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Literature summary extracted from

  • Wolz, R.L.; Bond, J.S.
    Meprins A and B (1995), Methods Enzymol., 248, 325-345.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.4.24.63 Trypsin
-
 Rattus norvegicus
3.4.24.63 Trypsin only with larger substrates (azocasein or insulin B), not smaller substrates Mus musculus
3.4.24.63 Trypsin by limited proteolysis (2 h at 37°C, with tosyl-Phe chloromethyl ketone treated trypsin, in 20 mM Tris-HCl buffer, pH 7.5) Mus musculus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.24.18 mouse Mus musculus
3.4.24.18 mouse Homo sapiens
3.4.24.18 mouse Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.18 1,10-phenanthroline
-
 Homo sapiens
3.4.24.18 1,10-phenanthroline
-
 Mus musculus
3.4.24.18 1,10-phenanthroline
-
 Rattus norvegicus
3.4.24.18 2-mercaptoethanol
-
 Homo sapiens
3.4.24.18 2-mercaptoethanol
-
 Mus musculus
3.4.24.18 2-mercaptoethanol
-
 Rattus norvegicus
3.4.24.18 Acetyl-Arg-Pro-Gly-Tyr hydroxamate kinetics Mus musculus
3.4.24.18 actinonin i.e. 3-[[1-[[2-(hydroxymethyl)-1-pyrolidinyl]carbonyl]-2-methylpropyl]carbamoyl]octano hydroxamic acid, strong, kinetics Mus musculus
3.4.24.18 Arg-Pro-Pro-Gly-(4-nitro)Phe-Glu-Pro-Phe-Arg
-
 Mus musculus
3.4.24.18 captopril not Homo sapiens
3.4.24.18 captopril not Mus musculus
3.4.24.18 captopril not Rattus norvegicus
3.4.24.18 cysteine
-
 Homo sapiens
3.4.24.18 cysteine
-
 Mus musculus
3.4.24.18 cysteine
-
 Rattus norvegicus
3.4.24.18 EDTA reversed by Zn2+ Homo sapiens
3.4.24.18 EDTA reversed by Zn2+ Mus musculus
3.4.24.18 EDTA reversed by Zn2+ Rattus norvegicus
3.4.24.18 Hydroxamyl-succinyl-Pro-Phe-Arg kinetics Mus musculus
3.4.24.18 additional information 3,4-dichloroisocoumarin; iodoacetate; no inhibition by phosphoramidon; PMSF, pepstatin; soybean trypsin inhibitor Homo sapiens
3.4.24.18 additional information 3,4-dichloroisocoumarin; iodoacetate; no inhibition by phosphoramidon; PMSF, pepstatin; soybean trypsin inhibitor Mus musculus
3.4.24.18 additional information 3,4-dichloroisocoumarin; iodoacetate; no inhibition by phosphoramidon; PMSF, pepstatin; soybean trypsin inhibitor Rattus norvegicus
3.4.24.63 1,10-phenanthroline strong Mus musculus
3.4.24.63 2-mercaptoethanol
-
 Mus musculus
3.4.24.63 cysteine
-
 Mus musculus
3.4.24.63 EDTA strong Mus musculus
3.4.24.63 additional information no inhibition by captopril, PMSF, pepstatin; phosphoramidon, iodoacetic acid, 3,4-dichloroisocoumarin or soybean trypsin inhibitor Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.24.18 0.174
-
 Arg-Pro-Pro-Gly-(4-nitro)Phe-Arg-Pro-Phe-Arg
-
 Mus musculus
3.4.24.18 0.182
-
 Arg-Pro-Pro-Gly-(4-nitro)Phe-Lys-Pro-Phe-Arg
-
 Mus musculus
3.4.24.18 0.183
-
 2-Aminobenzoyl-Arg-Hyp-Gly-Phe-Ser-Pro-(4-nitro)Phe-Arg
-
 Mus musculus
3.4.24.18 0.22
-
 2-Aminobenzoyl-Arg-Gly-Pro-Phe-Ser-Pro-(4-nitro)Phe-Arg
-
 Mus musculus
3.4.24.18 0.226
-
 Arg-Pro-Pro-Gly-(4-nitro)Phe-Phe-Pro-Phe-Arg
