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Information on EC 3.4.24.18 - meprin A and Organism(s) Mus musculus and UniProt Accession P28825
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3.4.24.18 meprin ASpecify your search results
Word Map
- 3.4.24.18
-
3.4.24.11
- enkephalinase
- metalloendopeptidase
- atrial
- phosphoramidon
-
natriuretic
- enkephalin
- thiorphan
-
angiotensin-converting
- angiotensin
- astacins
- metalloproteases
-
brush
- bradykinin
-
3.4.15.1
- captopril
- neprilysin
- metallopeptidases
- anp
- aminopeptidases
- acetorphan
-
math
- endopeptidases
-
brush-border
- microvillar
- actinonin
- calla
- bestatin
- amastatin
- azocasein
-
phosphoramidon-sensitive
- sheddase
-
dipeptidylaminopeptidase
-
metzincins
- pharmacology
- neurokinins
-
astacin-like
-
met5enkephalin
-
depressor
- medicine
- tachykinins
- neurotensin
- leu-enkephalin
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Hydrolysis of protein and peptide substrates preferentially on carboxyl side of hydrophobic residues
Synonyms
meprin, meprin a, mep1a, meprin alpha, meprin beta, meprin-a, meprin-alpha, endopeptidase-2, pph alpha, mouse meprin alpha, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E-24.18
-
-
-
-
Endopeptidase-2
-
-
-
-
Meprin
-
-
-
-
Meprin-a
-
-
-
-
N-Benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase
-
-
-
-
PABA peptide hydrolase
-
-
-
-
PABA-peptide hydrolase
-
-
-
-
PPH
-
-
-
-
PPH alpha
-
-
-
-
PPH beta
-
-
-
-
additional information
-
meprin A from mouse, endopeptidase-2 from rat and PPH from human are closely related enzymes of the astacin family
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
hydrolysis of arylamide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
148938-24-3
-
SUBSTRATE
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
2-aminobenzoyl-Arg-Gly-Pro-Phe-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Gly-Pro-Phe + Ser-Pro-(4-nitro)Phe-Arg
2-aminobenzoyl-Arg-Hyp-Gly-Phe-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Hyp-Gly-Phe + Ser-Pro-(4-nitro)Phe-Arg
2-aminobenzoyl-Arg-Pro-Gly-Ala-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Pro-Gly-Ala + Ser-Pro-(4-nitro)Phe-Arg
2-aminobenzoyl-Arg-Pro-Gly-Glu-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Pro-Gly-Glu + Ser-Pro-(4-nitro)Phe-Arg
2-aminobenzoyl-Arg-Pro-Gly-Leu-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Pro-Gly-Leu + Ser-Pro-(4-nitro)Phe-Arg
2-aminobenzoyl-Arg-Pro-Gly-Lys-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Pro-Gly + Lys-Ser-Pro-(4-nitro)Phe-Arg
2-aminobenzoyl-Arg-Pro-Ile-Phe-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Pro-Ile-Phe + Ser-Pro-(4-nitro)Phe-Arg
2-aminobenzoyl-RPPGFSPFRK-(dinitrophenyl)-G + H2O
?
-
fluorogenic bradykinin analog substrate
-
?
angiotensin I + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe + Ile-His-Pro-Phe-His-Leu
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu, cleavage site: Tyr-Ile
-
-
?
angiotensin III + H2O
Arg-Val-Tyr + Ile-His-Pro-Phe
-
i.e. Arg-Val-Tyr-Ile-His-Pro-Phe, cleavage site: Tyr-Ile
-
-
?
Arg-Pro-Pro-Gly-(4-nitro)Phe-Ala-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-(4-nitro)Phe + Ala-Pro-Phe-Arg
Arg-Pro-Pro-Gly-(4-nitro)Phe-Arg-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-(4-nitro)Phe + Arg-Pro-Phe-Arg
Arg-Pro-Pro-Gly-(4-nitro)Phe-Lys-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-(4-nitro)Phe + Lys-Pro-Phe-Arg
Arg-Pro-Pro-Gly-(4-nitro)Phe-Phe-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-(4-nitro)Phe + Phe-Pro-Phe-Arg
Arg-Pro-Pro-Gly-(4-nitro)Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-(4-nitro)Phe + Ser-Pro-Phe-Arg
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
-
-
?
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
-
-
?
gastri-releasing peptide-(14-27) + H2O
?
-
peptide of the gastrointestinal tract
-
?
protein kinase A + H2O
?
-
the enzyme cleaves at defined sites, isoform-specific interactions between the catalytic subunit of PKA (PKA C) and meprins, overview
-
-
?
protein kinase A catalytic subunit Cbeta1 + H2O
?
-
the enzyme cleaves at defined sites, cytosolic-enriched kidney proteins from meprin alphabeta double knockout mice, and purified forms of recombinant mouse PKA Calpha, Cbeta1, and Cbeta2, are incubated with activated forms of either homomeric meprinA or meprin B, EC 3.4.24.63, product analysis by mass spectrometry, overview. Meprin A only cleaves PKA Cbeta1
-
-
?
sCCK8NH2 + H2O
L-Asp-L-Tyr(SO3)-L-Met-Gly-L-Trp-L-Met + L-Asp-L-Phe
-
peptide of the gastrointestinal tract
-
?
