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. Author manuscript; available in PMC: 2013 Dec 9.
Published in final edited form as: Biochemistry. 2010 Jan 12;49(1):10.1021/bi9017957. doi: 10.1021/bi9017957

Table 2.

Apparent kinetic constants with alternate substrates. a

Enzyme Substrate kcat (s−1) Km (µM) kcat/Km (M−1 s−1) Relative kcat/Km (%)
MTH IPK IPb 27.5 ± 0.3 12.7 ± 0.6 2.2 × 106 100
ISP 8.22 ± 0.09 23.7 ± 0.8 3.5 × 105 16
DMAP 34.0 ± 0.3 43.2 ± 1.0 7.9 × 105 36
BP 31.8 ± 0.7 263 ± 18 1.2 × 105 5.5
BEP 20.5 ± 0.3 297 ± 12 6.9 × 104 3.1
GP 0.0142 ± 0.0002 740 ± 43 19 0.00086
THA IPK IPb 8.0 ± 0.2 4.4 ± 0.5 1.8 × 106 100
ISP 2.84 ± 0.06 14.5 ± 1.2 2.0 × 105 11
DMAP 11.3 ± 0.4 174 ± 18 6.5 × 104 3.6
BP 9.9 ± 0.1 173 ± 7 5.7 × 104 3.2
BEP 8.07 ± 0.09 103 ± 5 7.8 × 104 4.3
GPc 0.047 ± 0.008 4700 ± 1300 10 0.00055
a

Apparent kinetic constants determined at ATP = 200 µM.

b

Data from reference (the characterization paper).

c

The highest GP concentration used was 4.5 mM.