Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(7-methoxycoumarin-4-yl)acetyl-YVADAPK-(K-epsilon-DNP)-NH2 + H2O
?
-
-
-
-
?
2-aminobenzoic acid-RPPGFSPFRK(2,4-dinitrophenyl)G-OH + H2O
?
-
-
-
?
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
-
?
actin + H2O
?
-
murine homomeric recombinant enzyme
-
-
?
Aldolase + H2O
?
-
-
-
-
?
alpha-melanocyte stimulating hormone + H2O
?
alpha-melanocyte-stimulating hormone + H2O
?
angiotensin I + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe + Ile-His-Pro-Phe-His-Leu
angiotensin II + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
angiotensin III + H2O
Arg-Val-Tyr + Ile-His-Pro-Phe
annexin A1 + H2O
?
-
substrate identified by 2D IEF/SDS-PAGE-based image analysis
-
-
?
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
azocasein + H2O
fragments of azocasein
Azocoll + H2O
?
-
poor substrate
-
-
?
B-type natriuretic peptide + H2O
?
B-type natriuretic peptide 1-32 + H2O
B-type natriuretic peptide 8-32 + Ser-Pro-Lys-Met-Val-Gln-Gly
-
-
-
-
?
benzoyl-Gly-His-Leu + H2O
?
benzoyl-L-tyrosyl-4-aminobenzoic acid + H2O
?
Benzyloxycarbonyl-Arg-Arg 4-methylcoumarin 7-amide + H2O
?
Benzyloxycarbonyl-Glu-Lys-Lys 4-methylcoumarin 7-amide + H2O
?
-
poor substrate, hydrolysis at 9.1% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
-
-
?
Benzyloxycarbonyl-Phe-Arg 4-methylcoumarin 7-amide + H2O
?
Benzyloxycarbonyl-Val-Leu-Lys 4-methylcoumarin 7-amide + H2O
?
-
poor substrate, hydrolysis at 10.4% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
-
-
?
Big endothelin I + H2O
?
-
rat
-
-
?
bradykinin + H2O
Arg-Pro-Pro-Gly + Phe-Ser-Pro-Phe-Arg
catalytic subunit of protein kinase A + H2O
?
-
in rat kidney
-
-
?
CCK8NH2 + H2O
L-Asp-L-Tyr-L-Met-Gly-L-Trp-L-Met + L-Asp-L-Phe
-
-
-
-
?
cholecystokinin 8-sulfate + H2O
?
-
-
-
?
collagen I + H2O
?
-
-
-
?
Collagen type IV + H2O
Hydrolyzed collagen type IV
-
-
-
?
collagen type V + H2O
?
-
substrate identified by 2D IEF/SDS-PAGE-based image analysis
-
-
?
Endothelin I + H2O
?
-
rat
-
-
?
fibrillar procollagen type I + H2O
fibrillar collagen type I + fibrillar collagen type I propeptide
fibrillar procollagen type III + H2O
fibrillar collagen type III + fibrillar collagen type I propeptide
Fibronectin + H2O
Hydrolyzed fibronectin
-
-
-
?
gastri-releasing peptide-(14-27) + H2O
?
-
peptide of the gastrointestinal tract
-
?
gastrin 17 + H2O
?
-
mutant Y199K
-
?
gastrin-releasing peptide + H2O
?
gastrin-releasing peptide-(14-27) + H2O
?
-
-
-
-
?
Gelatin + H2O
Hydrolyzed gelatin
-
-
-
?
Glutaryl-Phe 4-methylcoumarin 7-amide + H2O
?
-
poor substrate, hydrolysis at 2.4% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
-
-
?
Gonadotropin + H2O
?
-
mouse
-
-
?
Hemoglobin + H2O
?
-
poor substrate
-
-
?
Human alpha-atrial natiuretic peptide + H2O
?
Human transforming growth factor + H2O
?
-
rat
-
-
?
insulin + H2O
?
-
in mouse kidney
-
-
?
insulin B chain + H2O
?
-
in human small intestine
-
-
?
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
interleukin-1beta + H2O
?
-
meprin beta activates interleukin 18
-
-
?
KKGYVADAP-4-nitroanilide + H2O
KKGYVA + DAP-4-nitroanilide
-
-
-
?
L-Leu 2-naphthylamide + H2O
?
-
-
-
-
?
laminin + H2O
fragments of laminin
-
-
-
?
laminin 1 + H2O
?
-
human homomeric recombinant enzyme
-
-
?
laminin 5 + H2O
?
-
human homomeric recombinant enzyme
-
-
?
laminin V + H2O
?
-
-
-
?
Leu-Val-Tyr 4-methylcoumarin 7-amide + H2O
?
-
poor substrate, hydrolysis at 6.2% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
-
-
?
Luliberin + H2O
?
-
i.e. luteinizing-hormone releasing hormone, preferred cleavage site: Trp3-Ser4, other sites are Ser4-Tyr5 and Tyr5-Gly6
-
-
?
luteinizing hormone releasing hormone LHRH + H2O
?
luteinizing-hormone-releasing hormone + H2O
?
lysyl oxidase + H2O
?
-
substrate identified by 2D IEF/SDS-PAGE-based image analysis
-
-
?
miniprocollagen alpha1(I) homotrimers + H2O
?
-
-
-
-
?
N-Benzoyl-L-tyrosyl-4-aminobenzoate + H2O
N-Benzoyl-L-tyrosine + 4-aminobenzoate
Nidogen + H2O
?
-
in rat kidney
-
-
?
orcokinin + H2O
?