Tyr-Leu-Val-Cys(SO3-)-Gly-Glu-Arg-Gly + H2O
?
-
synthetic peptide derived from insulin B-chain
-
-
?
Reelin + H2O
?
Reelin is a secreted glycoprotein whose function is regulated by proteolysis
-
-
?
Reelin + H2O
?
cleavage between Ala2688 and Asp2689, the specific cleavage site of Reelin called C-t is located approximately between the sixth and seventh Reelin repeat
-
-
?
2-aminobenzoyl-Arg-Gly-Pro-Phe-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Gly-Pro-Phe + Ser-Pro-(4-nitro)Phe-Arg
-
fluorogenic bradykinin analog substrate, cleavage site: Phe-Ser
-
?
2-aminobenzoyl-Arg-Gly-Pro-Phe-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Gly-Pro-Phe + Ser-Pro-(4-nitro)Phe-Arg
-
fluorogenic bradykinin analog substrate, cleavage site: Phe-Ser
-
?
2-aminobenzoyl-Arg-Hyp-Gly-Phe-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Hyp-Gly-Phe + Ser-Pro-(4-nitro)Phe-Arg
-
fluorogenic bradykinin analog substrate, cleavage site: Phe-Ser
-
?
2-aminobenzoyl-Arg-Hyp-Gly-Phe-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Hyp-Gly-Phe + Ser-Pro-(4-nitro)Phe-Arg
-
fluorogenic bradykinin analog substrate, cleavage site: Phe-Ser
-
?
2-aminobenzoyl-Arg-Pro-Gly-Ala-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Pro-Gly-Ala + Ser-Pro-(4-nitro)Phe-Arg
-
fluorogenic bradykinin analog substrate, cleavage site: Ala-Ser
-
?
2-aminobenzoyl-Arg-Pro-Gly-Ala-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Pro-Gly-Ala + Ser-Pro-(4-nitro)Phe-Arg
-
fluorogenic bradykinin analog substrate, cleavage site: Ala-Ser
-
?
2-aminobenzoyl-Arg-Pro-Gly-Glu-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Pro-Gly-Glu + Ser-Pro-(4-nitro)Phe-Arg
-
fluorogenic bradykinin analog substrate, cleavage site: Glu-Ser
-
?
2-aminobenzoyl-Arg-Pro-Gly-Glu-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Pro-Gly-Glu + Ser-Pro-(4-nitro)Phe-Arg
-
fluorogenic bradykinin analog substrate, cleavage site: Glu-Ser
-
?
2-aminobenzoyl-Arg-Pro-Gly-Leu-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Pro-Gly-Leu + Ser-Pro-(4-nitro)Phe-Arg
-
fluorogenic bradykinin analog substrate, cleavage sites: Leu-Ser (major site) and Gly-Leu
major products
?
2-aminobenzoyl-Arg-Pro-Gly-Leu-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Pro-Gly-Leu + Ser-Pro-(4-nitro)Phe-Arg
-
fluorogenic bradykinin analog substrate, cleavage sites: Leu-Ser (major site) and Gly-Leu
major products
?
2-aminobenzoyl-Arg-Pro-Gly-Lys-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Pro-Gly + Lys-Ser-Pro-(4-nitro)Phe-Arg
-
fluorogenic bradykinin analog substrate, cleavage sites: Gly-Lys (major site) and Lys-Ser
major products
?
2-aminobenzoyl-Arg-Pro-Gly-Lys-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Pro-Gly + Lys-Ser-Pro-(4-nitro)Phe-Arg
-
fluorogenic bradykinin analog substrate, cleavage sites: Gly-Lys (major site) and Lys-Ser
major products
?
2-aminobenzoyl-Arg-Pro-Ile-Phe-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Pro-Ile-Phe + Ser-Pro-(4-nitro)Phe-Arg
-
fluorogenic bradykinin analog substrates, cleavage site: Phe-Ser
-
?
2-aminobenzoyl-Arg-Pro-Ile-Phe-Ser-Pro-(4-nitro)Phe-Arg + H2O
2-aminobenzoyl-Arg-Pro-Ile-Phe + Ser-Pro-(4-nitro)Phe-Arg
-
fluorogenic bradykinin analog substrates, cleavage site: Phe-Ser
-
?
alpha-melanocyte stimulating hormone + H2O
?
-
i.e. acetyl-Ser-Tyr-Ser-Met-Gly-His-Phe-Arg-Trp-Gly-Lys-Pro-Val, cleavage sites: Ser-Met, Gly-Lys, mouse
-
-
?
alpha-melanocyte stimulating hormone + H2O
?
-
peptide of the gastrointestinal tract
-
?
alpha-melanocyte-stimulating hormone + H2O
?
