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Literature summary for 3.4.11.9 extracted from

  • Jao, S.C.; Huang, L.F.; Hwang, S.M.; Li, W.S.
    Tyrosine 387 and arginine 404 are critical in the hydrolytic mechanism of Escherichia coli aminopeptidase P (2006), Biochemistry, 45, 1547-1553.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
R153A enzymic activity similar to wild-type Escherichia coli
R153L enzymic activity similar to wild-type Escherichia coli
R153L/R370L decrease in Km-value Escherichia coli
R153W enzymic activity similar to wild-type Escherichia coli
R153W/R370L decrease in Km-value Escherichia coli
R370L enzymic activity similar to wild-type Escherichia coli
R404A decrease both in KM- and kcat-value Escherichia coli
R404K decrease in kcat-value Escherichia coli
W88L enzymic activity similar to wild-type Escherichia coli
Y387F decrease in kcat-value Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.047
-
bradykinin mutant R404A, pH 7.5, 37°C Escherichia coli
0.16
-
bradykinin mutant R153W/R370L, pH 7.5, 37°C Escherichia coli
0.18
-
bradykinin mutant R153L/R370L, pH 7.5, 37°C Escherichia coli
0.21
-
bradykinin mutant R370L, pH 7.5, 37°C Escherichia coli
0.41
-
bradykinin mutant R404K, pH 7.5, 37°C Escherichia coli
0.42
-
bradykinin mutant R153A, pH 7.5, 37°C Escherichia coli
0.43
-
bradykinin mutant R153W, pH 7.5, 37°C Escherichia coli
0.51
-
bradykinin mutant R153L, pH 7.5, 37°C Escherichia coli
0.78
-
bradykinin wild-type, pH 7.5, 37°C Escherichia coli
0.84
-
bradykinin mutant Y387F, pH 7.5, 37°C Escherichia coli
1.02
-
bradykinin mutant W88L, pH 7.5, 37°C Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ wild-type and mutat R404A, binding of Mn2+ with a stoichiometry of 2 per monomer Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide R404 participates in proton relay and in the hydrogen bond network Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.17
-
mutant R404A, pH 7.5, 37°C Escherichia coli
0.95
-
mutant R404A, presence of guanidine, pH 7.5, 37°C Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
bradykinin + H2O
-
Escherichia coli des-Arg-bradykinin + L-Arg
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.17
-
bradykinin mutant R404A, pH 7.5, 37°C Escherichia coli
0.24
-
bradykinin mutant R404K, pH 7.5, 37°C Escherichia coli
4.2
-
bradykinin mutant Y387F, pH 7.5, 37°C Escherichia coli
13.8
-
bradykinin mutant W88L, pH 7.5, 37°C Escherichia coli
57
-
bradykinin mutant R153L/R370L, pH 7.5, 37°C Escherichia coli
69
-
bradykinin wild-type, pH 7.5, 37°C Escherichia coli
70
-
bradykinin mutant R153W, pH 7.5, 37°C Escherichia coli
72
-
bradykinin mutant R153A, pH 7.5, 37°C Escherichia coli
87
-
bradykinin mutant R153W/R370L, pH 7.5, 37°C Escherichia coli
102
-
bradykinin mutant R370L, pH 7.5, 37°C Escherichia coli
109
-
bradykinin mutant R153L, pH 7.5, 37°C Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
wild-type and mutant R404A Escherichia coli