-
 Mus musculus
3.4.24.18 0.29
-
 Arg-Pro-Pro-Gly-(4-nitro)Phe-Ser-Pro-Phe-Arg
-
 Mus musculus
3.4.24.18 0.296
-
 2-Aminobenzoyl-Arg-Pro-Ile-Phe-Ser-Pro-(4-nitro)Phe-Arg
-
 Mus musculus
3.4.24.18 0.331
-
 Arg-Pro-Pro-Gly-(4-nitro)Phe-Ala-Pro-Phe-Arg
-
 Mus musculus
3.4.24.18 0.402
-
 2-Aminobenzoyl-Arg-Pro-Gly-Lys-Ser-Pro-(4-nitro)Phe-Arg
-
 Mus musculus
3.4.24.18 1.22
-
 2-Aminobenzoyl-Arg-Pro-Gly-Glu-Ser-Pro-(4-nitro)Phe-Arg
-
 Mus musculus
3.4.24.18 1.38
-
 2-Aminobenzoyl-Arg-Pro-Gly-Ala-Ser-Pro-(4-nitro)Phe-Arg
-
 Mus musculus
3.4.24.18 2.46
-
 2-Aminobenzoyl-Arg-Pro-Gly-Leu-Ser-Pro-(4-nitro)Phe-Arg
-
 Mus musculus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.24.18 membrane
-
 Homo sapiens 16020
-
3.4.24.18 membrane renal brush border membrane Mus musculus 16020
-
3.4.24.18 membrane renal brush border membrane Rattus norvegicus 16020
-
3.4.24.63 membrane
-
 Rattus norvegicus 16020
-
3.4.24.63 membrane renal brush-border membrane Mus musculus 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.24.18 Calcium metalloendopeptidase Mus musculus
3.4.24.18 Calcium metalloendopeptidase Homo sapiens
3.4.24.18 Calcium metalloendopeptidase Rattus norvegicus
3.4.24.18 Calcium 3 mol calcium per mol subunit (atomic absorption spectroscopy) Mus musculus
3.4.24.18 Calcium 3 mol calcium per mol subunit (atomic absorption spectroscopy) Homo sapiens
3.4.24.18 Calcium 3 mol calcium per mol subunit (atomic absorption spectroscopy) Rattus norvegicus
3.4.24.18 Calcium Ca2+ reactivates inactive apoenzyme Mus musculus
3.4.24.18 Calcium Ca2+ reactivates inactive apoenzyme Homo sapiens
3.4.24.18 Calcium Ca2+ reactivates inactive apoenzyme Rattus norvegicus
3.4.24.18 additional information Cu2+ does not reactivate inactive apoenzyme Mus musculus
3.4.24.18 additional information Cu2+ does not reactivate inactive apoenzyme Homo sapiens
3.4.24.18 additional information Cu2+ does not reactivate inactive apoenzyme Rattus norvegicus
3.4.24.18 Zinc metalloendopeptidase Mus musculus
3.4.24.18 Zinc metalloendopeptidase Homo sapiens
3.4.24.18 Zinc metalloendopeptidase Rattus norvegicus
3.4.24.18 Zinc 1 mol zinc per mol subunit (atomic absorption spectroscopy) Mus musculus
3.4.24.18 Zinc zinc binding motif Mus musculus
3.4.24.18 Zinc zinc binding motif Homo sapiens
3.4.24.18 Zinc zinc binding motif Rattus norvegicus
3.4.24.18 Zinc Zn2+ reactivates inactive apoenzyme Mus musculus
3.4.24.18 Zinc Zn2+ reactivates inactive apoenzyme Homo sapiens
3.4.24.18 Zinc Zn2+ reactivates inactive apoenzyme Rattus norvegicus
3.4.24.63 additional information metalloendopeptidase according to inhibition profile Mus musculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.24.18 additional information
-
-
 Homo sapiens
3.4.24.18 additional information
-
 amino acid sequence, domain structure and tertiary structure deduced from cDNAs Mus musculus
3.4.24.18 additional information
-
 amino acid sequence, domain structure and tertiary structure deduced from cDNAs Rattus norvegicus