-
murine homomeric recombinant enzyme
-
-
?
angiotensin II + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
poor substrate
-
?
angiotensin II + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
cleavage site: Tyr-Ile
-
?
angiotensin II + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
cleavage site: Tyr-Ile
-
-
?
angiotensin II + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
-
?
angiotensin II + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
-
-
?
Arg-Pro-Pro-Gly-(4-nitro)Phe-Ala-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-(4-nitro)Phe + Ala-Pro-Phe-Arg
-
chromogenic bradykinin analog
-
?
Arg-Pro-Pro-Gly-(4-nitro)Phe-Ala-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-(4-nitro)Phe + Ala-Pro-Phe-Arg
-
chromogenic bradykinin analog
-
?
Arg-Pro-Pro-Gly-(4-nitro)Phe-Arg-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-(4-nitro)Phe + Arg-Pro-Phe-Arg
-
chromogenic bradykinin analog
-
?
Arg-Pro-Pro-Gly-(4-nitro)Phe-Arg-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-(4-nitro)Phe + Arg-Pro-Phe-Arg
-
chromogenic bradykinin analog
-
?
Arg-Pro-Pro-Gly-(4-nitro)Phe-Lys-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-(4-nitro)Phe + Lys-Pro-Phe-Arg
-
chromogenic bradykinin analog
-
?
Arg-Pro-Pro-Gly-(4-nitro)Phe-Lys-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-(4-nitro)Phe + Lys-Pro-Phe-Arg
-
chromogenic bradykinin analog
-
?
Arg-Pro-Pro-Gly-(4-nitro)Phe-Phe-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-(4-nitro)Phe + Phe-Pro-Phe-Arg
-
chromogenic bradykinin analog
-
?
Arg-Pro-Pro-Gly-(4-nitro)Phe-Phe-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-(4-nitro)Phe + Phe-Pro-Phe-Arg
-
chromogenic bradykinin analog
-
?
Arg-Pro-Pro-Gly-(4-nitro)Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-(4-nitro)Phe + Ser-Pro-Phe-Arg
-
i.e. nitrobradykinin, chromogenic bradykinin analog
-
?
Arg-Pro-Pro-Gly-(4-nitro)Phe-Ser-Pro-Phe-Arg + H2O
Arg-Pro-Pro-Gly-(4-nitro)Phe + Ser-Pro-Phe-Arg
-
i.e. nitrobradykinin, chromogenic bradykinin analog
-
?
azocasein + H2O
fragments of azocasein
-
excellent substrate for mouse, poorer substrate for rat and human enzymes
-
-
?
azocasein + H2O
fragments of azocasein
-
better substrate for mouse enzyme than for rat enzyme
-
-
?
bradykinin + H2O
Arg-Pro-Pro-Gly + Phe-Ser-Pro-Phe-Arg
-
one cleavage site: Phe-Ser
-
-
?
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
prevalent cleavage sites are Gly20-Glu21, Phe24-Phe25 and Phe25-Tyr26
-
-
?
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
prevalent cleavage sites are Gly20-Glu21, Phe24-Phe25 and Phe25-Tyr26
15 different peptide fragments
?
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
the others are Leu6-Cys(SO3-)7, Ala14-Leu15, Gly8-Ser9, His10-Leu11, Leu15-Tyr16, His5-Leu6 and Leu17-Val18
13 different peptide fragments
?
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
10 cleavage sites
15 different peptide fragments
?
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
7 major and 3 minor sites
-
-
?
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
oxidized form
15 different peptide fragments
?
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
oxidized form
13 different peptide fragments
?
interleukin-6 + H2O
?
-
recombinant human substrate expressed in an eukaryotic cell line, inactivation
-
-
?
interleukin-6 + H2O
?
-
recombinant murine substrate expressed in Escherichia coli, inactivation. The enzyme cleaves 90% of the substrate within 2 h, approximately 50 and 15% of the mIL-6 signal remain after 0.5 and 1 h of incubation with mouse meprin A, fragmentation pattern, overview
-
-
?
luteinizing hormone releasing hormone LHRH + H2O
?
-
peptide of the gastrointestinal tract
-
?
luteinizing-hormone-releasing hormone + H2O
?
-
murine homomeric recombinant enzyme
-
-
?
neurotensin + H2O
?
-
i.e. pyro-Glu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu, mouse, rat, cleavage sites: Glu-Asn, Asn-Lys
-
-
?
occludin + H2O
?
-
recombinant substrate in micelles and recombinant enzyme, cleavage products of extracellular loop 1 and loop 2 are determined by mass spectrometry, overview. The cleavage site is between Gly100 and Ser101 is on the first extracellular loop of occludin
-
-
?
parathyroid hormone fragment 13-34 + H2O
?
-
peptide of the gastrointestinal tract
-
?
procollagen I + H2O
collagen I + propeptide of collagen III
-
meprin alpha 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
-
-
?
procollagen I + H2O
collagen I + propeptide of collagen III
-
recombinant human substrate, generation of mature collagen molecules that spontaneously assemble into collagen fibrils
-
-
?
Vasoactive intestinal peptide + H2O
?
-
peptide of the gastrointestinal tract
-
?
additional information
?
