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Literature summary for 3.4.21.118 extracted from

  • Shimizu, C.; Yoshida, S.; Shibata, M.; Kato, K.; Momota, Y.; Matsumoto, K.; Shiosaka, T.; Midorikawa, R.; Kamachi, T.; Kawabe, A.; Shiosaka, S.
    Characterization of recombinant and brain neuropsin, a plasticity-related serine protease (1998), J. Biol. Chem., 273, 11189-11196.
    View publication on PubMed
Search for more literature for 3.4.21.118

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of proneuropsin in Spodoptera frugiperda insect cells via baculovirus infection Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
(4-amidinohenyl)methanesulfonyl 1-fluoride 61% inhibition at 1 mM Mus musculus
antipain 95% inhibition at 0.1 mM Mus musculus
Aprotinin 65% inhibition at 0.1 mM Mus musculus
benzamidine 56% inhibition at 1 mM Mus musculus
chymostatin 80% inhibition at 0.1 mM Mus musculus
diisopropylfluorophosphate 16% inhibition at 0.1 mM Mus musculus
human alpha1-antichymotrypsin weak, 16% inhibition at 2 mM Mus musculus
human alpha1-antitrypsin weak, 20% inhibition at 10 mM Mus musculus
leupeptin complete inhibition at 0.1 mM Mus musculus
additional information enzyme is strongly inhibited by low molecular weight protease inhibitors that bind to His and Ser residues in the active center of serine proteases; no or very slight inhibition by pepstatin A, trypsin inhibitor, Ca2+, Mg2+, and metal chelators Mus musculus
trans-epoxysuccinyl-L-leucylamido(4-guanidinobutane) i.e. E-64, 15% inhibition at 0.1 mM Mus musculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.23
-
 D-Val-Leu-Arg-4-nitroanilide recombinant enzyme, pH 8.0, 37°C Mus musculus
0.27
-
 tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide recombinant enzyme, pH 8.0, 37°C Mus musculus
0.28
-
 D-Val-Leu-Arg-4-nitroanilide native enzyme, pH 8.0, 37°C Mus musculus
0.3
-
 tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide native enzyme, pH 8.0, 37°C Mus musculus
0.34
-
 tert-butyloxycarbonyl-Asp-Pro-Arg-4-methylcoumaryl-7-amide recombinant enzyme, pH 8.0, 37°C Mus musculus
0.5
-
 tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide recombinant enzyme, pH 8.0, 37°C Mus musculus
0.54
-
 tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide native enzyme, pH 8.0, 37°C Mus musculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
26000
-
 1 * 26000, non-reducing SDS-PAGE Mus musculus
26600
-
 recombinant enzyme, MALDI-TOF MS Mus musculus
29000
-
 recombinant enzyme, gel filtration Mus musculus
32000
-
 1 * 32000, reducing SDS-PAGE Mus musculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
polypeptide + H2O Mus musculus enzyme has significant limbic effects by changing the extracellular matrix environment peptides
-
 ?
polypeptide + H2O Mus musculus involvement in neural plasticity peptides
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus Q61955 adult balb/c mice
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification recombinant enzyme is produced as inactive proform and needs to be processed by an endoprotease, e.g. protease-1, EC 3.4.21.50, or trypsin, EC 3.4.21.4, for activation by specific cleavage of the Lys32-Ile33 bond near the N-terminus Mus musculus

Purification (Commentary)

Purification (Comment) Organism
1100fold from brain Mus musculus
recombinant from SF21 insect cells Mus musculus

Reaction

Reaction Comment Organism Reaction ID
cleavage of amide substrates following the basic amino acids Arg or Lys at the P1 position, with a preference for Arg over Lys enzyme is a trypsin-type serine protease Mus musculus
a

