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Information on EC 3.4.24.18 - meprin A
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3.4.24.18 meprin ASpecify your search results
Word Map
- 3.4.24.18
- renal
- metalloendopeptidase
- metalloproteases
- astacins
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brush
-
natriuretic
- actinonin
-
math
-
brush-border
- phosphoramidon
- azocasein
- sheddase
- enkephalinase
-
astacin-like
- thiorphan
- adam10
- microvillar
-
metzincins
- medicine
- pharmacology
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Hydrolysis of protein and peptide substrates preferentially on carboxyl side of hydrophobic residues
Synonyms
E-24.18, EC 3.4.24.11, Endopeptidase-2, M12.002, Meprin, meprin A, meprin A metalloprotease, meprin A metalloproteinase, meprin alpha, meprin alpha1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E-24.18
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EC 3.4.24.11
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formerly included in
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Endopeptidase-2
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Meprin
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meprin A metalloprotease
meprin A metalloproteinase
meprin alpha
Meprin-a
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meprin-alpha
metalloprotease meprin A
N-Benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase
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PABA peptide hydrolase
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PABA-peptide hydrolase
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PPH
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PPH alpha
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PPH beta
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procollagen proteinase
additional information
additional information
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meprin A from mouse, endopeptidase-2 from rat and PPH from human are closely related enzymes of the astacin family
additional information
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meprin A from mouse, endopeptidase-2 from rat and PPH from human are closely related enzymes of the astacin family
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of protein and peptide substrates preferentially on carboxyl side of hydrophobic residues
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of arylamide bond
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hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY
148938-24-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-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
?
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fluorogenic bradykinin analog substrate
-
?
annexin A1 + H2O
?
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substrate identified by 2D IEF/SDS-PAGE-based image analysis
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-
?
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
B-type natriuretic peptide 1-32 + H2O
B-type natriuretic peptide 8-32 + Ser-Pro-Lys-Met-Val-Gln-Gly
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-
-
-
?
Benzyloxycarbonyl-Glu-Lys-Lys 4-methylcoumarin 7-amide + H2O
?
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poor substrate, hydrolysis at 9.1% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
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Benzyloxycarbonyl-Val-Leu-Lys 4-methylcoumarin 7-amide + H2O
?
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poor substrate, hydrolysis at 10.4% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
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collagen type V + H2O
?
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substrate identified by 2D IEF/SDS-PAGE-based image analysis
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-
?
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
gastri-releasing peptide-(14-27) + H2O
?
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peptide of the gastrointestinal tract
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?
Glutaryl-Phe 4-methylcoumarin 7-amide + H2O
?
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poor substrate, hydrolysis at 2.4% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
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Leu-Val-Tyr 4-methylcoumarin 7-amide + H2O
?
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poor substrate, hydrolysis at 6.2% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
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Luliberin + H2O
?
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i.e. luteinizing-hormone releasing hormone, preferred cleavage site: Trp3-Ser4, other sites are Ser4-Tyr5 and Tyr5-Gly6
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luteinizing hormone releasing hormone LHRH + H2O
?
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peptide of the gastrointestinal tract
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?
lysyl oxidase + H2O
?
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substrate identified by 2D IEF/SDS-PAGE-based image analysis
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?
Parathyroid hormone + H2O
Hydrolyzed parathyroid hormone
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i.e. hPTH-(1-84), in vivo and in vitro
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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
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?
pro-KLK7 + H2O
KLK7 + ?
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meprin beta cleaves pro-KLK7 between Gly17 and Asp18
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?
protein kinase A + H2O
?
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the enzyme cleaves at defined sites, isoform-specific interactions between the catalytic subunit of PKA (PKA C) and meprins, overview
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?
protein kinase A catalytic subunit Cbeta1 + H2O
?
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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
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-
?
sCCK8NH2 + H2O
L-Asp-L-Tyr(SO3)-L-Met-Gly-L-Trp-L-Met + L-Asp-L-Phe
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peptide of the gastrointestinal tract
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?
Succinyl-Ala-Ala-Pro-Phe 4-methylcoumarin 7-amide + H2O
?
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poor substrate, hydrolysis at 9% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
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Succinyl-Ala-Pro-Ala 4-methylcoumarin 7-amide + H2O
?
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poor substrate, hydrolysis at 2.8% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
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Succinyl-Gly-Pro 4-methylcoumarin 7-amide + H2O
?
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poor substrate, hydrolysis at 10.7% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
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Succinyl-Leu-Tyr 4-methylcoumarin 7-amide + H2O
?
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poor substrate, hydrolysis at 5.6% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
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tissue growth factor-alpha + H2O
?