-
meprin alpha, but not meprin beta, cleaves Reelin in which Asp2689 is replaced with Lys (Reelin-DK mutant)
-
-
?
additional information
?
-
-
little or no activity towards benzoylarginine 2-naphthylamide, benzoylglycylarginine, benzyloxycarbonyl-Glu-Tyr, acetyl-Phe 2-naphthylester
-
-
?
additional information
?
-
-
no hydrolysis of Leu 4-nitroanilide, benzoyl-Arg-4-nitroanilide, succinyl-Ala 4-nitroanilide, Arg 4-methylcoumarinin 7-amide, benzoyl-Phe-Val-Arg 4-methylcoumarin 7-amide, Gly-Gly-Phe-Leu, Tyr-Gly-Gly-Phe-Leu, Tyr-Gly-Gly-Phe-Met, Leu-Arg-Arg-Ala-Ser-Leu-Gly, Ala-Phe-Pro-Leu-Gly-Phe, benzoyl-Phe-Val-Arg
-
-
?
additional information
?
-
-
hydrolyzes peptides of at least 8 amino acids and prefers peptide bonds flanked by hydrophobic or neutral amino acid residues although hydrolysis is not limited to these bonds
-
-
?
additional information
?
-
-
orcokinin and gastrin 17 are no substrates
-
?
additional information
?
-
-
orcokinin, gastrin 17, peptide YY, kinetensin, [Lys8]-vasopressin, somatostatin, kassinin, oxytocin, and alpha-neurokinin are no substrates
-
?
additional information
?
-
-
cleaves growth factors, extracellular matrix proteins, and biological active peptides
-
?
additional information
?
-
-
the enzyme is capable of hydrolyzing and processing a large number of substrates, including extracellular matrix proteins, cytokines, adherens junction proteins, hormones, bioactive peptides, and cell surface proteins
-
-
?
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
Reelin + H2O
?
Reelin is a secreted glycoprotein whose function is regulated by proteolysis
-
-
?
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
-
-
?
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
-
-
?
procollagen I + H2O
collagen I + propeptide of collagen III
-
meprin alpha 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
-
-
?
protein kinase A + H2O
?
-
the enzyme cleaves at defined sites, isoform-specific interactions between the catalytic subunit of PKA (PKA C) and meprins, overview
-
-
?
additional information
?
-
-
cleaves growth factors, extracellular matrix proteins, and biological active peptides
-
?
additional information
?
-
-
the enzyme is capable of hydrolyzing and processing a large number of substrates, including extracellular matrix proteins, cytokines, adherens junction proteins, hormones, bioactive peptides, and cell surface proteins
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Calcium
Zinc
Zn2+
additional information
additional information
-
considerable stimulation of azocasein hydrolysis at ionic strength values up to 0.15-0.2
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
actinonin
-
i.e. 3-[[1-[[2-(hydroxymethyl)-1-pyrolidinyl]carbonyl]-2-methylpropyl]carbamoyl]octano hydroxamic acid, strong, kinetics
actinonin
-
in a mouse model of sepsis induced by cecal ligation puncture that results in elevated levels of serum interleukin 1beta, meprin inhibitor actinonin significantly reduces levels of serum interleukin 1beta
actinonin
-
a hydroxamate derivate and naturally occurring compound produced in actinomycetes. Hydroxamate inhibitors chelate the zinc ion in the active site
additional information
-
diisopropyl phosphofluoridate, p-hydroxymercuribenzoate, phenylmercurisulfonate, antipain, cystine, oxidized glutathione
-
additional information
-
L-trans-epoxysuccinyl-leucylamido-(4-guanidino)-butane (i.e. E-64)
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
contrary to meprin B only very little activation by trypsin treatment
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0223
alpha-MSH
-
meprin A hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 between 8-30 min
0.156
luteinizing hormone releasing hormone LHRH
-
meprin A hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 for between 8-30 min
-
0.0296
protein GRP
-
meprin A hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 between 8-30 min
-
0.0672
protein PTH12-34
-
meprin A hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 between 8-30 min
0.111
secretin
-
meprin A hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 between 8-30 min
additional information
additional information
-
Michaelis-Menten enzyme kinetics, overview
-
0.101
bradykinin
-
meprin A hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 between 8-30 min
0.0306
Substance P
-
meprin A hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 between 8-30 min
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
4.6673 mg azocasein/min/mg (untreated enzyme), 7.2512 mg azocasein/min/mg (trypsin-treated enzyme)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
pI: multiple bonds in the range of 4-5, presumably due to glycosylation
additional information
-
pI: multiple bonds in the range of 4-5, presumably due to glycosylation
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
meprin A distribution in the mouse kidney, immunolacalization, overview
-
the enzyme is abundantly expressed in the brush border membranes of kidney proximal tubules. Localization of meprin A in the glomeruli of diabetic kidneys
additional information
-
tissue distribution (immuno-peroxidase staining), not in brain or spinal cord
additional information
-
co-localization of the enzyme with serum-type mannan-binding protein and C3b on both the cortex and the medulla in the renal I/R-operated mouse kidney, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
brush-border membranes of proximal tubules and intestines
-
meprin alpha is constitutively shed by furin during the secretory pathway and secreted into extracellular space. Meprin alpha tends to oligomerize to huge complexes ring and chain like structures up to the mega Dalton range, which makes it the largest extracellular protease
-
-
cell surface metalloproteinase, alphabeta-heterodimers firmly attached to brush border membrane, alpha2-homodimers only associated with membrane
-
beta subunits are type I integral membrane proteins and alpha subunits are disulfide linked to or non-covalently associated with membrane-anchored meprin beta subunits
