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Literature summary for 3.4.24.18 extracted from

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

Cloned(Commentary)

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

Inhibitors

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

KM Value [mM]

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

Localization

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
PPH
-
Homo sapiens PPH
-
PPH
-
Mus musculus
-
random bred ICR and at least 35 inbred, recombinant and congenic strains
-
Rattus norvegicus
-
-
-

Posttranslational Modification

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

Purification (Commentary)

Purification (Comment) Organism
-
Mus musculus

Specific Activity [micromol/min/mg]

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

Storage Stability

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?
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
-
?
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
-
?
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
-
?
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 ?
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 ?
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
-
?
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 ?
-
?
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
-
?
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
-
?
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
-
?
angiotensin II + H2O cleavage site: Tyr-Ile Mus musculus Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
?
angiotensin II + H2O cleavage site: Tyr-Ile Homo sapiens Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
?
angiotensin II + H2O cleavage site: Tyr-Ile Rattus norvegicus Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
?
angiotensin II + H2O i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe Mus musculus Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
?
angiotensin II + H2O i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe Homo sapiens Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
?
angiotensin II + H2O i.e. Asp-Arg-Val-Tyr-Ile-His-Pro-Phe Rattus norvegicus Asp-Arg-Val-Tyr + Ile-His-Pro-Phe
-
?
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
-
?
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
-
?
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
-
?
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
-
?
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
-
?
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
-
?
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
-
?
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
-
?
azocasein + H2O excellent substrate for mouse, poorer substrate for rat and human enzymes Mus musculus fragments of azocasein
-
?
azocasein + H2O excellent substrate for mouse, poorer substrate for rat and human enzymes Homo sapiens fragments of azocasein
-
?
azocasein + H2O excellent substrate for mouse, poorer substrate for rat and human enzymes Rattus norvegicus fragments of azocasein
-
?
azocasein + H2O excellent substrate for mouse, poorer substrate for rat and human enzymes Homo sapiens PPH fragments of azocasein
-
?
Big endothelin I + H2O rat Rattus norvegicus ?
-
?
bradykinin + H2O
-
Mus musculus Arg-Pro-Pro-Gly + Phe-Ser-Pro-Phe-Arg
-
?
bradykinin + H2O
-
Homo sapiens Arg-Pro-Pro-Gly + Phe-Ser-Pro-Phe-Arg
-
?
bradykinin + H2O
-
Rattus norvegicus Arg-Pro-Pro-Gly + Phe-Ser-Pro-Phe-Arg
-
?
Endothelin I + H2O rat Rattus norvegicus ?
-
?
Gonadotropin + H2O mouse Mus musculus ?
-
?
Human alpha-atrial natiuretic peptide + H2O rat Rattus norvegicus ?
-
?
Human transforming growth factor + H2O rat Rattus norvegicus ?
-
?
Insulin B-chain + H2O prevalent cleavage sites are Gly20-Glu21, Phe24-Phe25 and Phe25-Tyr26 Mus musculus Hydrolyzed insulin B-chain
-
?
Insulin B-chain + H2O prevalent cleavage sites are Gly20-Glu21, Phe24-Phe25 and Phe25-Tyr26 Homo sapiens Hydrolyzed insulin B-chain
-
?
Insulin B-chain + H2O prevalent cleavage sites are Gly20-Glu21, Phe24-Phe25 and Phe25-Tyr26 Rattus norvegicus Hydrolyzed insulin B-chain
-
?
Insulin B-chain + H2O 10 cleavage sites Mus musculus Hydrolyzed insulin B-chain
-
?
Insulin B-chain + H2O 10 cleavage sites Homo sapiens Hydrolyzed insulin B-chain
-
?
Insulin B-chain + H2O 10 cleavage sites Rattus norvegicus Hydrolyzed insulin B-chain
-
?
Insulin B-chain + H2O 7 major and 3 minor sites Mus musculus Hydrolyzed insulin B-chain
-
?
Insulin B-chain + H2O 7 major and 3 minor sites Homo sapiens Hydrolyzed insulin B-chain
-
?
Insulin B-chain + H2O 7 major and 3 minor sites Rattus norvegicus Hydrolyzed insulin B-chain
-
?
Insulin B-chain + H2O oxidized form Mus musculus Hydrolyzed insulin B-chain
-
?
Insulin B-chain + H2O oxidized form Homo sapiens Hydrolyzed insulin B-chain
-
?
Insulin B-chain + H2O oxidized form Rattus norvegicus Hydrolyzed insulin B-chain
-
?
Insulin B-chain + H2O prevalent cleavage sites are Gly20-Glu21, Phe24-Phe25 and Phe25-Tyr26 Homo sapiens PPH Hydrolyzed insulin B-chain
-
?
Insulin B-chain + H2O 10 cleavage sites Homo sapiens PPH Hydrolyzed insulin B-chain
-
?
Insulin B-chain + H2O 7 major and 3 minor sites Homo sapiens PPH Hydrolyzed insulin B-chain
-
?
Insulin B-chain + H2O oxidized form Homo sapiens PPH Hydrolyzed insulin B-chain
-
?
N-Benzoyl-L-tyrosyl-4-aminobenzoate + H2O i.e. PABA-peptide, rat, human, arylamidolysis Homo sapiens N-Benzoyl-L-tyrosine + 4-aminobenzoate
-
?
N-Benzoyl-L-tyrosyl-4-aminobenzoate + H2O i.e. PABA-peptide, rat, human, arylamidolysis Rattus norvegicus N-Benzoyl-L-tyrosine + 4-aminobenzoate
-
?
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 ?
-
?
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 ?
-
?
Substance P + H2O
-
Homo sapiens Hydrolyzed substance P
-
?
Substance P + H2O rat Rattus norvegicus Hydrolyzed substance P
-
?
[Met5]enkephalin-Arg6-Phe7 + H2O
-
Mus musculus ?
-
?
[Met5]enkephalin-Arg6-Phe7 + H2O
-
Homo sapiens ?
-
?
[Met5]enkephalin-Arg6-Phe7 + H2O
-
Rattus norvegicus ?
-
?

Subunits

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

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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