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meprin alpha can process tissue growth factor-alpha
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?
Tyr 4-methylcoumarin 7-amide + H2O
?
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poor substrate, hydrolysis at 3.3% the rate of succinyl-Leu-Leu-Val-Tyr 4-methylcoumarin 7-amide
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VEGF-A + H2O
?
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human meprin alpha cleaves VEGF-A in vitro, generating proteolytic fragments as found in wild-type zebrafish
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?
vinculin + H2O
?
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substrate identified by 2D IEF/SDS-PAGE-based image analysis
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?
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
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fluorogenic bradykinin analog substrate, cleavage site: Phe-Ser
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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
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fluorogenic bradykinin analog substrate, cleavage site: Phe-Ser
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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
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fluorogenic bradykinin analog substrate, cleavage site: Phe-Ser
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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
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fluorogenic bradykinin analog substrate, cleavage site: Phe-Ser
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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
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fluorogenic bradykinin analog substrate, cleavage site: Ala-Ser
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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
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fluorogenic bradykinin analog substrate, cleavage site: Ala-Ser
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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
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fluorogenic bradykinin analog substrate, cleavage site: Glu-Ser
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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
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fluorogenic bradykinin analog substrate, cleavage site: Glu-Ser
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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
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fluorogenic bradykinin analog substrate, cleavage sites: Leu-Ser (major site) and Gly-Leu
major products
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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
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fluorogenic bradykinin analog substrate, cleavage sites: Leu-Ser (major site) and Gly-Leu
major products
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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
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fluorogenic bradykinin analog substrate, cleavage sites: Gly-Lys (major site) and Lys-Ser
major products
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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
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fluorogenic bradykinin analog substrate, cleavage sites: Gly-Lys (major site) and Lys-Ser
major products
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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
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fluorogenic bradykinin analog substrates, cleavage site: Phe-Ser
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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
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fluorogenic bradykinin analog substrates, cleavage site: Phe-Ser
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alpha-melanocyte stimulating hormone + H2O
?
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i.e. acetyl-Ser-Tyr-Ser-Met-Gly-His-Phe-Arg-Trp-Gly-Lys-Pro-Val, cleavage sites: Ser-Met, Gly-Lys, mouse
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alpha-melanocyte stimulating hormone + H2O
?
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peptide of the gastrointestinal tract
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?
alpha-melanocyte-stimulating hormone + H2O
?
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human homomeric recombinant enzyme
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?
alpha-melanocyte-stimulating hormone + H2O
?
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murine homomeric recombinant enzyme
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?
Angiotensin I + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe + Ile-His-Pro-Phe-His-Leu
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2 cleavage sites: Tyr-Ile and Phe-His
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Angiotensin I + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe + Ile-His-Pro-Phe-His-Leu
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i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu, cleavage site: Tyr-Ile
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Angiotensin I + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe + Ile-His-Pro-Phe-His-Leu
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i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu, cleavage site: Tyr-Ile
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-
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Angiotensin I + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe + Ile-His-Pro-Phe-His-Leu
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i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu, cleavage site: Tyr-Ile
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-
-
Angiotensin I + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe + Ile-His-Pro-Phe-His-Leu
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i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu, cleavage site: Tyr-Ile
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-
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Angiotensin II + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
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cleavage site: Tyr-Ile
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Angiotensin II + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
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cleavage site: Tyr-Ile
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Angiotensin II + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
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i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
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Angiotensin II + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
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i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
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-
-
Angiotensin II + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
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poor substrate
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-
Angiotensin II + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
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cleavage site: Tyr-Ile
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-
Angiotensin II + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
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cleavage site: Tyr-Ile
-
-
-
Angiotensin II + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
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i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
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Angiotensin II + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
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i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe
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-
-
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
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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
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-
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
fragments of azocasein
-
excellent substrate for mouse, poorer substrate for rat and human enzymes
-
-
-
azocasein + H2O
fragments of azocasein
-
excellent substrate for mouse, poorer substrate for rat and human enzymes
-
-
-
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
-
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
?
-
meprin A degrades rat BNP but not human BNP
-
-
?
benzoyl-Gly-His-Leu + H2O
?
-
very poor substrate, t1/2 of more than 16 h
-
-
-
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
-
-
-
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
-
one cleavage site: Phe-Ser
-
-
-
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
-
-
-
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
-
-
?