-
meprin A, is a membrane-associated neutral metalloendoprotease. Importance of a sheddase involved in the release of membrane-associated meprin A under pathological conditions
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme encoded by Mmepa 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
physiological function
actinonin, a meprin alpha and meprin beta (EC 3.4.24.63) inhibitor, does not inhibit the Reelin-cleaving activity of cerebellar granular neurons (CGN) and the amount of Reelin fragments in brains of meprin beta knock-out mice is not significantly different from that of the wild-type, indicating that meprin beta does not play a major role in Reelin cleavage under basal conditions. Meprin alpha and meprin beta probably join the modulators of Reelin signalling as they cleave Reelin at a specific site and are upregulated under specific pathological conditions
evolution
malfunction
metabolism
physiological function
additional information
the hydrogen bonding residues of the enzyme are Thr151 and Leu210, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 4GWN) and docking study, and potential binding site, detailed overview
evolution
-
meprin A, is a membrane-associated neutral metalloendoprotease that belongs to the astacin family of zinc endopeptidases
evolution
-
meprin metalloproteases belong to the astacin family of zinc endopeptidases and the metzincin superfamily
malfunction
-
meprin inhibition elevates levels of natriuretic peptides in plasma and the vascular wall, decreases plaque volume and suppresses lipid deposition in carotid arteries, reduces production of reactive oxygen species and apoptosis (which are associated with atherosclerosis) in the vascular wall, and increases natriuretic peptide function on cell apoptosis, proliferation, and intracellular reactive oxygen species generation in the THP-1 cell line and primary vascular smooth muscle cells
malfunction
-
altered localization and shedding of meprin A in places other than the apical membranes may be deleterious in vivo in acute tubular injury. Importance of a sheddase involved in the release of membrane-associated meprin A under pathological conditions
malfunction
-
enzyme-deficient mice show lower amounts of mature collagen I compared with wild-type mice and exhibit significantly reduced collagen deposition in skin, along with markedly decreased tissue tensile strength
malfunction
-
meprin alpha knock-out mice exhibit decreased collagen deposition in skin resulting in impaired tensile strength, overview. Overexpression of meprin metalloproteases occurs under fibrotic conditions in the skin (keloids) and the lung (pulmonary hypertension)
malfunction
-
mice lacking meprin alpha and meprin beta are significantly protected against renal ischaemia/reperfusion injury and bladder inflammation. Meprin alpha-knockout mice exhibit less renal damage compared with wild-type mice
malfunction
-
monocytes from meprin knockout mice on a C57BL/6 background are less able to migrate through an MDCK cell monolayer than monocytes from their wild-type counterparts
metabolism
-
following ischemia-reperfusion- and cisplatin-induced acute kidney injury, meprin A is redistributed toward the basolateral plasma membrane, and the cleaved form of meprin A is excreted in the urine
metabolism
-
meprins show higher substrate and cleavage specificity compared to matrix metalloproteases
metabolism
-
role of interaction of mannan-binding protein with meprins at the initial step of complement activation in ischemia/reperfusion injury to mouse kidney. Co-localization of the enzyme with serum-type mannan-binding protein and C3b on both the cortex and the medulla in the renal I/R-operated mouse kidney
physiological function
-
meprin-alpha is capable of increasing lipopolysaccharide-induced production of cytokines in peripheral blood mononuclear cells, which is associated with the activation of nuclear factor-kappaB
physiological function
-
meprins may impact kidney injury, in part, via modulation of protein kinase A signaling pathways, meprins are implicated in ischemia-reperfusion-induced renal injury and diabetic nephropathy. Meprin cleavage decreases the kinase activity of protein kinase A subunits Calpha, Cbeta1, and Cbeta2
physiological function
-
physiological relevance of the unique ability of meprin alpha and meprin beta, EC 3.4.24.63, to remove the both the C- and N-propeptides of type I procollagen, subsequently releasing fibril-forming mature collagen molecules. The enzyme contributes to the integrity of connective tissue in skin
physiological function
-
serum-type mannan-binding protein interacts with meprins in vivo in the I/R-operated mouse kidney and initiates the complement activation through the interaction with meprins in vitro, overview
physiological function
-
the activity of meprin A enables monocytes to migrate through an epithelial barrier more readily allowing inflammatory molecules such as cytokines and monocytes to gain access to sites of injury. Meprin A impairs epithelial barrier function, enhances monocyte migration, and cleaves the tight junction protein occludin
physiological function
-
the enzyme is involved in inflammation by the release and maturation of cytokines and proteoglycans, it induces extracellular matrix assembly and fibrosis, and enhances cancer progression through transactivation of epidermal growth factor receptors. The cleavage of fibrillar procollagen by the enzyme is required and sufficient to induce collagen fibril assembly
physiological function
-
the metalloproteases meprin alpha and meprin beta are involved in inflammation, neurodegeneration, cancer and fibrosis, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MEP1A_MOUSE
747
1
84231
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
167000
-
mouse, native enzyme, sedimentation equilibrium centrifugation with 4 M guanidine-HCl
320000
-
