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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
-
3.4.24.11
- enkephalinase
- metalloendopeptidase
- atrial
- phosphoramidon
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natriuretic
- enkephalin
- thiorphan
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angiotensin-converting
- angiotensin
- astacins
- metalloproteases
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brush
- bradykinin
-
3.4.15.1
- captopril
- neprilysin
- metallopeptidases
- anp
- aminopeptidases
- acetorphan
-
math
- endopeptidases
-
brush-border
- microvillar
- actinonin
- calla
- bestatin
- amastatin
- azocasein
-
phosphoramidon-sensitive
- sheddase
-
dipeptidylaminopeptidase
-
metzincins
- pharmacology
- neurokinins
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astacin-like
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met5enkephalin
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depressor
- medicine
- tachykinins
- neurotensin
- leu-enkephalin
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Hydrolysis of protein and peptide substrates preferentially on carboxyl side of hydrophobic residues
Synonyms
meprin, meprin a, meprin alpha, mep1a, meprin beta, meprin-a, meprin-alpha, endopeptidase-2, pph alpha, mouse meprin alpha, 
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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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MEP1A
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
?
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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
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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-
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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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?
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
?
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
?
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
?
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
?
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
-
?
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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-
?
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
-
-
?
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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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
-
-
?
angiotensin II + H2O
Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
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poor substrate
-
?
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
-
-
?
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
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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