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. Author manuscript; available in PMC: 2017 Dec 1.
Published in final edited form as: Biochim Biophys Acta. 2016 Sep 14;1864(12):1732–1738. doi: 10.1016/j.bbapap.2016.09.005

Table 2.

Kinetic data for the four hybrid enzymes

dF393A-1 dF393W-1 sL407C-1 dQ403W-1
reduction rate (kET)
SFb n.d.a 1.20x105 ± 0.06 s−1 1.49x105 ± 0.02 s−1 2.02x105 ± 0.01s−1
SB 1.04x105 ± 0.02 s−1 6.25x104 ± 0.01 s−1 7.32x104 ± 0.04 s−1 1.45x105 ± 0.02s−1
kcat (eq.min−1), < 2 21 36c 44
Km (μM) 11.3 5.0 11.0c 9.5
TTNd <5 192 230 420
a

could not be determined as the SF-dF393A-1 was unstable under the laser experiments leading to the SB-F393A-1 species;

b

SF: Substrate free and N-palmitoylglycine bound (SB);

c

value determined previously[15]

d

TTN: total turnover numbers as nmol of products / nmol of enzymes at the end of the reaction.