-
-
-
-
?
oxytocin + H2O
?
-
in human small intestine
-
-
?
Oxytocin + H2O
Hydrolyzed oxytocin
-
poor substrate
-
?
Parathyroid hormone + H2O
?
Parathyroid hormone + H2O
Hydrolyzed parathyroid hormone
-
i.e. hPTH-(1-84), in vivo and in vitro
-
?
parathyroid hormone fragment 13-34 + H2O
?
pro-interleukin 1beta + H2O
interleukin 1beta + H2O
cleavage at the H115-D116 bond, which is one amino acid N-terminal to the caspase-1 cleavage site and five amino acids C-terminal to the meprin beta site. Both oligomeric meprin A and recombinant meprin alpha are capable of cleaving
the biological activity of the pro-interleukin-1beta cleaved product produced by meprin A, is 3fold higher to that of the interleukin-1beta product produced by meprin b or caspase-1
-
?
Pro-interleukin-1beta + H2O
?
-
-
-
-
?
pro-KLK7 + H2O
KLK7 + ?
-
meprin beta cleaves pro-KLK7 between Gly17 and Asp18
-
-
?
procollagen I + H2O
collagen I + propeptide of collagen III
procollagen III + H2O
?
-
meprin alpha can process procollagen III
-
-
?
procollagen type III + H2O
?
-
human homomeric recombinant enzyme
-
-
?
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
-
?
Substance P + H2O
Hydrolyzed substance P
Succinyl-Ala-Ala-Ala 4-nitroanilide + H2O
?
-
arylamidolysis
-
-
?
Succinyl-Ala-Ala-Pro-Phe 4-methylcoumarin 7-amide + H2O
?
-
poor substrate, hydrolysis at 9% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
-
-
?
Succinyl-Ala-Pro-Ala 4-methylcoumarin 7-amide + H2O
?
-
poor substrate, hydrolysis at 2.8% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
-
-
?
Succinyl-Gly-Pro 4-methylcoumarin 7-amide + H2O
?
-
poor substrate, hydrolysis at 10.7% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
-
-
?
Succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide + H2O
?
Succinyl-Leu-Tyr 4-methylcoumarin 7-amide + H2O
?
-
poor substrate, hydrolysis at 5.6% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
-
-
?
tissue growth factor-alpha + H2O
?
-
meprin alpha can process tissue growth factor-alpha
-
-
?
tumor necrosis factor alpha + H2O
?
-
in rat kidney
-
-
?
Tyr 4-methylcoumarin 7-amide + H2O
?
-
poor substrate, hydrolysis at 3.3% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
-
-
?
Tyr-Leu-Val-Cys(SO3-)-Gly-Glu-Arg-Gly + H2O
?
vascular endothelial growth factor A + H2O
?
-
-
-
-
?
vascular endothelial growth factor-A + H2O
?
Vasoactive intestinal peptide + H2O
?
VEGF-A + H2O
?
-
human meprin alpha cleaves VEGF-A in vitro, generating proteolytic fragments as found in wild-type zebrafish
-
-
?
villin + H2O
?
-
murine homomeric recombinant enzyme
-
-
?
vinculin + H2O
?
-
substrate identified by 2D IEF/SDS-PAGE-based image analysis
-
-
?
[Met5]enkephalin-Arg6-Phe7 + H2O
?
additional information
?
-
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
?
-
human homomeric recombinant enzyme
-
-
?
alpha-melanocyte-stimulating hormone + H2O
?
-
-
-
-
?
alpha-melanocyte-stimulating hormone + H2O
?
-
murine homomeric recombinant enzyme
-
-
?
alpha-MSH + H2O
?
-
-
-
-
?
alpha-MSH + H2O
?
-
-
-
-
?
angiotensin I + H2O
?
-
in human small intestine
-
-
?
angiotensin I + H2O
?
-
-
-
-
?
angiotensin I + H2O
?
-
peptide of the gastrointestinal tract
-
?
angiotensin I + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe + Ile-His-Pro-Phe-His-Leu
-
2 cleavage sites: Tyr-Ile and Phe-His
-
?
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 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 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 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 II + H2O
?
-
-
-
?
angiotensin II + H2O
?
-
in human small intestine
-
-
?
angiotensin II + H2O
?
-
in mouse kidney
-
-
?
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
-
-
?
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
-
-
?
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
-
i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
-
-
?
angiotensin III + H2O
Arg-Val-Tyr + Ile-His-Pro-Phe
-
i.e. Arg-Val-Tyr-Ile-His-Pro-Phe, 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
-
-
?
angiotensin III + H2O
Arg-Val-Tyr + Ile-His-Pro-Phe
-
poor substrate
-
?
angiotensin III + H2O
Arg-Val-Tyr + Ile-His-Pro-Phe
-
i.e. Arg-Val-Tyr-Ile-His-Pro-Phe, 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
-
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
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
fragments of azocasein
-
-
-
?
azocasein + H2O
fragments of azocasein
-
excellent substrate for mouse, poorer substrate for rat and human enzymes
-
-
?
azocasein + H2O
fragments of azocasein
-
-
-
?
azocasein + H2O
fragments of azocasein
-
excellent substrate for mouse, poorer substrate for rat and human enzymes
-
-
?
azocasein + H2O
fragments of azocasein
-
-
-
-
?
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
-
-
?
azocasein + H2O
fragments of azocasein
-
-
-
-
?
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
-
-
?
B-type natriuretic peptide + H2O
?
-
-
-
-
?
B-type natriuretic peptide + H2O
?
