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Literature summary for 3.4.14.4 extracted from

  • Hirose, J.; Hata, T.; Kawaoka, C.; Ikeura, T.; Kitahara, S.; Horii, K.; Tomida, H.; Iwamoto, H.; Ono, Y.; Fukasawa, K.M.
    Flexibility of the coordination geometry around the cupric ions in Cu(II)-rat dipeptidyl peptidase III is important for the expression of enzyme activity (2012), Arch. Biochem. Biophys., 525, 71-81.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
Leu453del activity of mutant Cu(II)-del-DPP III, in which Leu453 is deleted from the metal-binding motif, is only 1-2% of the enzyme activity of del-DPP. The EPR spectra of Cu(II) del-DPP III do not change in the presence of excess Lys-Ala-beta-naphthylamide. The deletion of Leu453 from the HELLGH motif of rat DPP III leads to a complete loss of flexibility in the ligand geometry around the cupric ions Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.07
-
L-Lys-L-Ala-2-naphthylamide wild-type in presence of Cu2+, pH 7.4, 25°C Rattus norvegicus
0.12
-
L-Lys-L-Ala-2-naphthylamide wild-type, pH 7.4, 25°C Rattus norvegicus
0.2
-
L-Lys-L-Ala-2-naphthylamide mutant Leu453del, pH 7.4, 25°C Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ activity of the cupric derivative for Lys-Ala-beta-naphthylamide is about 30% of that of the wild-type zinc enzyme. The enzyme activity of mutant Cu(II)-del-DPP III, in which Leu453 is deleted from the metal-binding motif, is only 1-2% of the enzyme activity of del-DPP III. The EPR spectra of Cu(II) del-DPP III do not change in the presence of excess Lys-Ala-beta-naphthylamide. The deletion of Leu453 from the HELLGH motif of rat DPP III leads to a complete loss of flexibility in the ligand geometry around the cupric ions Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Lys-L-Ala-2-naphthylamide + H2O activity of the cupric derivative for Lys-Ala-beta-naphthylamide is about 30% of that of the wild-type enzyme Rattus norvegicus L-Lys-L-Ala + 2-naphthylamine
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.4
-
L-Lys-L-Ala-2-naphthylamide wild-type in presence of Cu2+, pH 7.4, 25°C Rattus norvegicus
1.1
-
L-Lys-L-Ala-2-naphthylamide mutant Leu453del, pH 7.4, 25°C Rattus norvegicus
1.4
-
L-Lys-L-Ala-2-naphthylamide wild-type, pH 7.4, 25°C Rattus norvegicus

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
5.5
-
L-Lys-L-Ala-2-naphthylamide mutant Leu453del, pH 7.4, 25°C Rattus norvegicus
5.7
-
L-Lys-L-Ala-2-naphthylamide wild-type in presence of Cu2+, pH 7.4, 25°C Rattus norvegicus
12
-
L-Lys-L-Ala-2-naphthylamide wild-type, pH 7.4, 25°C Rattus norvegicus