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additional information
-
homology modeling of the protease domain of meprin alpha on the astacin crystal structure and molecular dynamics simulation study, overview
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 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 metalloproteases belong to the astacin family of zinc endopeptidases and the metzincin superfamily
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 A, is a membrane-associated neutral metalloendoprotease that belongs to the astacin family of zinc endopeptidases
-
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
knockdown of meprin alpah1 mRNA causes defects in general tissue differentiation; meprin alpha2 morphants show severe failures in the formation of the vascular system
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
meprins show higher substrate and cleavage specificity compared to matrix metalloproteases
metabolism
-
meprins show higher substrate and cleavage specificity compared to matrix metalloproteases
metabolism
-
meprin A is more effective than meprin B, EC 3.4.24.63, in impairing MDCK epithelial barrier function
-
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
-
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 A plays a role in the regulation of B-type natriuretic peptide 1-32 bioactivity in the kidney
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; 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 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-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
-
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 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
-
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
-
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
-
the metalloproteases meprin alpha and meprin beta are involved in inflammation, neurodegeneration, cancer and fibrosis, overview
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 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
-
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
-
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
-
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
-
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(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
?
-
-
-
-
?
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 + H2O
?
-
-
-
-
?
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
-
-
?
L-Leu 2-naphthylamide + H2O
?
-
-
-
-
-
laminin + H2O
fragments of laminin
-
-
-
-
laminin 1 + H2O
?
-
human homomeric recombinant enzyme
-
-
?
laminin 5 + H2O
?
-
human homomeric recombinant enzyme
-
-
?
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
?
-
peptide of the gastrointestinal tract
-
?
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
?
-
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

?
-
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
?
-
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
?
-
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

?
-
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-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 + 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

?
-
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
?
-
-
-
-
?
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
?
-
-
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
?
-
-
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
-
-
-
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