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. Author manuscript; available in PMC: 2009 Dec 23.
Published in final edited form as: ACS Nano. 2008 Dec 23;2(12):2519–2525. doi: 10.1021/nn800577h

Table 1.

Comparison of steady-state kinetic parameters of hydrolysis of a fluorogenic substrate, tryptamine adenosine phosphoramidate (TpAd) monoester by DHFR-hHint1 fusion proteins with different length of peptide linkers. Data was obtained at 25 °C in HEPES buffer (20 mM HEPES pH 7.2, 1 mM MgCl2) as previously described a.10

Protein kcat
(s−1)		 Km
(nM)		 kcat/Km
(s−1M−1)×10−7
hHint1* 2.1 ± 0.1 130 ± 20 1.5 ± 0.3
1DHG 2.1 ± 0.02 69 ± 5 3.1 ± 0.4
1DHT 2.1 ± 0.01 93 ± 10 2.3 ± 0.6
3DH-GLG 2.9 ± 0.09 150 ± 20 2.0 ± 0.5
3DH-GLE 0.73 ± 0.01 28 ± 1 2.6 ± 0.2
7DH 3.2 ± 0.01 130 ± 10 2.4 ± 0.1
15DH 3.3 ± 0.01 120 ± 10 2.7 ± 0.2
a

Measurements were carried out in duplicate and variants are given as standard deviations.

*

Data for hHint1 were adapted from ref 10.