-
meprin A degrades rat BNP but not human BNP
-
-
?
benzoyl-Gly-His-Leu + H2O
?
-
very poor substrate, t1/2 of more than 16 h
-
-
?
benzoyl-Gly-His-Leu + H2O
?
-
very poor substrate, t1/2 of more than 16 h
-
-
?
benzoyl-L-tyrosyl-4-aminobenzoic acid + H2O
?
-
-
-
-
?
benzoyl-L-tyrosyl-4-aminobenzoic acid + H2O
?
-
-
-
-
?
benzoyl-L-tyrosyl-4-aminobenzoic acid + H2O
?
-
-
-
-
?
Benzyloxycarbonyl-Arg-Arg 4-methylcoumarin 7-amide + H2O
?
-
poor substrate, hydrolysis at 8.2% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
-
-
?
Benzyloxycarbonyl-Arg-Arg 4-methylcoumarin 7-amide + H2O
?
-
poor substrate, hydrolysis at 8.2% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
-
-
?
Benzyloxycarbonyl-Phe-Arg 4-methylcoumarin 7-amide + H2O
?
-
poor substrate, hydrolysis at 3.6% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
-
-
?
Benzyloxycarbonyl-Phe-Arg 4-methylcoumarin 7-amide + H2O
?
-
poor substrate, hydrolysis at 3.6% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
-
-
?
Benzyloxycarbonyl-Phe-Arg 4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
bombesin + H2O
?
-
-
-
-
?
bombesin + H2O
?
-
peptide of the gastrointestinal tract
-
?
bradykinin + H2O
?
-
-
-
-
?
bradykinin + H2O
?
-
-
-
?
bradykinin + H2O
?
-
in human small intestine
-
-
?
bradykinin + H2O
?
-
human homomeric recombinant enzyme
-
-
?
bradykinin + H2O
?
-
-
-
?
bradykinin + H2O
?
-
-
-
-
?
bradykinin + H2O
?
-
peptide of the gastrointestinal tract
-
?
bradykinin + H2O
?
-
in mouse kidney
-
-
?
bradykinin + H2O
?
-
murine homomeric recombinant enzyme
-
-
?
bradykinin + H2O
?
-
-
-
?
bradykinin + H2O
?
-
in rat kidney
-
-
?
bradykinin + H2O
Arg-Pro-Pro-Gly + Phe-Ser-Pro-Phe-Arg
-
-
-
-
?
bradykinin + H2O
Arg-Pro-Pro-Gly + Phe-Ser-Pro-Phe-Arg
-
i.e. Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg, bradykinin(1-7) and bradykinin(1-8) best substrates next to substance P
-
-
?
bradykinin + H2O
Arg-Pro-Pro-Gly + Phe-Ser-Pro-Phe-Arg
-
one cleavage site: Phe-Ser
-
-
?
bradykinin + H2O
Arg-Pro-Pro-Gly + Phe-Ser-Pro-Phe-Arg
-
-
-
-
?
bradykinin + H2O
Arg-Pro-Pro-Gly + Phe-Ser-Pro-Phe-Arg
-
one cleavage site: Phe-Ser
-
-
?
bradykinin + H2O
Arg-Pro-Pro-Gly + Phe-Ser-Pro-Phe-Arg
-
-
-
-
?
bradykinin + H2O
Arg-Pro-Pro-Gly + Phe-Ser-Pro-Phe-Arg
-
one cleavage site: Phe-Ser (major cleavage site)
-
-
?
bradykinin + H2O
Arg-Pro-Pro-Gly + Phe-Ser-Pro-Phe-Arg
-
one cleavage site: Phe-Ser
-
-
?
bradykinin + H2O
Arg-Pro-Pro-Gly + Phe-Ser-Pro-Phe-Arg
-
minor cleavage site: Gly-Phe
-
-
?
CCK8 nonsulfated + H2O
?
-
human homomeric recombinant enzyme
-
-
?
CCK8 nonsulfated + H2O
?
-
murine homomeric recombinant enzyme
-
-
?
cerulein + H2O
?
-
-
-
-
?
cerulein + H2O
?
-
peptide of the gastrointestinal tract
-
?
Collagen IV + H2O
?
-
-
-
-
?
Collagen IV + H2O
?
-
-
-
?
Collagen IV + H2O
?
-
-
-
?
Collagen IV + H2O
?
-
in rat kidney
-
-
?
collagen type IV + H2O
?
-
meprin alpha can degrade collagen type IV
-
-
?
collagen type IV + H2O
?
-
human homomeric recombinant enzyme
-
-
?
E-cadherin + H2O
?
-
an extracellular matrix-related substrate
-
-
?
E-cadherin + H2O
?
-
an extracellular matrix-related substrate
-
-
?
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 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
-
-
?
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
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
cleavage at positions Y294-Q295, N709-T210 and in the linker regions between fibronectin type I repeats 5 and 6 and fibronectin type II repeats 1 and 2
-
-
?
Fibronectin + H2O
?
-
an extracellular matrix-related substrate
-
-
?
Fibronectin + H2O
?
-
human homomeric recombinant enzyme
-
-
?
Fibronectin + H2O
?
-
-
-
?
Fibronectin + H2O
?
-
an extracellular matrix-related substrate
-
-
?
Fibronectin + H2O
?
-
in rat kidney
-
-
?
gastrin + H2O
?
-
-
-
-
?
gastrin-releasing peptide + H2O
?
-
human homomeric recombinant enzyme
-
-
?
gastrin-releasing peptide + H2O
?