3.4.24.18 85000
-
 4 * 85000, mouse Mus musculus
3.4.24.18 85000
-
 4 * 85000, mouse Rattus norvegicus
3.4.24.18 90000
-
 x * 90000, mouse, SDS-PAGE, reducing conditions Mus musculus
3.4.24.18 90000
-
 x * 90000, mouse, SDS-PAGE, reducing conditions Rattus norvegicus
3.4.24.18 270000 320000 mouse, gel filtration Mus musculus
3.4.24.18 320000
-
 mouse, gel filtration, SDS-PAGE in the absence of 2-mercaptoethanol Mus musculus
3.4.24.63 additional information
-
 amino acid composition and secondary structure similar to meprin A Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.18 Homo sapiens
-
 PPH
-
3.4.24.18 Homo sapiens PPH
-
 PPH
-
3.4.24.18 Mus musculus
-
 random bred ICR and at least 35 inbred, recombinant and congenic strains
-
3.4.24.18 Rattus norvegicus
-
-
-
3.4.24.63 Homo sapiens
-
-
-
3.4.24.63 Mus musculus
-
 more than 20 inbred, recombinant and congenic strains
-
3.4.24.63 Mus musculus
-
 inbred strain C3H/He
-
3.4.24.63 Mus musculus
-
 male adults
-
3.4.24.63 Rattus norvegicus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.4.24.18 glycoprotein no sialic acid Mus musculus
3.4.24.18 glycoprotein no sialic acid Homo sapiens
3.4.24.18 glycoprotein no sialic acid Rattus norvegicus

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.24.18
-
 Mus musculus
3.4.24.63 C3H/He mouse Mus musculus
3.4.24.63 papain-solubilized Mus musculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.24.63 small intestine
-
 Mus musculus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.24.18 additional information
-
 3.25-13 mg azocasein/min/mg Mus musculus
3.4.24.18 additional information
-
 3.25-13 mg azocasein/min/mg Homo sapiens
3.4.24.18 additional information
-
 3.25-13 mg azocasein/min/mg Rattus norvegicus
3.4.24.63 additional information
-
-
 Mus musculus

Storage Stability

EC Number Storage Stability Organism
3.4.24.18 -20°C, 1 mg enzyme/ml, more than a year with little loss of activity Mus musculus
3.4.24.18 4°C, 1 mg enzyme/ml at least 2 weeks with little loss of activity Mus musculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.18 2-aminobenzoyl-Arg-Gly-Pro-Phe-Ser-Pro-(4-nitro)Phe-Arg + H2O fluorogenic bradykinin analog substrate, cleavage site: Phe-Ser Mus musculus 2-aminobenzoyl-Arg-Gly-Pro-Phe + Ser-Pro-(4-nitro)Phe-Arg
-
 ?
3.4.24.18 2-aminobenzoyl-Arg-Hyp-Gly-Phe-Ser-Pro-(4-nitro)Phe-Arg + H2O fluorogenic bradykinin analog substrate, cleavage site: Phe-Ser Mus musculus 2-aminobenzoyl-Arg-Hyp-Gly-Phe + Ser-Pro-(4-nitro)Phe-Arg
-
 ?
3.4.24.18 2-aminobenzoyl-Arg-Pro-Gly-Ala-Ser-Pro-(4-nitro)Phe-Arg + H2O fluorogenic bradykinin analog substrate, cleavage site: Ala-Ser Mus musculus 2-aminobenzoyl-Arg-Pro-Gly-Ala + Ser-Pro-(4-nitro)Phe-Arg
-
 ?
3.4.24.18 2-aminobenzoyl-Arg-Pro-Gly-Glu-Ser-Pro-(4-nitro)Phe-Arg + H2O fluorogenic bradykinin analog substrate, cleavage site: Glu-Ser Mus musculus 2-aminobenzoyl-Arg-Pro-Gly-Glu + Ser-Pro-(4-nitro)Phe-Arg
-
 ?