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Mus musculus
-
hippocampus
-
 Mus musculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.23
-
 purified native enzyme, substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide Mus musculus
6.26
-
 purified recombinant enzyme, substrate tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-Pro-Phe-Arg-4-nitroanilide + H2O low activity Mus musculus acetyl-Pro-Phe-Arg + 4-nitroaniline
-
 ?
acetyl-Pro-Phe-Arg-4-nitroanilide + H2O recombinant, not native enzyme Mus musculus acetyl-Pro-Phe-Arg + 4-nitroaniline
-
 ?
D-Val-Leu-Arg-4-nitroanilide + H2O native and recombinant enzyme Mus musculus D-Val-Leu-Arg + 4-nitroaniline
-
 ?
D-Val-Leu-Lys-4-nitroanilide + H2O native and recombinant enzyme Mus musculus D-Val-Leu-Lys + 4-nitroaniline
-
 ?
Fibronectin + H2O recombinant enzyme Mus musculus ?
-
 ?
additional information recombinant enzyme is produced as inactive proform and needs to be processed by an endoprotease, e.g. protease-1, EC 3.4.21.50, or trypsin, EC 3.4.21.4, for activation by specific cleavage of the Lys32-Ile33 bond near the N-terminus Mus musculus ?
-
 ?
additional information substrate specificty of native and recombinant enzyme Mus musculus ?
-
 ?
polypeptide + H2O
-
 Mus musculus peptides
-
 ?
polypeptide + H2O enzyme has significant limbic effects by changing the extracellular matrix environment Mus musculus peptides
-
 ?
polypeptide + H2O involvement in neural plasticity Mus musculus peptides
-
 ?
tert-butyloxycarbonyl-Ala-Gly-Pro-Arg-4-methylcoumaryl-7-amide + H2O recombinant, not native, enzyme Mus musculus tert-butyloxycarbonyl-Ala-Gly-Pro-Arg + 7-amino-4-methylcoumarin
-
 ?
tert-butyloxycarbonyl-Asp-Pro-Arg-4-methylcoumaryl-7-amide + H2O recombinant, not native, enzyme Mus musculus tert-butyloxycarbonyl-Asp-Pro-Arg + 7-amino-4-methylcoumarin
-
 ?
tert-butyloxycarbonyl-Glu-Gly-Arg-4-methylcoumaryl-7-amide + H2O native and recombinant enzyme Mus musculus tert-butyloxycarbonyl-Glu-Gly-Arg + 7-amino-4-methylcoumarin
-
 ?
tert-butyloxycarbonyl-Glu-Gly-Arg-4-methylcoumaryl-7-amide + H2O recombinant, not native, enzyme Mus musculus tert-butyloxycarbonyl-Glu-Gly-Arg + 7-amino-4-methylcoumarin
-
 ?
tert-butyloxycarbonyl-Glu-Lys-Lys-4-methylcoumaryl-7-amide + H2O low activity Mus musculus tert-butyloxycarbonyl-Glu-Lys-Lys + 7-amino-4-methylcoumarin
-
 ?
tert-butyloxycarbonyl-Glu-Lys-Lys-4-methylcoumaryl-7-amide + H2O recombinant and native enzyme Mus musculus tert-butyloxycarbonyl-Glu-Lys-Lys + 7-amino-4-methylcoumarin
-
 ?
tert-butyloxycarbonyl-Leu-Arg-Arg-4-methylcoumaryl-7-amide + H2O low activity Mus musculus tert-butyloxycarbonyl-Leu-Arg-Arg + 7-amino-4-methylcoumarin
-
 ?
tert-butyloxycarbonyl-Leu-Arg-Arg-4-methylcoumaryl-7-amide + H2O recombinant, not native, enzyme Mus musculus tert-butyloxycarbonyl-Leu-Arg-Arg + 7-amino-4-methylcoumarin
-
 ?
tert-butyloxycarbonyl-Leu-Thr-Arg-4-methylcoumaryl-7-amide + H2O low activity Mus musculus tert-butyloxycarbonyl-Leu-Thr-Arg + 7-amino-4-methylcoumarin
-
 ?
tert-butyloxycarbonyl-Leu-Thr-Arg-4-methylcoumaryl-7-amide + H2O recombinant, not native, enzyme Mus musculus tert-butyloxycarbonyl-Leu-Thr-Arg + 7-amino-4-methylcoumarin
-
 ?
tert-butyloxycarbonyl-Phe-Ser-Arg-4-methylcoumaryl-7-amide + H2O native and recombinant enzyme Mus musculus tert-butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
-
 ?
tert-butyloxycarbonyl-pyroglutamyl-Gly-Arg-4-methylcoumaryl-7-amide + H2O recombinant and native enzyme Mus musculus tert-butyloxycarbonyl-pyroglutamyl-Gly-Arg + 7-amino-4-methylcoumarin
-
 ?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O best substrate Mus musculus tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
 ?
tert-butyloxycarbonyl-Val-Pro-Arg-4-methylcoumaryl-7-amide + H2O native and recombinant enzyme Mus musculus tert-butyloxycarbonyl-Val-Pro-Arg + 7-amino-4-methylcoumarin
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 26000, non-reducing SDS-PAGE Mus musculus
monomer 1 * 32000, reducing SDS-PAGE Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 recombinant enzyme Mus musculus