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Literature summary for 3.4.23.25 extracted from

  • Winterburn, T.J.; Wyatt, D.M.; Phylip, L.H.; Bur, D.; Harrison, R.J.; Berry, C.; Kay, J.
    Key features determining the specificity of aspartic proteinase inhibition by the helix-forming IA3 polypeptide (2007), J. Biol. Chem., 282, 6508-6516.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
A213I increased Km and 50% higher turnover than wild type enzyme Saccharomyces cerevisiae
T222A 50% of wild type turnover Saccharomyces cerevisiae
T287A/P288G 50% of wild type turnover Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
IA3 highly specific polypeptide inhibitor synthesized by Saccharomyces cerevisiae, a hydrogen bond network also residues K18 and D22 of the inhibitor directly to the catalytic Asp-32 and Tyr-75 residues of the enzyme, thus deadlocking the inhibitor in position, numerous mutants of IA3 created and tested for inhibition, all mutants are found to be inhibitory although to different extent, variations within residues 2-32 at positions other than 18 and 22 appears to have relatively minor effects Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.1
-
Lys-Pro-Ile-Glu-Phe-L-nitrophenylalanine-Arg-Leu T222A mutant, pH 4.7 Saccharomyces cerevisiae
0.12
-
Lys-Pro-Ile-Glu-Phe-L-nitrophenylalanine-Arg-Leu T287A/P288G mutant, pH 4.7 Saccharomyces cerevisiae
0.14
-
Lys-Pro-Ile-Glu-Phe-L-nitrophenylalanine-Arg-Leu wild type enzyme, pH 4.7 Saccharomyces cerevisiae
0.25
-
Lys-Pro-Ile-Glu-Phe-L-nitrophenylalanine-Arg-Leu A213I mutant, pH 4.7 Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-/-Val-Tyr bond in a synthetic substrate. Does not act on esters of Tyr or Arg Asp-32 and Tyr-75 residues involved in catalysis Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Lys-Pro-Ile-Glu-Phe-L-nitrophenylalanine-Arg-Leu + H2O
-
Saccharomyces cerevisiae Lys-Pro-Ile-Glu-Phe + L-nitrophenylalanine-Arg-Leu
-
?

Synonyms

Synonyms Comment Organism
Proteinase A use of recommended name should be favored Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
21
-
Lys-Pro-Ile-Glu-Phe-L-nitrophenylalanine-Arg-Leu T222A mutant, pH 4.7 Saccharomyces cerevisiae
21
-
Lys-Pro-Ile-Glu-Phe-L-nitrophenylalanine-Arg-Leu T287A/P288G mutant, pH 4.7 Saccharomyces cerevisiae
44
-
Lys-Pro-Ile-Glu-Phe-L-nitrophenylalanine-Arg-Leu wild type enzyme, pH 4.7 Saccharomyces cerevisiae
66
-
Lys-Pro-Ile-Glu-Phe-L-nitrophenylalanine-Arg-Leu A213I mutant, pH 4.7 Saccharomyces cerevisiae

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
additional information
-
below 0.1 nM, exact detection impossible Saccharomyces cerevisiae IA3