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Information on EC 3.4.24.63 - meprin B and Organism(s) Rattus norvegicus and UniProt Accession P28826

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.63 meprin B
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This record set is specific for:
Rattus norvegicus
UNIPROT: P28826 not found.
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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, meprin b, metalloprotease meprin, meprinbeta, meprin-beta, cell surface sheddase, mouse meprin beta, metalloproteinase meprin beta, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Meprin b
meprin B metalloprotease
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
150679-52-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
interleukin-6 + H2O
?
show the reaction diagram
2-aminobenzoyl-MGWMDEIDK(2,4-dinitrophenyl)SG + H2O
2-aminobenzoyl-MGWM + DEIDK(2,4-dinitrophenyl)SG
show the reaction diagram
-
-
-
?
actin + H2O
?
show the reaction diagram
-
villin and actin bind to the cytoplasmic tail of meprin beta
-
-
?
azocasein + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
bradykinin + H2O
?
show the reaction diagram
-
-
-
?
Cholecystokinin + H2O
?
show the reaction diagram
-
-
-
?
N-Benzoyl-Tyr 4-aminobenzoate + H2O
?
show the reaction diagram
-
rat or human enzyme, cleaves arylamide bond
-
-
?
orcokinin + H2O
?
show the reaction diagram
-
-
-
?
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
-
-
-
-
?
villin + H2O
?
show the reaction diagram
-
villin and actin bind to the cytoplasmic tail of meprin beta
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
-
zinc-dependent endopeptidase
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
a common inhibitor of several astacin metalloproteases
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Trypsin
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00073
actin
-
pH 7.5, 37°C
0.00104
bradykinin
-
pH 7.5, 37°C
0.00117
villin
-
pH 7.5, 37°C
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.625
actin
-
pH 7.5, 37°C
11
bradykinin
-
pH 7.5, 37°C
150
villin
-
pH 7.5, 37°C
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
860
actin
-
pH 7.5, 37°C
128200
villin
-
pH 7.5, 37°C
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 10
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
membrane-bound
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the enzyme encoded by Rmepb belongs to the BTP cluster of the astacin enzyme family. Structure-activity relationship of astacin metalloproteases, EDTA is used to dock into the active site cleft of the astacins to know the interaction network and to identify the important residues for binding, comparative three-dimensional structure homology modeling and docking study, and potential binding site, detailed overview
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
additional information
the hydrogen bonding residues of the enzyme are Cys125, Thr150, Tyr212, and His211, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 4GWN) and docking study, and potential binding site, detailed overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MEP1B_RAT
704
1
79236
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
154000
-
homooligomeric isoform, active, dimer, MALDI-TOF mass spectroscopy
171000
-
homooligomeric isoform, latent, dimer, MALDI-TOF mass spectroscopy
74000
-
x * 74000, deglycosylated enzyme, SDS-PAGE under reducing conditions
76100
-
homooligomeric isoform, active, monomer, MALDI-TOF mass spectroscopy
84000
-
x * 84000, expressed in human kidney 293 cells, deglycosylated form, SDS-PAGE under reducing conditions
85500
-
homooligomeric isoform, latent, monomer, MALDI-TOF mass spectroscopy
97000
-
x * 97000, expressed in human kidney 293 cells, SDS-PAGE under reducing conditions
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
a model of the meprin B dimer structure is proposed that provides insight into the relationship between structure and function of thus isoforms
oligomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
activation of recombinant zymogen enzyme by trypsin
glycoprotein
-
N-glycosidase F-sensitive
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged meprin beta protein (1-648) from human HEK-293 cells by metal-chelating affinity chromatography
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
LITERATURE
gene Mep1B, sequence comparisons
recombinant expression of C-terminally His6-tagged meprin beta protein (1-648) in human HEK-293 cells
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
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wolz, R.L.; Bond, J.S.
Meprins A and B
Methods Enzymol.
248
325-345
1995
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Johnson, G.D.; Hersh, L.B.
Expression of meprin subunit precursors. Membrane anchoring through the beta subunit and mechanism of zymogen activation
J. Biol. Chem.
269
7682-7688
1994
Rattus norvegicus
Manually annotated by BRENDA team
Bertenshaw, G.P.; Villa, J.P.; Hengst, J.A.; Bond, J.S.
Probing the active sites and mechanisms of rat metalloproteases meprin A and B
Biol. Chem.
383
1175-1183
2002
Rattus norvegicus
Manually annotated by BRENDA team
Bertenshaw, G.P.; Norcum, M.T.; Bond, J.S.
Structure of homo- and hetero-oligomeric meprin metalloproteases
J. Biol. Chem.
278
2522-2532
2003
Rattus norvegicus
Manually annotated by BRENDA team
Ishmael, F.T.; Shier, V.K.; Ishmael, S.S.; Bond, J.S.
Intersubunit and domain interactions of the meprin B metalloproteinase. Disulfide bonds and protein-protein interactions in the MAM and TRAF domains
J. Biol. Chem.
280
13895-13901
2005
Rattus norvegicus
Manually annotated by BRENDA team
Ongeri, E.M.; Anyanwu, O.; Reeves, W.B.; Bond, J.S.
Villin and actin in the mouse kidney brush-border membrane bind to and are degraded by meprins, an interaction that contributes to injury in ischemia-reperfusion
Am. J. Physiol. Renal Physiol.
301
F871-F882
2011
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Keiffer, T.R.; Bond, J.S.
Meprin metalloproteases inactivate interleukin 6
J. Biol. Chem.
289
7580-7588
2014
Homo sapiens (Q16820), Homo sapiens, Rattus norvegicus (P28826)
Manually annotated by BRENDA team
Chaudhuri, A.; Chakraborty, S.
Structure-activity relationship of astacin metalloproteases A comparative study using EDTA
Curr. Enzyme Inhib.
14
131-140
2018
Rattus norvegicus (P28826), Mus musculus (Q61847)
-
Manually annotated by BRENDA team