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. Author manuscript; available in PMC: 2009 Jun 11.
Published in final edited form as: J Biol Chem. 2007 Aug 22;282(43):31744–31754. doi: 10.1074/jbc.M703378200

TABLE 2. Comparison of kinetic constants for EAH mutants to those for HPO.

Constants were calculated by nonlinear regression fits to the Michaelis-Menten equation.

Enzyme Substrate Product Km kcat kcat/Km
µm S−1
HPOa PSD Solavetivol 14.0 ± 1.9 2.1 ± 0.10 0.15
EAH PSD Solavetivol 9.2 ± 1.1 0.4 ± 0.02 0.04
EAH, S368V PSD Solavetivol 11.4 ± 1.2 0.6 ± 0.02 0.05
EAH, S368V/I484V PSD Solavetivol 7.6 ± 1.2 0.4 ± 0.02 0.05
EAH, S368V/S482V PSD Solavetivol 6.5 ± 1.2 0.6 ± 0.03 0.09
a

Data are from Table I; PSD, premnaspirodiene; EA, 5-epi-aristolochene.