3.4.24.18 2-aminobenzoyl-Arg-Pro-Gly-Leu-Ser-Pro-(4-nitro)Phe-Arg + H2O fluorogenic bradykinin analog substrate, cleavage sites: Leu-Ser (major site) and Gly-Leu Mus musculus 2-aminobenzoyl-Arg-Pro-Gly-Leu + Ser-Pro-(4-nitro)Phe-Arg major products ?
3.4.24.18 2-aminobenzoyl-Arg-Pro-Gly-Lys-Ser-Pro-(4-nitro)Phe-Arg + H2O fluorogenic bradykinin analog substrate, cleavage sites: Gly-Lys (major site) and Lys-Ser Mus musculus 2-aminobenzoyl-Arg-Pro-Gly + Lys-Ser-Pro-(4-nitro)Phe-Arg major products ?
3.4.24.18 2-aminobenzoyl-Arg-Pro-Ile-Phe-Ser-Pro-(4-nitro)Phe-Arg + H2O fluorogenic bradykinin analog substrates, cleavage site: Phe-Ser Mus musculus 2-aminobenzoyl-Arg-Pro-Ile-Phe + Ser-Pro-(4-nitro)Phe-Arg
-
 ?
3.4.24.18 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 Mus musculus ?
-
 ?
3.4.24.18 angiotensin I + H2O i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu, cleavage site: Tyr-Ile Mus musculus Asp-Arg-Val-Tyr + Ile-His-Pro-Phe + Ile-His-Pro-Phe-His-Leu
-
 ?
3.4.24.18 angiotensin I + H2O i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu, cleavage site: Tyr-Ile Homo sapiens Asp-Arg-Val-Tyr + Ile-His-Pro-Phe + Ile-His-Pro-Phe-His-Leu
-
 ?
3.4.24.18 angiotensin I + H2O i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu, cleavage site: Tyr-Ile Rattus norvegicus Asp-Arg-Val-Tyr + Ile-His-Pro-Phe + Ile-His-Pro-Phe-His-Leu
-
 ?
3.4.24.18 angiotensin II + H2O cleavage site: Tyr-Ile Mus musculus Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
 ?
3.4.24.18 angiotensin II + H2O cleavage site: Tyr-Ile Homo sapiens Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
 ?
3.4.24.18 angiotensin II + H2O cleavage site: Tyr-Ile Rattus norvegicus Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
 ?
3.4.24.18 angiotensin II + H2O i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe Mus musculus Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
 ?
3.4.24.18 angiotensin II + H2O i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe Homo sapiens Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
 ?
3.4.24.18 angiotensin II + H2O i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe Rattus norvegicus Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
 ?
3.4.24.18 angiotensin III + H2O i.e. Arg-Val-Tyr-Ile-His-Pro-Phe, cleavage site: Tyr-Ile Mus musculus Arg-Val-Tyr + Ile-His-Pro-Phe
-
 ?
3.4.24.18 angiotensin III + H2O i.e. Arg-Val-Tyr-Ile-His-Pro-Phe, cleavage site: Tyr-Ile Homo sapiens Arg-Val-Tyr + Ile-His-Pro-Phe
-
 ?
3.4.24.18 angiotensin III + H2O i.e. Arg-Val-Tyr-Ile-His-Pro-Phe, cleavage site: Tyr-Ile Rattus norvegicus Arg-Val-Tyr + Ile-His-Pro-Phe
-
 ?
3.4.24.18 Arg-Pro-Pro-Gly-(4-nitro)Phe-Ala-Pro-Phe-Arg + H2O chromogenic bradykinin analog Mus musculus Arg-Pro-Pro-Gly-(4-nitro)Phe + Ala-Pro-Phe-Arg
-
 ?
3.4.24.18 Arg-Pro-Pro-Gly-(4-nitro)Phe-Arg-Pro-Phe-Arg + H2O chromogenic bradykinin analog Mus musculus Arg-Pro-Pro-Gly-(4-nitro)Phe + Arg-Pro-Phe-Arg
-
 ?