-
murine homomeric recombinant enzyme
-
-
?
Gelatin + H2O
?
-
-
-
?
Gelatin + H2O
?
-
in rat kidney
-
-
?
ghrelin + H2O
?
-
human homomeric recombinant enzyme
-
-
?
ghrelin + H2O
?
-
murine homomeric recombinant enzyme
-
-
?
Glucagon + H2O
?
-
human homomeric recombinant enzyme
-
-
?
Glucagon + H2O
?
-
-
-
-
?
Glucagon + H2O
?
-
peptide of the gastrointestinal tract
-
?
Glucagon + H2O
?
-
murine homomeric recombinant enzyme
-
-
?
Human alpha-atrial natiuretic peptide + H2O
?
-
-
-
-
?
Human alpha-atrial natiuretic peptide + H2O
?
-
rat
-
-
?
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
-
10 cleavage sites
-
-
?
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
7 major and 3 minor sites
-
-
?
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
oxidized form
-
-
?
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
-
10 cleavage sites
-
-
?
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
7 major and 3 minor sites
-
-
?
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
oxidized form
-
-
?
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
-
-
-
?
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
-
-
?
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
-
-
?
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
?
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
-
10 cleavage sites
15 different peptide fragments
?
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
oxidized form
15 different peptide fragments
?
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
I125-iodinated
-
-
?
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
-
10 cleavage sites
-
-
?
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
7 major and 3 minor sites
-
-
?
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
oxidized form
-
-
?
interleukin-6 + H2O
?
-
recombinant human substrate expressed in eukaryotic B9 cell line, inactivation. Human meprin A cleaves 20% of human interleukin-6 of about 22 kDa to a smaller product of about 21 kDa within 2 h. Meprin A cleaves human interleukin-6 at its C-terminus, fragmentation pattern, overview
-
-
?
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
-
-
?
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
-
-
?
Laminin + H2O
?
-
-
-
?
Laminin + H2O
?
-
in rat kidney
-
-
?
luteinizing hormone releasing hormone LHRH + H2O
?
-
-
-
-
?
luteinizing hormone releasing hormone LHRH + H2O
?
-
-
-
-
?
luteinizing hormone releasing hormone LHRH + H2O
?
-
peptide of the gastrointestinal tract
-
?
luteinizing-hormone-releasing hormone + H2O
?
-
in human small intestine
-
-
?
luteinizing-hormone-releasing hormone + H2O
?
-
human homomeric recombinant enzyme
-
-
?
luteinizing-hormone-releasing hormone + H2O
?
-
-
-
-
?
luteinizing-hormone-releasing hormone + H2O
?
-
murine homomeric recombinant enzyme
-
-
?
luteinizing-hormone-releasing hormone + H2O
?
-
in rat kidney
-
-
?
MMP1 protein + H2O
?
-
an extracellular matrix-related substrate
-
-
?
MMP1 protein + H2O
?
-
an extracellular matrix-related substrate
-
-
?
Muc2 protein + H2O
?
-
an extracellular matrix-related substrate
-
-
?
Muc2 protein + H2O
?
-
an extracellular matrix-related substrate
-
-
?
N-Benzoyl-L-tyrosyl-4-aminobenzoate + H2O
N-Benzoyl-L-tyrosine + 4-aminobenzoate
-
i.e. PABA-peptide, rat, human, arylamidolysis
-
-
?
N-Benzoyl-L-tyrosyl-4-aminobenzoate + H2O
N-Benzoyl-L-tyrosine + 4-aminobenzoate
-
very poor substrate, t1/2 of more than 16 h
-
?
N-Benzoyl-L-tyrosyl-4-aminobenzoate + H2O
N-Benzoyl-L-tyrosine + 4-aminobenzoate
-
very poor substrate, t1/2 of more than 16 h
-
?
N-Benzoyl-L-tyrosyl-4-aminobenzoate + H2O
N-Benzoyl-L-tyrosine + 4-aminobenzoate
-
-
-
-
?
N-Benzoyl-L-tyrosyl-4-aminobenzoate + H2O
N-Benzoyl-L-tyrosine + 4-aminobenzoate
-
i.e. PABA-peptide, rat, human, arylamidolysis
-
-
?
neuropeptide Y + H2O
?
-
-
-
-
?
neuropeptide Y + H2O
?
-
peptide of the gastrointestinal tract
-
?
neurotensin + H2O
?
-
human homomeric recombinant enzyme
-
-
?
neurotensin + H2O
?
-
-
-
-
?
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
-
-
?
neurotensin + H2O
?
-
peptide of the gastrointestinal tract
-
?
neurotensin + H2O
?
-
murine homomeric recombinant enzyme
-
-
?
neurotensin + H2O
?
-
-
-
-
?
neurotensin + 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
-
-
?
nidogen 1 + H2O
?
-
-
-
?
nidogen 1 + H2O
?
-
an extracellular matrix-related substrate
-
-
?
nidogen 1 + H2O
?
-
an extracellular matrix-related substrate
-
-
?
nidogen-1 + H2O
?
-
cleavage at D67-R68 and Q363-H364
-
-
?
nidogen-1 + H2O
?
-
human homomeric recombinant enzyme
-
-
?
occludin + H2O
?
-
in MDCK cells and in micelles
-
-
?
occludin + H2O
?
-
recombinant MBP-conjugated human substrate 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
-
-
?
occludin + H2O
?
-
in MDCK cells and in micelles
-
-
?
occludin + H2O
?
-
recombinant MBP-conjugated human substrate 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
-
-
?
occludin + H2O
?
