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\section{Computational Methodology}  Five systems are investigated: L-aspartate $\alpha$-decarboxylase (AspDC), 4-oxalocrotonate tautomerase (4-OT), phosphotriesterase (PTE), histone lysine methyltransferase (HKMT), and haloalcohol dehalogenase (HheC).  The B3LYP/6-311+G(2d,2p)//B3LYP/6-31G(d,p) (LANL2DZ is used for Zn in 1HZY)  barrier heights and reaction energies are taken from the literature \cite{Chen_2007,Georgieva_2010,Hopmann_2008,Liao_2011,Sevastik_2007} (LANL2DZ is used for Zn in 1HZY) literature: AspDC \cite{Liao_2008}, 4-OT \cite{Sevastik_2007}, PTE \cite{Chen_2007}, HKMT \cite{Georgieva_2010}, and HhecC \cite{Hopmann_2008}  and the corresponding atomic coordinates are taken from the supplementary information or supplied by Fahmi Himo. The largest model system for each study is used unless otherwise noted and PCM results for for a dielectric constant of 80. The PM6 \cite{Stewart_2007} and PM7 single point calculations are performed using MOPAC2012 while theDFTB2 (xx) and  DFTB3 (xx) single point calculations are performed using GAMESS-US \cite{Schmidt_1993,Nishimoto_2015}. For PM6/COSMO \cite{Klamt_1993} and DFTB/PCM (xx) calculations are performed using a dielectric constant of 80. The B3LYP results include zero-point energy corrections.