mouse, gel filtration, SDS-PAGE in the absence of 2-mercaptoethanol
69000
-
x * 69000 + x * 79000, mouse, deglycosylated alpha and beta-subunit, SDS-PAGE in the presence of 2-mercaptoethanol
79000
-
x * 69000 + x * 79000, mouse, deglycosylated alpha and beta-subunit, SDS-PAGE in the presence of 2-mercaptoethanol
86000
90000
additional information
86000
-
x * 86000, mouse, performic acid oxidized enzyme, sedimentation equilibrium centrifugation with 4 M guanidine-HCl
additional information
-
amino acid sequence, domain structure and tertiary structure deduced from cDNAs
additional information
-
amino acid sequence of protease domain of meprin A compared to that of meprin B, EC 3.4.24.63
additional information
-
molecular weight above the highest marker 669000, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
tetramer
additional information
oligomer
-
x * 69000 + x * 79000, mouse, deglycosylated alpha and beta-subunit, SDS-PAGE in the presence of 2-mercaptoethanol
oligomer
-
x * 86000, mouse, performic acid oxidized enzyme, sedimentation equilibrium centrifugation with 4 M guanidine-HCl
tetramer
-
disulfide-bridged dimers (alpha2 or alphabeta) aggregate non-covalently to form higher MW complexes, predominantly tetramers
additional information
-
the mouse enzyme is composed of disulfide linked dimers associating non-covalently to form tetramers and sometimes higher order oligomers
additional information
-
enzyme forms oligomers of ten or more subunits with intersubunit disulfide bonds and further association of subunits. No single glycan is essential for oligomer formation
additional information
-
meprin alpha is a multidomain metalloprotease, enzyme domain structure, overview. It tends to oligomerize to huge complexes ring and chain like structures up to the mega Dalton range, which makes it the largest extracellular protease. 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. Additionally, there is a so called inserted domain found in meprin alpha between the TRAF and the EGF like domain. This inserted domain is cleaved by furin resulting in secretion into extracellular space
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
glycoprotein
-
nine out of ten potential glycoslytation sites are glycosylated. Removal of two glycans at N234 and N270, as well as removal of glycan at N452, decrease the chemical and thermal stability of the homooligomer without affecting quarternary structure
proteolytic modification
-
meprins are secreted as zymogens and are activated by trypsin-like serine proteases
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N152Q/N270Q
-
no formation of intersubunit disulfide bonds and noncovalent association of subunits, loss of enzymatic activity
additional information
additional information
meprin A subunit alpha knock-out mice exhibit a more severe intestinal injury and inflammation than their wild-type counterparts following oral administration of dextran sulfate sodium
additional information
-
meprin A subunit alpha knock-out mice exhibit a more severe intestinal injury and inflammation than their wild-type counterparts following oral administration of dextran sulfate sodium
additional information
-
replacement of enzyme transmembrane and cytoplasmic domains, alphaT and alphaC, with their beta counterparts allows rapid movement of the alpha subunit to the cell surface. Enzyme alphaT and alphaC domains substituted into mephrin beta delayed movement of this chimera through the secretory pathway. Enzyme mutant C320ADELTAI, lacking a 56 amino acid inserted domain and unable to form disulfide bridges or higher order oligomers, is transported through the secretory pathway, but more slowly than mephrin beta
additional information
-
generation of knock-out mice deficient for meprin alpha, phenotype, overview
additional information
-
generation of meprin A deficient Mep1a-/- mice, phenotype overview. Maturation of type I procollagen is reduced in skin and primary fibroblasts from Mep1a?/? mice, the skin shows reduced tensile strength
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
-
wild-type enzyme retains 55% activity after 20 min, similar results for the mutants N41Q, N330Q, N426Q, N452Q, N546Q, and N553Q, mutants N234Q, N270Q, and N614Q retains 10% activity after 20 min, N152Q retains 6% activity after 5 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isolation of meprins from the mouse kidneys by immunoaffinity chromatography using mannan-binding protein resin
-
recombinant His6-tagged meprin alpha protein (1-615) from HEK-293 cells by metal-chelating affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
pcDNAI/Amp plasmid containing full-length wild-type meprin alpha-subunit cDNA transfected into MDCK cells and human embryonic kidney 293 cells
-
recombinant expression of C-terminally His6-tagged meprin alpha protein (1-615) in human HEK-293 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
meprin A subunit alpha knock-out mice exhibit a more severe intestinal injury and inflammation than their wild-type counterparts following oral administration of dextran sulfate sodium
medicine
pharmacology
-
in a mouse model of sepsis induced by cecal ligation puncture that results in elevated levels of serum interleukin 1beta, meprin inhibitor actinonin significantly reduces levels of serum interleukin 1beta
medicine
-
db/db mice lacking the hypothalamic leptin receptor, representing a model of type 2 diabetes mellitus, manifest decreased enzyme and meprin-beta gene and protein expression before the development of overt kidney disease. Inverse relationship between renal enzyme content and the severity of the renal injury. Treatment with an inhibitor of angiotensin-converting enzyme is more effective than ANG II receptor type I blocker therapy in ameliorating diabetic nephrosis
medicine
-
meprin inhibition is therapeutically useful in atherosclerosis prevention
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Beynon, R.J.; Shannon, J.D.; Bond, J.S.