3.4.24.18 Arg-Pro-Pro-Gly-(4-nitro)Phe-Lys-Pro-Phe-Arg + H2O chromogenic bradykinin analog Mus musculus Arg-Pro-Pro-Gly-(4-nitro)Phe + Lys-Pro-Phe-Arg
-
 ?
3.4.24.18 Arg-Pro-Pro-Gly-(4-nitro)Phe-Phe-Pro-Phe-Arg + H2O chromogenic bradykinin analog Mus musculus Arg-Pro-Pro-Gly-(4-nitro)Phe + Phe-Pro-Phe-Arg
-
 ?
3.4.24.18 Arg-Pro-Pro-Gly-(4-nitro)Phe-Ser-Pro-Phe-Arg + H2O i.e. nitrobradykinin, chromogenic bradykinin analog Mus musculus Arg-Pro-Pro-Gly-(4-nitro)Phe + Ser-Pro-Phe-Arg
-
 ?
3.4.24.18 azocasein + H2O excellent substrate for mouse, poorer substrate for rat and human enzymes Mus musculus fragments of azocasein
-
 ?
3.4.24.18 azocasein + H2O excellent substrate for mouse, poorer substrate for rat and human enzymes Homo sapiens fragments of azocasein
-
 ?
3.4.24.18 azocasein + H2O excellent substrate for mouse, poorer substrate for rat and human enzymes Rattus norvegicus fragments of azocasein
-
 ?
3.4.24.18 azocasein + H2O excellent substrate for mouse, poorer substrate for rat and human enzymes Homo sapiens PPH fragments of azocasein
-
 ?
3.4.24.18 Big endothelin I + H2O rat Rattus norvegicus ?
-
 ?
3.4.24.18 bradykinin + H2O
-
 Mus musculus Arg-Pro-Pro-Gly + Phe-Ser-Pro-Phe-Arg
-
 ?
3.4.24.18 bradykinin + H2O
-
 Homo sapiens Arg-Pro-Pro-Gly + Phe-Ser-Pro-Phe-Arg
-
 ?
3.4.24.18 bradykinin + H2O
-
 Rattus norvegicus Arg-Pro-Pro-Gly + Phe-Ser-Pro-Phe-Arg
-
 ?
3.4.24.18 Endothelin I + H2O rat Rattus norvegicus ?
-
 ?
3.4.24.18 Gonadotropin + H2O mouse Mus musculus ?
-
 ?
3.4.24.18 Human alpha-atrial natiuretic peptide + H2O rat Rattus norvegicus ?
-
 ?
3.4.24.18 Human transforming growth factor + H2O rat Rattus norvegicus ?
-
 ?
3.4.24.18 Insulin B-chain + H2O prevalent cleavage sites are Gly20-Glu21, Phe24-Phe25 and Phe25-Tyr26 Mus musculus Hydrolyzed insulin B-chain
-
 ?
3.4.24.18 Insulin B-chain + H2O prevalent cleavage sites are Gly20-Glu21, Phe24-Phe25 and Phe25-Tyr26 Homo sapiens Hydrolyzed insulin B-chain
-
 ?
3.4.24.18 Insulin B-chain + H2O prevalent cleavage sites are Gly20-Glu21, Phe24-Phe25 and Phe25-Tyr26 Rattus norvegicus Hydrolyzed insulin B-chain
-
 ?
3.4.24.18 Insulin B-chain + H2O 10 cleavage sites Mus musculus Hydrolyzed insulin B-chain
-
 ?
3.4.24.18 Insulin B-chain + H2O 10 cleavage sites Homo sapiens Hydrolyzed insulin B-chain
-
 ?
3.4.24.18 Insulin B-chain + H2O 10 cleavage sites Rattus norvegicus Hydrolyzed insulin B-chain
-
 ?
3.4.24.18 Insulin B-chain + H2O 7 major and 3 minor sites Mus musculus Hydrolyzed insulin B-chain
-
 ?
3.4.24.18 Insulin B-chain + H2O 7 major and 3 minor sites Homo sapiens Hydrolyzed insulin B-chain
-
 ?
3.4.24.18 Insulin B-chain + H2O 7 major and 3 minor sites Rattus norvegicus Hydrolyzed insulin B-chain
-
 ?