-
in MDCK cells
-
-
?
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
-
-
?
occludin + H2O
?
-
in MDCK cells
-
-
?
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 + H2O
?
-
involved in PTH-degradation in human kidney
-
-
?
Parathyroid hormone + H2O
?
-
human homomeric recombinant enzyme
-
-
?
Parathyroid hormone + H2O
?
-
involved in PTH-degradation in human kidney
-
-
?
Parathyroid hormone + H2O
?
-
murine homomeric recombinant enzyme
-
-
?
Parathyroid hormone + H2O
?
-
murine homomeric recombinant enzyme
-
-
?
Parathyroid hormone + H2O
?
-
in rat kidney
-
-
?
parathyroid hormone fragment 13-34 + H2O
?
-
-
-
-
?
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
-
-
?
protein GRP + H2O
?
-
-
-
-
?
protein GRP + H2O
?
-
-
-
-
?
protein LHRH + H2O
?
-
-
-
-
?
protein LHRH + H2O
?
-
-
-
-
?
protein PTH12-34 + H2O
?
-
-
-
-
?
protein PTH12-34 + H2O
?
-
-
-
-
?
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
-
-
?
Secretin + H2O
?
-
-
-
-
?
Secretin + H2O
?
-
human homomeric recombinant enzyme
-
-
?
Secretin + H2O
?
-
-
-
-
?
Secretin + H2O
?
-
peptide of the gastrointestinal tract
-
?
Secretin + H2O
?
-
murine homomeric recombinant enzyme
-
-
?
Substance P + H2O
?
-
-
-
-
?
Substance P + H2O
?
-
in human small intestine
-
-
?
Substance P + H2O
?
-
human homomeric recombinant enzyme
-
-
?
Substance P + H2O
?
-
-
-
-
?
Substance P + H2O
?
-
peptide of the gastrointestinal tract
-
?
Substance P + H2O
?
-
murine homomeric recombinant enzyme
-
-
?
Substance P + H2O
?
-
in rat kidney
-
-
?
Substance P + H2O
Hydrolyzed substance P
-
-
-
-
?
Substance P + H2O
Hydrolyzed substance P
-
best substrate
-
?
Substance P + H2O
Hydrolyzed substance P
-
rat
-
-
?
Substance P + H2O
Hydrolyzed substance P
-
cleavage sites: Glu6-Phe7, Phe7-Phe8, Phe8-Gly9
-
-
?
Succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
Succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
tenascin-C + H2O
?
-
an extracellular matrix-related substrate
-
-
?
tenascin-C + H2O
?
-
an extracellular matrix-related substrate
-
-
?
Tyr-Leu-Val-Cys(SO3-)-Gly-Glu-Arg-Gly + H2O
?
-
synthetic peptide derived from insulin B-chain
-
-
?
Tyr-Leu-Val-Cys(SO3-)-Gly-Glu-Arg-Gly + H2O
?
-
synthetic peptide derived from insulin B-chain
-
-
?
valosin + H2O
?
-
-
-
-
?
valosin + H2O
?
-
peptide of the gastrointestinal tract
-
?
vascular endothelial growth factor-A + H2O
?
-
-
-
?
vascular endothelial growth factor-A + H2O
?
cleavage of the vascular endothelial growth factor-A monomer by meprin alpha yields in two distinct fragments of 19600 Da, the N-terminal cleavage site in human vascular endothelial growth factor-A165 is between Ala30 and Glu31 due to recombinant human meprin alpha activity
-
-
?
Vasoactive intestinal peptide + H2O
?
-
-
-
-
?
Vasoactive intestinal peptide + H2O
?
-
peptide of the gastrointestinal tract
-
?
[Met5]enkephalin-Arg6-Phe7 + H2O
?
-
-
-
-
?
[Met5]enkephalin-Arg6-Phe7 + H2O
?
-
-
-
-
?
[Met5]enkephalin-Arg6-Phe7 + H2O
?
-
-
-
-
?
additional information
?
-
-
2D IEF/SDS-PAGE-based image analysis procedure to analyse candidate substrates for meprin in a cell culture system-based approach and identification of meprin substrates with cleaved non-trypsin-generated N- and C-termini in peptide fragments upon LC-MS/MS analysis
-
-
?
additional information
?
-
-
no activity with claudin-4 in MDCK cells
-
-
?
additional information
?
-
-
no activity with claudin-4 in MDCK cells
-
-
?
additional information
?
-
-
hydrolysis occurs on carboxy side of aromatic residues
-
-
?
additional information
?
-
-
poor substrates are compounds with 3 or less amino acids
-
-
?
additional information
?
-
-
dansyl-(D)-Ala-Gly-4-phenylalanylglycine, [Leu]-enkephalin, [Met]-enkephalin
-
-
?
additional information
?
-
-
no substrate: intact collagen I
-
-
?
additional information
?
-
-
meprin interacts with epithelial Na+ channel (ENaC)
-
-
?
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
-
-
?
additional information
?
-
-
enzyme cleavage specificity, overview
-
-
?
additional information
?
-
meprin beta preferentially cleaves substrates with acidic amino acids in P1'-position
-
-
?
additional information
?
-
the cleavage of a meprin alpha substrate leads to generation of the prolyl tripeptidyl aminopeptidase (PtP, EC 3.4.14.12) substrate, and the activity of PtP results in release of a chromophore or fluorophore, coupled assay method evaluation, overview
-
-
?
additional information
?
-
-
hydrolysis occurs on carboxy side of aromatic residues
-
-
?
additional information
?