Purification and characterization of a metallo-endoproteinase from mouse kidney
Biochem. J.
199
591-598
1981
Mus musculus
Butler, P.E.; McKay, M.J.; Bond, J.S.
Characterization of meprin, a membrane-bound metalloendopeptidase from mouse kidney
Biochem. J.
241
229-235
1987
Mus musculus
Dumermuth, E.; Sterchi, E.E.; Jiang, W.; Wolz, R.L.; Bond, J.S.; Flannery, A.V.; Beynon, R.J.
The astacin family of metalloendopeptidases
J. Biol. Chem.
266
21381-21385
1991
Homo sapiens, Homo sapiens PPH, Mus musculus
Barnes, K.; Ingram, J.; Kenny, A.J.
Proteins of the kidney microvillar membrane. Structural and immunochemical properties of rat endopeptidase-2 and its immunohistochemical localization in tissues of rat and mouse
Biochem. J.
264
335-346
1989
Mus musculus, Rattus norvegicus
Kounnas, M.Z.; Woltz, R.L.; Gorbea, C.M.; Bond, J.S.
Meprin-A and -B. Cell surface endopeptidases of the mouse kidney
J. Biol. Chem.
266
17350-17357
1991
Mus musculus, Mus musculus male ICR
Marchand, P.; Tang, J.; Bond, J.S.
Membrane association and oligomeric organization of the alpha and beta subunits of mouse meprin A
J. Biol. Chem.
269
15388-15393
1994
Mus musculus, Rattus norvegicus
Wolz, R.L.
A kinetic comparison of the homologous proteases astacin and meprin A
Arch. Biochem. Biophys.
310
144-151
1994
Mus musculus
Marchand, P.; Tang, J.; Johnson, G.D.; Bond, J.S.
COOH-Terminal proteolytic processing of secreted and membrane forms of the alpha subunit of the metalloprotease meprin A. Requirement of the I domain for processing in the endoplasmic reticulum
J. Biol. Chem.
270
5449-5456
1995
Mus musculus, Rattus norvegicus
Wolz, R.L.; Bond, J.S.
Meprins A and B
Methods Enzymol.
248
325-345
1995
Homo sapiens, Mus musculus, Rattus norvegicus, Homo sapiens PPH
Doll, B.A.; Villa, J.P.; Ishmael, F.T.; Bond, J.S.
Zinc ligands in an astacin family metalloprotease meprin A
Biol. Chem.
383
1167-1173
2002
Mus musculus
Kadowaki, T.; Tsukuba, T.; Bertenshaw, G.P.; Bond, J.S.
N-Linked oligosaccharides on the meprin A metalloprotease are important for secretion and enzymatic activity, but not for apical targeting
J. Biol. Chem.
275
25577-25584
2000
Mus musculus
Bertenshaw, G.P.; Turk, B.E.; Hubbard, S.J.; Matters, G.L.; Bylander, J.E.; Crisman, J.M.; Cantley, L.C.; Bond, J.S.
Marked differences between metalloproteases meprin A and B in substrate and peptide bond specificity
J. Biol. Chem.
276
13248-13255
2001
Mus musculus
Ishmael, F.T.; Norcum, M.T.; Benkovic, S.J.; Bond, J.S.
Multimeric structure of the secreted meprin A metalloproteinase and characterization of the functional protomer
J. Biol. Chem.
276
23207-23211
2001
Mus musculus
Villa, J.P.; Bertenshaw, G.P.; Bond, J.S.
Critical Amino Acids in the Active Site of Meprin Metalloproteinases for Substrate and Peptide Bond Specificity
J. Biol. Chem.
278
42545-42550
2003
Mus musculus
Mathew, R.; Futterweit, S.; Valderrama, E.; Tarectecan, A.A.; Bylander, J.E.; Bond, J.S.; Trachtman, H.
Meprin-alpha in chronic diabetic nephropathy: interaction with the renin-angiotensin axis
Am. J. Physiol. Renal Physiol.
289
F911-F921
2005
Mus musculus, Rattus norvegicus
Hengst, J.A.; Bond, J.S.
Transport of meprin subunits through the secretory pathway: role of the transmembrane and cytoplasmic domains and oligomerization
J. Biol. Chem.
279
34856-34864
2004
Mus musculus
Ishmael, S.S.; Ishmael, F.T.; Jones, A.D.; Bond, J.S.