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
-
7 major and 3 minor sites
-
-
-
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
-
7 major and 3 minor sites
-
-
-
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
prevalent cleavage sites are Gly20-Glu21, Phe24-Phe25 and Phe25-Tyr26
-
-
-
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
prevalent cleavage sites are Gly20-Glu21, Phe24-Phe25 and Phe25-Tyr26
15 different peptide fragments
-
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
the others are Leu6-Cys(SO3-)7, Ala14-Leu15, Gly8-Ser9, His10-Leu11, Leu15-Tyr16, His5-Leu6 and Leu17-Val18
13 different peptide fragments
-
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
10 cleavage sites
15 different peptide fragments
-
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
7 major and 3 minor sites
-
-
-
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
oxidized form
15 different peptide fragments
-
Insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
oxidized form
13 different peptide fragments
-
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
-
7 major and 3 minor sites
-
-
-
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
-
-
?
luteinizing-hormone-releasing hormone + H2O
?
-
human homomeric recombinant enzyme
-
-
?
luteinizing-hormone-releasing hormone + H2O
?
-
murine homomeric recombinant enzyme
-
-
?
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
-
-
-
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
?
-
i.e. pyro-Glu-Leu-Tyr-Glu-Asn-Lys-Pro-Arg-Arg-Pro-Tyr-Ile-Leu, mouse, rat, cleavage sites: Glu-Asn, Asn-Lys
-
-
-
occludin + H2O
?
-
recombinant 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
?
-
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
?
-
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
?
-
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
?
-
murine homomeric recombinant enzyme
-
-
?
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
-
-
?
Substance P + H2O
Hydrolyzed substance P
-
cleavage sites: Glu6-Phe7, Phe7-Phe8, Phe8-Gly9
-
-
-
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
-
-
-
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
?
-
peptide of the gastrointestinal tract
-
?
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
?
-
-
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
?
-
-
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
?
-
-
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
procollagen I + H2O
collagen I + propeptide of collagen III
-
meprin alpha removes both the C- and N-propeptides of type I procollagen, subsequently releasing fibril-forming mature collagen molecules. The C-terminal cleavage sites in the proalpha1(I) chain generated by the enzyme is identified as Ala1218/Asp1219, identical to the BMP-1 cleavage site, and also Arg1227/Asp1228, nine residues C-terminal to the BMP-1 cleavage site
-
-
?
protein kinase A + H2O
?
-
the enzyme cleaves at defined sites, isoform-specific interactions between the catalytic subunit of PKA (PKA C) and meprins, overview
-
-
?
tissue growth factor-alpha + H2O
?
-
meprin alpha can process tissue growth factor-alpha
-
-
?
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
-
-
?
Parathyroid hormone + H2O
?
-
involved in PTH-degradation in human kidney
-
-
-
additional information
?
-
-
no activity with claudin-4 in MDCK cells
-
-
-
additional information
?
-
-
no activity with claudin-4 in MDCK cells
-
-
-
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
?
-
-
cleaves growth factors, extracellular matrix proteins, and biological active peptides
-
?
additional information
?
-
-
the enzyme is capable of hydrolyzing and processing a large number of substrates, including extracellular matrix proteins, cytokines, adherens junction proteins, hormones, bioactive peptides, and cell surface proteins
-
-
-
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
?
-
-
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.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Calcium
Zinc
Zn2+
additional information
Calcium
-
3 mol calcium per mol subunit (atomic absorption spectroscopy); Ca2+ reactivates inactive apoenzyme; metalloendopeptidase
Calcium
-
3 mol calcium per mol subunit (atomic absorption spectroscopy); metalloendopeptidase; tightly bound, no addition of Ca2+ required
Calcium
-
3 mol calcium per mol subunit (atomic absorption spectroscopy); Ca2+ reactivates inactive apoenzyme; metalloendopeptidase
Calcium
-
3 mol calcium per mol subunit (atomic absorption spectroscopy); Ca2+ reactivates inactive apoenzyme; metalloendopeptidase
Zinc
-
metalloendopeptidase; zinc binding motif; Zn2+ reactivates inactive apoenzyme
Zinc
-