-
-
dansyl-(D)-Ala-Gly-4-phenylalanylglycine, [Leu]-enkephalin, [Met]-enkephalin
-
-
?
additional information
?
-
-
poor substrates are compounds with 3 or less amino acids
-
-
?
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
?
-
-
no activity with claudin-4 in MDCK cells
-
-
?
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
-
-
?
additional information
?
-
meprin alpha, but not meprin beta, cleaves Reelin in which Asp2689 is replaced with Lys (Reelin-DK mutant)
-
-
?
additional information
?
-
-
no activity with claudin-4 in MDCK cells
-
-
?
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
-
-
?
additional information
?
-
-
hydrolysis occurs on carboxy side of aromatic residues
-
-
?
additional information
?
-
-
insulin, [Arg8]-vasopressin, cytochrome c, ovalbumin, serum albumin
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
-
meprin A, is a membrane-associated neutral metalloendoprotease that belongs to the astacin family of zinc endopeptidases
evolution
-
meprin A, is a membrane-associated neutral metalloendoprotease that belongs to the astacin family of zinc endopeptidases
evolution
-
meprin A, is a membrane-associated neutral metalloendoprotease that belongs to the astacin family of zinc endopeptidases
evolution
-
meprin alpha is a metalloprotease of the astacin family characterized by a conserved zinc-binding motif (HExxHxxGFxHExxRxDR). Human meprin-alpha and -beta protease, EC 3.4.24.63, subunits are 55% identical at the amino acid level, while the substrate and peptide bond specificities vary markedly
evolution
-
meprin metalloproteases belong to the astacin family of zinc endopeptidases and the metzincin superfamily
evolution
-
meprin metalloproteases belong to the astacin family of zinc endopeptidases and the metzincin superfamily
evolution
-
meprin metalloproteases belong to the astacin family of zinc endopeptidases and the metzincin superfamily. Meprins belong to the astacin family of metalloproteases, comprising only six members in humans. These enzymes are characterized by a conserved zinc-binding motif (HExxHxxGxxHxxxRxDR) and by a sequence in close proximity to the active-site cleft, the so called Met-turn, that includes a tyrosine residue as a fifth zinc ligand. Within the astacin family, meprins exhibit a unique domain composition
evolution
meprin alpha belongs to the astacin family of zinc-endopeptidases and the metzincin superfamily, characterized by the conserved motif HExxHxxGxxHxxxRxDR
evolution
the astacin proteases meprin alpha and meprin beta are zinc-dependent metalloproteases of the metzincin superfamily
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
evolution
the enzyme encoded by Rmepa 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
evolution
-
meprin A, is a membrane-associated neutral metalloendoprotease that belongs to the astacin family of zinc endopeptidases
-
malfunction
knockdown of meprin alpah1 mRNA causes defects in general tissue differentiation
malfunction
meprin alpha2 morphants show severe failures in the formation of the vascular system
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
-
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
-
breast cancer MDA-MB-435 cells treated with the meprin inhibitor actinonin are less invasive in vitro. 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 downregulation causes impaired intestinal mucin release and barrier function,and decreases tensile strength in the skin, but it also leads to protection against sepsis and renal injury. Enzyme upregulation can cause fibrosis, pulmonary hypertension, the Kawasaki syndrome, inflammatory bowel disease, and is involved in nephritis, cancer, and Alzheimer's disease, overview
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
malfunction
-
the knockdown of meprin beta in zebrafish embryos leads to a general failure in organogenesis, resulting in the death of the embryos between days 1 and 3 postfertilization
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
-
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
-
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
-
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
-
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
-
meprin A is more effective than meprin B, EC 3.4.24.63, in impairing MDCK epithelial barrier function
metabolism
-
meprins show higher substrate and cleavage specificity compared to matrix metalloproteases
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
metabolism
Mep1A is a target of reptin, a protein that is oncogenic in hepatocellular carcinoma (HCC). Silencing reptin decreases Mep1A expression and activity, without affecting meprin beta (EC 3.4.24.63)
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
-
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
-
meprin A is more effective than meprin B, EC 3.4.24.63, in impairing MDCK epithelial barrier function
-
physiological function
-
meprin A plays a role in the regulation of B-type natriuretic peptide 1-32 bioactivity in the kidney
physiological function
-
meprin beta induces a dramatic change in cell morphology and a significant reduction in cell number, whereas meprin alpha plays a role for basal keratinocyte proliferation in vitro
physiological function
meprin metalloproteases are important for cell differentiation and proliferation already during embryogenesis, predominantly by the activation of growth factors. Meprins play a significant role in vascular endothelial growth factor-A processing, subsequently regulating angiogenesis
physiological function
meprin metalloproteases are important for cell differentiation and proliferation already during embryogenesis, predominantly by the activation of growth factors. Meprins play a significant role in VEGF-A processing, subsequently regulating angiogenesis
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 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
physiological function
-
