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. Author manuscript; available in PMC: 2014 Jun 13.
Published in final edited form as: Science. 2013 Sep 6;341(6150):1089–1094. doi: 10.1126/science.1242345

Fig. 2.

Fig. 2

Enzymatic production of activated extender units for C–C bond formation reactions. (A) Formation of malonyl-CoA (left) and fluoromalonyl-CoA (right) from 500 μM CoA and either acetate or fluoroacetate, respectively (AckA, acetate kinase; Pta, phosphotransacetylase; ACCase, acetyl-CoA carboxylase). Values are reported as the mean ± s.d. (n = 3). (B) Kinetic parameters for malonate activation (MatB, malonyl-CoA synthetase). Kinetic parameters are reported as mean ± s.e. (n = 3) as determined from non-linear curve-fitting. Error in the kcat/KM parameter was obtained from propagation of error from the individual kinetic terms.