Skip to main content

Table 2 Michaelis–Menten constant, Km (μM), and specificity constant, kcat/Km (M−1 s−1) of dUTPases from different origins

From: Enzyme kinetics of dUTPase from the planarian Dugesia ryukyuensis

Substrate

D. ryukyuensis

H. sapiens

S. cerevisiae

E. coli

P. falciparum

dUTP

4.0 (8.5 × 106)

1.1 (6.6 × 106)

1.3 × 102 (7.4 × 105)

0.2 (3.6 × 106)

1.9 (7.1 × 106)

dATP

9.4 × 10 (1.6 × 104)

NR

NR

NR

1.1 × 103 (2.7)

dTTP

1.1 × 102 (1.3 × 104)

7.6 × 102 (2.0 × 10)

NR

> 2.0 × 104 (< 0.1 × 103)

2.9 × 102 (9.2)

dCTP

7.7 × 10 (2.1 × 104)

6.9 × 102 (1.6 × 102)

NR

4.0 × 103 (0.1 × 103)

4.7 × 102 (2.2 × 10)

dGTP

2.1 × 102 (1.4 × 104)

NR

NR

NR

2.0 × 103 (1.3 × 10−1)

Sources

This study

[21]

[28]

[20]

[21]

  1. In dUTPase from E. coli, the Km for dTTP and dCTP were presented congruent to Kd
  2. NR not reported