3.4.24.18 Insulin B-chain + H2O oxidized form Mus musculus Hydrolyzed insulin B-chain
-
 ?
3.4.24.18 Insulin B-chain + H2O oxidized form Homo sapiens Hydrolyzed insulin B-chain
-
 ?
3.4.24.18 Insulin B-chain + H2O oxidized form Rattus norvegicus Hydrolyzed insulin B-chain
-
 ?
3.4.24.18 Insulin B-chain + H2O prevalent cleavage sites are Gly20-Glu21, Phe24-Phe25 and Phe25-Tyr26 Homo sapiens PPH Hydrolyzed insulin B-chain
-
 ?
3.4.24.18 Insulin B-chain + H2O 10 cleavage sites Homo sapiens PPH Hydrolyzed insulin B-chain
-
 ?
3.4.24.18 Insulin B-chain + H2O 7 major and 3 minor sites Homo sapiens PPH Hydrolyzed insulin B-chain
-
 ?
3.4.24.18 Insulin B-chain + H2O oxidized form Homo sapiens PPH Hydrolyzed insulin B-chain
-
 ?
3.4.24.18 N-Benzoyl-L-tyrosyl-4-aminobenzoate + H2O i.e. PABA-peptide, rat, human, arylamidolysis Homo sapiens N-Benzoyl-L-tyrosine + 4-aminobenzoate
-
 ?
3.4.24.18 N-Benzoyl-L-tyrosyl-4-aminobenzoate + H2O i.e. PABA-peptide, rat, human, arylamidolysis Rattus norvegicus N-Benzoyl-L-tyrosine + 4-aminobenzoate
-
 ?
3.4.24.18 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 Mus musculus ?
-
 ?
3.4.24.18 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 Rattus norvegicus ?
-
 ?
3.4.24.18 Substance P + H2O
-
 Homo sapiens Hydrolyzed substance P
-
 ?
3.4.24.18 Substance P + H2O rat Rattus norvegicus Hydrolyzed substance P
-
 ?
3.4.24.18 [Met5]enkephalin-Arg6-Phe7 + H2O
-
 Mus musculus ?
-
 ?
3.4.24.18 [Met5]enkephalin-Arg6-Phe7 + H2O
-
 Homo sapiens ?
-
 ?
3.4.24.18 [Met5]enkephalin-Arg6-Phe7 + H2O
-
 Rattus norvegicus ?
-
 ?
3.4.24.63 azocasein + H2O poor substrate Mus musculus ?
-
 ?
3.4.24.63 azocasein + H2O poor substrate Homo sapiens ?
-
 ?
3.4.24.63 azocasein + H2O poor substrate Rattus norvegicus ?
-
 ?
3.4.24.63 azocasein + H2O mouse enzyme: poor substrate unless activated by trypsin treatment (i.e. latent azocaseinase activity) Mus musculus ?
-
 ?
3.4.24.63 Insulin B-chain + H2O 4 cleavage sites (2 major and 2 minor): His5-Leu6, Leu6-Cys(SO3-)7, Ala14-Leu15, Cys(SO3-)19-Gly20 Mus musculus ?
-
 ?
3.4.24.63 Insulin B-chain + H2O mouse enzyme Mus musculus ?
-
 ?
3.4.24.63 additional information no substrates are nitrobradykinin Mus musculus ?
-
 ?
3.4.24.63 additional information no substrates are nitrobradykinin Homo sapiens ?
-
 ?
3.4.24.63 additional information no substrates are nitrobradykinin Rattus norvegicus ?
-
 ?
3.4.24.63 additional information member of astacin family Mus musculus ?
-
 ?
3.4.24.63 additional information member of astacin family Homo sapiens ?
-
 ?
3.4.24.63 additional information member of astacin family Rattus norvegicus ?
-
 ?
3.4.24.63 N-Benzoyl-Tyr 4-aminobenzoate + H2O rat or human enzyme, cleaves arylamide bond Homo sapiens ?
-
 ?
3.4.24.63 N-Benzoyl-Tyr 4-aminobenzoate + H2O rat or human enzyme, cleaves arylamide bond Rattus norvegicus ?
-
 ?