besides its contribution in the regulation of angiogenesis, meprin alpha is involved in cardiovascular homoeostasis by enzymatic cleavage of the 32-amino acid B-type natriuretic peptide in vitro and in vivo, leading to its reduced bioactivity. Procollagen III is processed to its mature form by meprin alpha and meprin beta, an essential step in collagen fibril assembly. The metalloprotease meprin alpha is involved in inflammation, neurodegeneration, cancer and fibrosis, overview. Gene MEP1A is genetically associated with inflammatory bowel disease, on the basis of single nucleotide polymorphisms in ulcerative colitis patients. Meprin alpha induces inflammation by transactivation of the EGF receptor through the release of its ligands transforming growth factor alpha and EGF from the cell surface, meprin alpha is able to release soluble EGF and TGFalpha, consequently activating the EGFR and ERK1/2 (extracellular-signal-regulated kinase 1/2) signalling cascade in a ligand-dependent manner. Meprin alpha expressed in basal epidermis promotes cell proliferation
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 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 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 enzyme is involved in the progression of colon cancer, the ability of meprins to degrade extracellular matrix components is implicated in cell migration of leukocytes of mesenteric lymph nodes and invasion of tumor cells that express meprin
physiological function
-
the metalloproteases meprin alpha and meprin beta are involved in inflammation, neurodegeneration, cancer and fibrosis, 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
physiological function
Mep1A is overexpressed in most hepatocellular carcinomas and induces hepatocellular carcinoma (HCC) cell migration and invasion. Mep1A expression is regulated by reptin, or RUVBL2, a member of the AAA+ ATPase family. And Mep1A mediates reptin-induced migration. Meprin alpha has a limited effect on HCC cell proliferation
physiological function
meprins cleave compounds of the extracellular matrix such as laminin-V, collagen IV, fibronectin or nidogen 1, but also growth factors, cytokines and peptide hormones, including bradykinin, angiotensins, and gastrin
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 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
-
additional information
-
homology modeling of the protease domain of meprin alpha on the astacin crystal structure and molecular dynamics simulation study, overview
additional information
human meprin alpha is modelled using the template structure of astacin
additional information
-
human meprin alpha is modelled using the template structure of astacin
additional information
the hydrogen bonding residues of the enzyme are Ser131, Glu157, His166, Ser169, and Tyr195, comparative three-dimensional structure homology modeling (template crystal structure PDB ID 4GWN) and docking study, and potential binding site, detailed overview
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
brenda
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
brenda
Stephenson, S.L.; Kenny, A.J.
The metabolism of neuropeptides. Hydrolysis of peptides by the phosphoramidon-insensitive rat kidney enzyme endopeptidase-2 and by rat microvillar membranes
Biochem. J.
255
45-51
1988
Rattus norvegicus
brenda
Sterchi, E.E.; Naim, H.Y.; Lentze, M.J.; Hauri, H.P.; Fransen, J.A.M.
N-Benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase: a metalloendopeptidase of the human intestinal microvillus membrane which degrades biologically active peptides
Arch. Biochem. Biophys.
265
105-118
1988
Homo sapiens, Homo sapiens PPH
brenda
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, Mus musculus, Homo sapiens PPH
brenda
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
brenda
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
brenda
Johnson, G.D.; Hersh, L.B.
Cloning a rat meprin cDNA reveals the enzyme is a heterodimer [published erratum appears in J Biol Chem 1993 Aug 15;268(23):17647]
J. Biol. Chem.
267
13505-13512
1992
Rattus norvegicus
brenda
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
brenda
Yamaguchi, T.; Fukase, M.; Sugimoto, T.; Kido, H.; Chihara, K.
Purification of meprin from human kidney and its role in parathyroid hormone degradation
Biol. Chem. Hoppe-Seyler
375
821-824
1994
Homo sapiens, Homo sapiens PPH
brenda
Wolz, R.L.
A kinetic comparison of the homologous proteases astacin and meprin A
Arch. Biochem. Biophys.
310
144-151
1994
Mus musculus
brenda
Kaushal, G.P.; Walker, P.D.; Shah, S.V.
An old enzyme with a new function: purification and characterization of a distinct matrix-degrading metalloproteinase in rat kidney cortex and its identification as meprin
J. Cell Biol.
126
1319-1327
1994
Rattus norvegicus
brenda
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
brenda
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
brenda
Sterchi, E.E.; Naim, H.Y.; Lentze, M.J.
Biosynthesis of N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase: disulfide-linked dimers are formed at the site of synthesis in the rough endoplasmic reticulum
Arch. Biochem. Biophys.
265
119-127
1988
Homo sapiens, Homo sapiens PPH
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Kruse, M.; Becker, C.; Lottaz, D.; Koehler, D.; Yiallouros, I.; Krell, H.; Sterchi, E.E.; Stoecker, W.
Human meprin alpha and beta homo-oligomers: cleavage of basement membrane proteins and sensitivity to metalloprotease inhibitors
Biochem. J.
378
383-389
2004
Homo sapiens
brenda
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
brenda
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
brenda
DeGuzman, J.B.; Speiser, P.W.; Trachtman, H.
Urinary meprin-a: a potential marker of diabetic nephropathy
J. Pediatr. Endocrinol. Metab.
17
1663-1666
2004
Homo sapiens
brenda
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
brenda
Heinzelmann-Schwarz, V.A.; Scolyer, R.A.; Scurry, J.P.; Smith, A.N.; Gardiner-Garden, M.; Biankin, A.V.; Baron-Hay, S.; Scott, C.; Ward, R.L.; Fink, D.; Hacker, N.F.; Sutherland, R.L.; OBrien, P.M.
Low meprin alpha expression differentiates primary ovarian mucinous carcinoma from gastrointestinal cancers that commonly metastasise to the ovaries
J. Clin. Pathol.
60
622-626
2007
Homo sapiens
brenda
Becker-Pauly, C.; Hoewel, M.; Walker, T.; Vlad, A.; Aufenvenne, K.; Oji, V.; Lottaz, D.; Sterchi, E.E.; Debela, M.; Magdolen, V.; Traupe, H.; Stoecker, W.
