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. Author manuscript; available in PMC: 2010 Sep 2.
Published in final edited form as: Chem Biol. 2009 Jun 26;16(6):667–675. doi: 10.1016/j.chembiol.2009.04.011

Table 1.

Catalytic Properties wild-type MT Enzyme and Mutants

Enzyme Mutation Malonyl CoA Acetyl CoA
KM (µM) kcat (min−1) kcat/ KM KM (µM) kcat (min−1) kcat/ KM
MTa WT 3.1 ± 0.6 65.1 ± 6.1 21 - 0 -
R142Q 38.6 ±9.6 0.13 ± 0.01 0.003 9.1 ± 1.25 0.37 ± 0.03 0.04
R142G 71.2 ± 21 0.17 ± 0.02 0.0023 32.2 ± 6.9 0.40 ± 0.05 0.012
R142A 1060 ± 99 0.37 ± 0.02 0.00035 32.9 ± 5.7 0.29 ± 0.04 0.009

MATb WT 1.9 ± 0.23 72 ± 0.5 37.9 3.9 ± 0.4± 114 ± 3.6 29.2
R606A 16.2 ±2.4 0.6 ± 0.048 0.037 1.8 ± 0.28 852 ±12 473
a

Assayed at 20 °C.

b

Assayed on the rat enzyme at 0 °C; data from {Rangan, 1997 #7104}.