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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