed in human kidney 293 cells, SDS-PAGE under reducing conditions
oligomer
-
-
oligomer
-
homooligomer
oligomer
Mus musculus male ICR
-
x * 90000, mouse, SDS-PAGE under reducing or non-reducing conditions
-
dimer
-
a model of the meprin B dimer structure is proposed that provides insight into the relationship between structure and function of thus isoforms
additional information
-
the enzyme is formed by alpha and/or beta subunits, the alpha/beta isoform is deleterious in case of ischemia-reperfusion, overview
additional information
-, Q5RHM1, Q5RHM2, Q5RKM1
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; 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; 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; 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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-, Q5RHM1, Q5RHM2, Q5RKM1
-
glycoprotein
-
-
glycoprotein
Mus musculus male ICR
-
-
-
glycoprotein
-
N-glycosidase F-sensitive
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
58
-
-
t1/2: 2.5 min, less stable than meprin A
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-
Q16820
recombinant soluble tail switch mutant pro-meprinbeta from BT1-TN-5B1-4 insect cells by nickel affinity chromatography after activation to meprinbeta by trypsin, trypsin is removed by chicken ovomucoid affinity chromatography
-
C3H/He mouse; papain-solubilized
-
papain-solubilized
-
expressed in human kidney cell line 293, papain-solubilized
-
purified from stably transfected human embryonic kidney HEK-293 cells
-
recombinant His-tagged enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4 genes encoding alpha and beta subunits of the enzyme are located on chromosome 20, DNA and amino acid sequence determination and anaylsis, phylogenetic tree, sequence comparisons, overview; 4 genes encoding alpha and beta subunits of the enzyme are located on chromosome 20, DNA and amino acid sequence determination and anaylsis, phylogenetic tree, sequence comparisons, overview; 4 genes encoding alpha and beta subunits of the enzyme are located on chromosome 20, DNA and amino acid sequence determination and anaylsis, phylogenetic tree, sequence comparisons, overview; 4 genes encoding alpha and beta subunits of the enzyme are located on chromosome 20, DNA and amino acid sequence determination and anaylsis, phylogenetic tree, sequence comparisons, overview
-, Q5RHM1, Q5RHM2, Q5RKM1
expression of mepbetaDELTATM, meprin beta coding region lacking the transmembrane and intracellular domains with V5 and hexahistidine C-terminal tags (termed as mepbetaDELTATM) in HEK-293F cells
Q16820
expression of the soluble tail switch mutant pro-meprinbeta in BT1-TN-5B1-4 insect cells using the baculovirus transfection system
-
analysis of expression level of meprinbeta in high IgA mouse (time dependent)
-
mouse, Mep-1beta structural gene, localized to chromosome 18
-
homooligomeric meprin B produced by transfecting cells with alpha or beta cDNA
-
rat, expressed in human kidney cell line 293, the expressed protein displays no detectable peptidase activity unless it is activated by removal of amino-terminal prosequence by limited trypsin digestion
-
recombinant His-tagged enzyme, cDNA transfected into human embryonic kidney 293 cells
-
recombinantly expressed
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K185Y
-
site-directed mutagenesis
additional information
-
homozygous knockout mice deficient in beta-subunit are produced from wild-type C57BL/6 mice with 129/Sv F2 embryonic stem cells and subjected to ischemia-reperfusion, they show a higher susceptability to renal injury, while wild-type mice show rapid redistribution of meprin beta-subunits in proximal tubule cells, overview
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
results suggest that meprinbeta may play a protective role against the progression of renal injury through the degradation of extracellular matrix and bioactive peptides