3.4.24.63 Tyr-Leu-Val-Cys(SO3-)-Gly-Glu-Arg-Gly + H2O synthetic octapeptide, derived from insulin B-chain Mus musculus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.4.24.18 More the mouse enzyme is composed of disulfide linked dimers associating non-covalently to form tetramers and sometimes higher order oligomers Mus musculus
3.4.24.18 More the mouse enzyme is composed of disulfide linked dimers associating non-covalently to form tetramers and sometimes higher order oligomers Rattus norvegicus
3.4.24.18 oligomer x * 90000, mouse, SDS-PAGE, reducing conditions Mus musculus
3.4.24.18 oligomer x * 90000, mouse, SDS-PAGE, reducing conditions Rattus norvegicus
3.4.24.18 tetramer 4 * 85000, mouse Mus musculus
3.4.24.18 tetramer 4 * 85000, mouse Rattus norvegicus
3.4.24.18 tetramer in the presence of 2-mercaptoethanol Mus musculus
3.4.24.18 tetramer in the presence of 2-mercaptoethanol Rattus norvegicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.24.18 30
-
 assay at Mus musculus
3.4.24.18 30
-
 nitrobradykinin assay Mus musculus
3.4.24.18 37
-
 assay at Mus musculus
3.4.24.18 37
-
 assay at Homo sapiens
3.4.24.18 37
-
 assay at Rattus norvegicus
3.4.24.63 37
-
 assay at Mus musculus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.24.63 58
-
 t1/2: 2.5 min, less stable than meprin A Mus musculus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.24.18 1.1
-
 2-Aminobenzoyl-Arg-Gly-Pro-Phe-Ser-Pro-(4-nitro)Phe-Arg
-
 Mus musculus
3.4.24.18 2.4
-
 2-Aminobenzoyl-Arg-Pro-Gly-Lys-Ser-Pro-(4-nitro)Phe-Arg
-
 Mus musculus
3.4.24.18 4.9
-
 2-Aminobenzoyl-Arg-Pro-Gly-Glu-Ser-Pro-(4-nitro)Phe-Arg
-
 Mus musculus
3.4.24.18 5
-
 Arg-Pro-Pro-Gly-(4-nitro)Phe-Lys-Pro-Phe-Arg
-
 Mus musculus
3.4.24.18 7.6
-
 Arg-Pro-Pro-Gly-(4-nitro)Phe-Phe-Pro-Phe-Arg
-
 Mus musculus
3.4.24.18 12
-
 2-Aminobenzoyl-Arg-Pro-Gly-Leu-Ser-Pro-(4-nitro)Phe-Arg
-
 Mus musculus
3.4.24.18 19.6
-
 Arg-Pro-Pro-Gly-(4-nitro)Phe-Arg-Pro-Phe-Arg
-
 Mus musculus
3.4.24.18 26.7
-
 2-Aminobenzoyl-Arg-Hyp-Gly-Phe-Ser-Pro-(4-nitro)Phe-Arg
-
 Mus musculus
3.4.24.18 40.9
-
 Arg-Pro-Pro-Gly-(4-nitro)Phe-Ser-Pro-Phe-Arg
-
 Mus musculus
3.4.24.18 51.5
-
 Arg-Pro-Pro-Gly-(4-nitro)Phe-Ala-Pro-Phe-Arg
-
 Mus musculus
3.4.24.18 98.5
-
 2-Aminobenzoyl-Arg-Pro-Gly-Ala-Ser-Pro-(4-nitro)Phe-Arg
-
 Mus musculus
3.4.24.18 133
-
 2-Aminobenzoyl-Arg-Pro-Ile-Phe-Ser-Pro-(4-nitro)Phe-Arg
-
 Mus musculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.24.18 additional information
-
 pI: multiple bonds in the range of 4-5, presumably due to glycosylation Mus musculus
3.4.24.18 additional information
-
 pI: multiple bonds in the range of 4-5, presumably due to glycosylation Homo sapiens
3.4.24.18 additional information
-
 pI: multiple bonds in the range of 4-5, presumably due to glycosylation Rattus norvegicus