Protease domain glycans affect oligomerization, disulfide bond formation, and stability of the meprin A metalloprotease homooligomer
J. Biol. Chem.
281
37404-37415
2006
Mus musculus
Bylander, J.E.; Bertenshaw, G.P.; Matters, G.L.; Hubbard, S.J.; Bond, J.S.
Human and mouse homo-oligomeric meprin A metalloendopeptidase: substrate and inhibitor specificities
Biol. Chem.
388
1163-1172
2007
Homo sapiens, Mus musculus
Herzog, C.; Haun, R.S.; Kaushal, V.; Mayeux, P.R.; Shah, S.V.; Kaushal, G.P.
Meprin A and meprin alpha generate biologically functional IL-1beta from pro-IL-1beta
Biochem. Biophys. Res. Commun.
379
904-908
2009
Mus musculus, Rattus norvegicus (Q64230)
Banerjee, S.; Oneda, B.; Yap, L.M.; Jewell, D.P.; Matters, G.L.; Fitzpatrick, L.R.; Seibold, F.; Sterchi, E.E.; Ahmad, T.; Lottaz, D.; Bond, J.S.
MEP1A allele for meprin A metalloprotease is a susceptibility gene for inflammatory bowel disease
Mucosal Immunol.
2
220-231
2009
Mus musculus (P28825), Mus musculus, Homo sapiens (Q16819), Homo sapiens
Gao, P.; Guo, R.W.; Chen, J.F.; Chen, Y.; Wang, H.; Yu, Y.; Huang, L.
A meprin inhibitor suppresses atherosclerotic plaque formation in ApoE-/- mice
Atherosclerosis
207
84-92
2009
Mus musculus
Gao, P.; Si, L.Y.
Meprin-alpha metalloproteases enhance lipopolysaccharide-stimulated production of tumour necrosis factor-alpha and interleukin-1beta in peripheral blood mononuclear cells via activation of NF-kappaB
Regul. Pept.
160
99-105
2010
Mus musculus
Kaushal, G.P.; Haun, R.S.; Herzog, C.; Shah, S.V.
Meprin A metalloproteinase and its role in acute kidney injury
Am. J. Physiol. Renal Physiol.
304
F1150-F1158
2013
Homo sapiens, Mus musculus, Rattus norvegicus, Mus musculus C57BL/6N
Bao, J.; Yura, R.E.; Matters, G.L.; Bradley, S.G.; Shi, P.; Tian, F.; Bond, J.S.
Meprin A impairs epithelial barrier function, enhances monocyte migration, and cleaves the tight junction protein occludin
Am. J. Physiol. Renal Physiol.
305
F714-F726
2013
Canis lupus familiaris, Canis lupus familiaris Madin-Darby, Mus musculus, Mus musculus C57BL/6
Niyitegeka, J.M.; Bastidas, A.C.; Newman, R.H.; Taylor, S.S.; Ongeri, E.M.
Isoform-specific interactions between meprin metalloproteases and the catalytic subunit of protein kinase A: significance in acute and chronic kidney injury
Am. J. Physiol. Renal Physiol.
308
F56-68
2015
Mus musculus
Broder, C.; Becker-Pauly, C.
The metalloproteases meprin alpha and meprin beta: Unique enzymes in inflammation, neurodegeneration, cancer and fibrosis
Biochem. J.
450
253-264
2013
Danio rerio, Homo sapiens, Mus musculus
Hirano, M.; Ma, B.; Kawasaki, N.; Oka, S.; Kawasaki, T.
Role of interaction of mannan-binding protein with meprins at the initial step of complement activation in ischemia/reperfusion injury to mouse kidney
Glycobiology
22
84-95
2012
Mus musculus, Mus musculus BALB/c
Keiffer, T.R.; Bond, J.S.
Meprin metalloproteases inactivate interleukin 6
J. Biol. Chem.
289
7580-7588
2014
Homo sapiens, Mus musculus, Mus musculus C57BL6
Prox, J.; Arnold, P.; Becker-Pauly, C.
Meprin alpha and meprin beta: procollagen proteinases in health and disease
Matrix Biol.
44-46
7-13
2015
Homo sapiens, Mus musculus
Broder, C.; Arnold, P.; Vadon-Le Goff, S.; Konerding, M.A.; Bahr, K.; Mueller, S.; Overall, C.M.; Bond, J.S.; Koudelka, T.; Tholey, A.; Hulmes, D.J.; Moali, C.; Becker-Pauly, C.
Metalloproteases meprin ? and meprin ? are C- and N-procollagen proteinases important for collagen assembly and tensile strength
Proc. Natl. Acad. Sci. USA
110
14219-14224
2013
Mus musculus
Chaudhuri, A.; Chakraborty, S.
Structure-activity relationship of astacin metalloproteases A comparative study using EDTA
Curr. Enzyme Inhib.
14
131-140
2018
Mus musculus (P28825), Rattus norvegicus (Q64230)
-
EXTERNAL LINKS (specific for EC-Number 3.4.24.18)
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