The alpha and beta subunits of the metalloprotease meprin are expressed in separate layers of human epidermis, revealing different functions in keratinocyte proliferation and differentiation
J. Invest. Dermatol.
127
1115-1125
2007
Homo sapiens
brenda
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)
brenda
Takayama, J.; Takaoka, M.; Yamamoto, S.; Nohara, A.; Ohkita, M.; Matsumura, Y.
Actinonin, a meprin inhibitor, protects ischemic acute kidney injury in male but not in female rats
Eur. J. Pharmacol.
581
157-163
2008
Rattus norvegicus
brenda
Ambort, D.; Stalder, D.; Lottaz, D.; Huguenin, M.; Oneda, B.; Heller, M.; Sterchi, E.E.
A novel 2D-based approach to the discovery of candidate substrates for the metalloendopeptidase meprin
FEBS J.
275
4490-4509
2008
Canis lupus familiaris
brenda
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
brenda
Ohler, A.; Debela, M.; Wagner, S.; Magdolen, V.; Becker-Pauly, C.
Analyzing the protease web in skin: meprin metalloproteases are activated specifically by KLK4, 5 and 8 vice versa leading to processing of proKLK7 thereby triggering its activation
Biol. Chem.
391
455-460
2010
Homo sapiens
brenda
Boerrigter, G.; Costello-Boerrigter, L.C.; Harty, G.J.; Huntley, B.K.; Cataliotti, A.; Lapp, H.; Burnett, J.C.
B-type natriuretic peptide 8-32, which is produced from mature BNP 1-32 by the metalloprotease meprin A, has reduced bioactivity
Am. J. Physiol. Regul. Integr. Comp. Physiol.
296
R1744-R1750
2009
Homo sapiens
brenda
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
brenda
Schuette, A.; Hedrich, J.; Stoecker, W.; Becker-Pauly, C.
Let it flow: Morpholino knockdown in zebrafish embryos reveals a pro-angiogenic effect of the metalloprotease meprin alpha2
PLoS ONE
5
e8835
2010
Danio rerio (B3DKP9), Danio rerio (Q5RHM1), Danio rerio, Homo sapiens (Q16819), Homo sapiens
brenda
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
brenda
Dickey, D.M.; Potter, L.R.
Human B-type natriuretic peptide is not degraded by meprin A
Biochem. Pharmacol.
80
1007-1011
2010
Homo sapiens
brenda
Garca-Caballero, A.; Ishmael, S.; Dang, Y.; Gillie, D.; Bond, J.; Milgram, S.; Stutts, M.
Activation of the epithelial sodium channel by the metalloprotease meprin beta subunit
Channels
5
14-22
2011
Homo sapiens
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Madoux, F.; Tredup, C.; Spicer, T.P.; Scampavia, L.; Chase, P.S.; Hodder, P.S.; Fields, G.B.; Becker-Pauly, C.; Minond, D.
Development of high throughput screening assays and pilot screen for inhibitors of metalloproteases meprin alpha and beta
Biopolymers
102
396-406
2014
Homo sapiens
brenda
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
brenda
Herzog, C.; Haun, R.S.; Ludwig, A.; Shah, S.V.; Kaushal, G.P.
ADAM10 is the major sheddase responsible for the release of membrane-associated meprin A
J. Biol. Chem.
289
13308-13322
2014
Homo sapiens, Homo sapiens (Q16819), Homo sapiens (Q16820)
brenda
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
brenda
Chaudhuri, A.; Sarkar, I.; Chakraborty, S.
Comparative analysis of binding sites of human meprins with hydroxamic acid derivative by molecular dynamics simulation study
J. Biomol. Struct. Dyn.
32
1969-1978
2014
Homo sapiens
brenda
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
brenda
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
brenda
Schulze, A.; Wermann, M.; Demuth, H.U.; Yoshimoto, T.; Ramsbeck, D.; Schlenzig, D.; Schilling, S.
Continuous assays for meprin alpha and beta using prolyl tripeptidyl aminopeptidase (PtP) from Porphyromonas gingivalis
Anal. Biochem.
559
11-16
2018
Homo sapiens (Q16819)
brenda
Chaudhuri, A.; Bera, A.K.; Sarkar, I.; Chakraborty, S.
Insights from analysis of binding sites of human meprins screening of inhibitors by molecular dynamics simulation study
Comb. Chem. High Throughput Screen.
19
246-258
2016
Homo sapiens (Q16819), Homo sapiens
brenda
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)
-
brenda
Sato, Y.; Kobayashi, D.; Kohno, T.; Kidani, Y.; Prox, J.; Becker-Pauly, C.; Hattori, M.
Determination of cleavage site of Reelin between its sixth and seventh repeat and contribution of meprin metalloproteases to the cleavage
J. Biochem.
159
305-312
2015
Mus musculus (P28825)
brenda
Becker-Pauly, C.; Rose-John, S.
Meprin and ADAM metalloproteases two sides of the same coin?
Matrix Metalloproteinase Biology (ed. Sagi I. and Gaffney J.P.)
7j
115-130
2015
Homo sapiens (Q16819)
-
brenda
Breig, O.; Yates, M.; Neaud, V.; Couchy, G.; Grigoletto, A.; Lucchesi, C.; Prox, J.; Zucman-Rossi, J.; Becker-Pauly, C.; Rosenbaum, J.
Metalloproteinase meprin alpha regulates migration and invasion of human hepatocarcinoma cells and is a mediator of the oncoprotein Reptin
Oncotarget
8
7839-7851
2017
Homo sapiens (Q16819), Homo sapiens
brenda