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Literature summary for 3.4.21.94 extracted from

  • Kacprzak, M.M.; Than, M.E.; Juliano, L.; Juliano, M.A.; Bode, W.; Lindberg, I.
    Mutations of the PC2 substrate binding pocket alter enzyme specificity (2005), J. Biol. Chem., 280, 31850-31858.
    View publication on PubMed
Search for more literature for 3.4.21.94

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant PC2 in CHO-K1 cells Mus musculus

Protein Variants

Protein Variants Comment Organism
A322T/S323N site-directed mutagenesis, the mutant shows unaltered activity, but slightly decreased sensitivity for inhibitor 7B2 CT peptide compared to the wild-type enzyme Mus musculus
D278E site-directed mutagenesis of the S4/S5 subsite residue, the mutant shows altered substrate preferences, increased activity and reduced sensitivity to inhibitor 7B2 CT peptide compared to the wild-type enzyme Mus musculus
L341W site-directed mutagenesis of the residue from the far edge of subsite S2', the mutant shows increased activity, and slightly decreased sensitivity for inhibitor 7B2 CT peptide compared to the wild-type enzyme Mus musculus
N356S site-directed mutagenesis of the distant prime site residue, the mutant shows altered substrate preferences compared to the wild-type enzyme Mus musculus
R281G/E282R site-directed mutagenesis of the S6 edge residue R281, the mutant shows largely altered substrate preferences and reduced activity compared to the wild-type enzyme Mus musculus
S206K site-directed mutagenesis of the S1' subsite residue, inactive mutant Mus musculus
S206R site-directed mutagenesis of the S1' subsite residue, inactive mutant Mus musculus
S380T site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Mus musculus
T271E site-directed mutagenesis of the residue separating the subsites S3 and S5, the mutant shows increased activity compared to the wild-type enzyme Mus musculus
T271N site-directed mutagenesis of the residue separating the subsites S3 and S5, the mutant shows unaltered activity, but slightly decreased sensitivity for inhibitor 7B2 CT peptide compared to the wild-type enzyme Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
7B2 CT peptide potent specific inhibition of PC2 Mus musculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics of wild-type and mutant enzymes Mus musculus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ dependent on Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant PC2 from CHO-K1 cells by adsorption chromatography Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
peptide B-derived peptides + H2O cleavage site specificity of wild-type and mutant PC2, overview Mus musculus ?
-
 ?
proenkphalin-derived peptide + H2O the preferred cleavage site sequence of PC2 is YGGFLKR-/-FAESL Mus musculus ?
-
 ?

Synonyms

Synonyms Comment Organism
More the enzyme belongs to the proprotein protease family of mammalian calcium-dependent serine proteases Mus musculus
PC2
-
 Mus musculus
prohormone convertase
-
 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
additional information
-
 pH optima of mutant enzymes, overview Mus musculus
5
-
 wild-type enzyme Mus musculus

pH Range

pH Minimum pH Maximum Comment Organism
4.5 6 pH profiles of wild-type and mutant enzymes, overview Mus musculus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
 additional information inhibition kinetics of wild-type and mutant enzymes Mus musculus