1 mol zinc per mol subunit (atomic absorption spectroscopy); metalloendopeptidase; tightly bound, no addition of Zn2+ required
Zinc
-
1 mol zinc per mol subunit (atomic absorption spectroscopy); metalloendopeptidase; zinc binding motif; Zn2+ reactivates inactive apoenzyme
Zinc
-
metalloendopeptidase; zinc binding motif; Zn2+ reactivates inactive apoenzyme
Zn2+
-
meprin alpha is a metalloprotease of the astacin family characterized by a conserved zinc-binding motif (HExxHxxGFxHExxRxDR)
additional information
-
considerable stimulation of azocasein hydrolysis at ionic strength values up to 0.15-0.2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-(N-Hydroxycarboxamido)-4-methylpentanoyl-L-alanyl-glycylamide
-
i.e. Zinkov inhibitor
3-[(E)-[4-formyl-5-hydroxy-6-methyl-3-[(phosphonooxy)methyl]pyridin-2-yl]diazenyl]-7-nitronaphthalene-1,5-disulfonic acid
-
competitive inhibition
N-[1-[(1-amino-1-oxopropan-2-yl)amino]-3-(naphthalen-1-yl)-1-oxopropan-2-yl]-4-(hydroxyamino)-2-(2-methylpropyl)pent-4-enamide
-
-
N-[4-(hydroxyamino)-2-(2-methylpropyl)pent-4-enoyl]-3-methylvalyl-N-(2-aminoethyl)-DL-alaninamide
-
-
N4-hydroxy-N1-[3-(1H-indol-3-yl)-1-(methylamino)-1-oxopropan-2-yl]-2-(2-methylpropyl)butanediamide
-
-
verapamil
-
verapamil at 1 mg/kg, i.v. can efficiently prevent the ischemic acute kidney injury in female rats, as well as male rats
actinonin
-
a hydroxamate derivate and naturally occurring compound produced in actinomycetes. Hydroxamate inhibitors chelate the zinc ion in the active site
actinonin
-
i.e. 3-[[1-[[2-(hydroxymethyl)-1-pyrolidinyl]carbonyl]-2-methylpropyl]carbamoyl]octano hydroxamic acid, strong, kinetics
actinonin
-
in a mouse model of sepsis induced by cecal ligation puncture that results in elevated levels of serum interleukin 1beta, meprin inhibitor actinonin significantly reduces levels of serum interleukin 1beta
actinonin
-
a hydroxamate derivate and naturally occurring compound produced in actinomycetes. Hydroxamate inhibitors chelate the zinc ion in the active site
actinonin
-
pre-ischemic treatment with actinonin at 10 or 30 mg/kg, i.v. dose-ependently attenuates the ischemia/reperfusion-induced renal injury in male rats, but fails to improve the renal injury in female rats
EDTA
-
restored by divalent metal ions, Zn2+ being more effective than Ca2+ or Mg2+
Pro-Leu-Gly-hydroxamate
-
binding structure in S subsites, overview. A decrease in solvent accessibility values at specific residues upon inhibitor binding occurs. The S subsite of the enzyme interacts with residues at P site of the inhibitor
additional information
-
amastatin, bestatin, puromycin, N-tosyl-L-Phe chloromethyl ketone, monoclonal antibody HBB 3/716/36; iodoacetate; leupeptin; no inhibition by phosphoramidon; PMSF, pepstatin
-
additional information
-
inhibitors of elastase, aminopeptidase, serine, aspartic or cysteic proteases; no inhibition by phosphoramidon
-
additional information
-
3,4-dichloroisocoumarin; iodoacetate; no inhibition by phosphoramidon; PMSF, pepstatin; soybean trypsin inhibitor
-
additional information
-
inhibitor screening, overview. Poor inhibition by NF449, a suramin analogue
-
additional information
-
binding sites and binding structure of hydroxamic acid derivative inhibitors, molecular dynamics simulation study, overview
-
additional information
-
diisopropyl phosphofluoridate, p-hydroxymercuribenzoate, phenylmercurisulfonate, antipain, cystine, oxidized glutathione; iodoacetate; leupeptin; no inhibition by phosphoramidon; PMSF, pepstatin
-
additional information
-
iodoacetate; L-trans-epoxysuccinyl-leucylamido-(4-guanidino)-butane (i.e. E-64); no inhibition by phosphoramidon; soybean trypsin inhibitor
-
additional information
-
3,4-dichloroisocoumarin; iodoacetate; no inhibition by phosphoramidon; PMSF, pepstatin; soybean trypsin inhibitor
-
additional information
-
hippuryl-His-Leu, His-Leu, benzamidine; soybean trypsin inhibitor
-
additional information
-
leupeptin; L-trans-epoxysuccinyl-leucylamido-(4-guanidino)-butane (i.e. E-64); NEM, tissue inhibitor of metalloproteinases; no inhibition by phosphoramidon; PMSF, pepstatin; soybean trypsin inhibitor
-
additional information
-
3,4-dichloroisocoumarin; iodoacetate; no inhibition by phosphoramidon; PMSF, pepstatin; soybean trypsin inhibitor
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
alpha- and beta-tryptase, urokinase plasminogen activator, KLK2, KLK6, KLK7, and KLK11 do not activate meprin alpha and beta
-
additional information
-
contrary to meprin B only very little activation by trypsin treatment
-
additional information
-
no activation by organomercurials or trypsin treatment
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
gastrin
-
hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 between 8-30 min
0.0732
orcokinin
-
hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 between 8-30 min
0.0296
protein GRP
-
meprin A hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 between 8-30 min
-
additional information
additional information
-
Michaelis-Menten enzyme kinetics, overview
-
0.0223
alpha-MSH
-
meprin A hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 between 8-30 min
0.292
alpha-MSH
-
hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 between 8-30 min
0.101
bradykinin
-
meprin A hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 between 8-30 min
0.125
bradykinin
-
hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 between 8-30 min
0.0565
LHRH
-
hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 between 8-30 min
-
0.156
LHRH
-
meprin A hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 for between 8-30 min
-
0.018
protein PTH12-34
-
hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 between 8-30 min
0.0672
protein PTH12-34
-
meprin A hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 between 8-30 min
0.0339
secretin
-
hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 between 8-30 min
0.111
secretin
-
meprin A hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 between 8-30 min
0.0306
Substance P
-
meprin A hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 between 8-30 min
0.0413
Substance P
-
hydrolysis in 20 mM Tris-HCl, 150 mM NaCl, pH 7.5 between 8-30 min
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00053
DL-Pro-DL-Leu-Gly-NH2
-
pH and temperature not specified in the publication
0.0004
N-isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid
-
pH 7.5, 37°C
0.0022
N-[1-[(1-amino-1-oxopropan-2-yl)amino]-3-(naphthalen-1-yl)-1-oxopropan-2-yl]-4-(hydroxyamino)-2-(2-methylpropyl)pent-4-enamide
-
pH and temperature not specified in the publication
0.0015
N-[4-(hydroxyamino)-2-(2-methylpropyl)pent-4-enoyl]-3-methylvalyl-N-(2-aminoethyl)-DL-alaninamide
-
pH and temperature not specified in the publication
0.0004
N4-hydroxy-N1-[3-(1H-indol-3-yl)-1-(methylamino)-1-oxopropan-2-yl]-2-(2-methylpropyl)butanediamide
-
pH and temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.067
3-[(E)-[4-formyl-5-hydroxy-6-methyl-3-[(phosphonooxy)methyl]pyridin-2-yl]diazenyl]-7-nitronaphthalene-1,5-disulfonic acid
Homo sapiens
-
pH 7.5, 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.9
additional information
additional information
-
4.6673 mg azocasein/min/mg (untreated enzyme), 7.2512 mg azocasein/min/mg (trypsin-treated enzyme)
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
7.5
additional information
additional information
-
marked microheterogeneity due to glycosylation with pIs in the range of 6-6.85
additional information
-
pI: multiple bonds in the range of 4-5, presumably due to glycosylation
additional information
-
pI: multiple bonds in the range of 4-5, presumably due to glycosylation
additional information
-
pI: multiple bonds in the range of 4-5, presumably due to glycosylation
additional information
-
pI: multiple bonds in the range of 4-5, presumably due to glycosylation
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
667471, 685446, 687981, 688204, 707623, 710819, 717227, 717474, 733064, 733519, 734259, 734296, 734332, 734610
-
-
brenda
-
31018, 31019, 31022, 31026, 31028, 31030, 669250, 685446, 696035, 711053, 713492, 733064, 733065, 733066, 733288, 733947, 734296, 734610, 735169
-
-
brenda
db/db mice lacking the hypothalamic leptin receptor, representing a model of type 2 diabetes mellitus
-
-
brenda
random bred ICR and at least 35 inbred, recombinant and congenic strains
-
-
brenda
treated with streptozocin, representing a model of type 1 diabetes mellitus
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
in human epidermis, meprin alpha is expressed exclusively in the keratinocytes of the stratum basale
brenda
-
in human epidermis, meprin beta is restricted to the cells of the stratum granulosum
brenda
additional information
-
in human epidermis, meprin alpha is expressed exclusively in the keratinocytes of the stratum basale, whereas meprin beta is restricted to the cells of the stratum granulosum
brenda
-
higher specific activity in distal ileum than in proximal duodenum
brenda
-
; higher specific activity in distal ileum than in proximal duodenum
-
brenda
-
meprin A distribution in the mouse kidney, immunolacalization, overview
brenda
-
the enzyme is abundantly expressed in the brush border membranes of kidney proximal tubules. Localization of meprin A in the glomeruli of diabetic kidneys
brenda
-
meprin A distribution in the mouse kidney, immunolacalization, overview
-
brenda