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Literature summary for 3.4.21.93 extracted from

  • Rabah, N.; Gauthier, D.; Wilkes, B.C.; Gauthier, D.J.; Lazure, C.
    Single amino acid substitution in the PC1/3 propeptide can induce significant modifications of its inhibitory profile toward its cognate enzyme (2006), J. Biol. Chem., 281, 7556-7567.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D65A site-directed mutagenesis of the propeptide residue, leads to reduced inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide Mus musculus
D66A site-directed mutagenesis of the propeptide residue, leads to reduced inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide Mus musculus
D67A site-directed mutagenesis of the propeptide residue, leads to increased inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide Mus musculus
K61A site-directed mutagenesis of the propeptide residue, leads to reduced inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide Mus musculus
additional information single amino acid substitution in the PC1/3 propeptide can induce significant modifications of its inhibitory profile toward its cognate enzyme Mus musculus
R50A site-directed mutagenesis of the propeptide residue, leads to increased inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide Mus musculus
R51A site-directed mutagenesis of the propeptide residue, leads to increased inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide Mus musculus
R53A site-directed mutagenesis of the propeptide residue, leads to reduced inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide Mus musculus
R54A site-directed mutagenesis of the propeptide residue, leads to increased inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide Mus musculus
R62A site-directed mutagenesis of the propeptide residue, leads to reduced inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide Mus musculus
S52A site-directed mutagenesis of the propeptide residue, unaltered inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide Mus musculus
S52A/R53A site-directed mutagenesis of the propeptide residues, leads to increased inhibition of mature PC1 by the separated propeptide mutant compared to the wild-type propeptide Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
PC1/3 propeptide inhibits the mature enzyme competitively, inhibition mechanism, interaction with the enzyme at the 50RRSRR54, 61KR62 and 65DDD67 sequences, molecular modeling, overview Mus musculus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+
-
Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus P63239
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pGlu-Arg-Thr-Lys-Arg-7-amido-4-methylcoumarin + H2O
-
Mus musculus pGlu-Arg-Thr-Lys-Arg + 7-amino-4-methylcoumarin
-
?

Synonyms

Synonyms Comment Organism
PC1/3
-
Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at room temperature Mus musculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
assay at Mus musculus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00000015
-
mutant D67A propeptide pH 6.0, 22°C Mus musculus
0.0000002
-
mutant R54A propeptide pH 6.0, 22°C Mus musculus
0.00000036
-
mutant R50A propeptide pH 6.0, 22°C Mus musculus
0.00000074
-
mutant R51A propeptide pH 6.0, 22°C Mus musculus
0.000004
-
mutant R52A propeptide pH 6.0, 22°C Mus musculus
0.0000044
-
wild-type propeptide pH 6.0, 22°C Mus musculus
0.0000054
-
mutant R53A propeptide pH 6.0, 22°C Mus musculus
0.0000086
-
mutant D66A propeptide pH 6.0, 22°C Mus musculus
0.00001
-
mutant K61A propeptide pH 6.0, 22°C Mus musculus
0.00001
-
mutant D65A propeptide pH 6.0, 22°C Mus musculus
0.0000165
-
mutant R62A propeptide pH 6.0, 22°C Mus musculus